1972 E.K.-Frey Medal, Gesellschaft für Chirurgie
1977 Otto-Warburg Medal, Gesellschaft für Biologische Chemie
1982 Emil von Behring Medal, Universität Marburg
1987 Keilin Medal, Biochemical Society, London
1987 Richard-Kuhn Medal, Gesellschaft Deutscher Chemiker
1988 Nobel Prize in Chemistry
1990 Kone Award, Association of Clinical Biochemists, United Kingdom
1991 Rudi Lemberg Travelling Fellowshipal Societies
1993 Bayerischer Maximiliansorden für Wissenschaft und Kunst
1993/94 The Linus Pauling Medal
1995 Miami Winter Symposia, The Distinguished Service Award
1997 Max Tishler Prize, Harvard University, USA
1997 Max-Bergmann-Medaille des Max-Bergmann-Kreises zur Förderung der peptidchemischen Forschung
1997 Das Grosse Verdienstkreuz mit Stern und Schulterband der Bundesrepublik Deutschland
2002 Honorary Professor, Ocean University, Qingdao
2003 Honorary Professor, Peking University, Peking
2003 Honorary Professor, Sichuan University, Chengdu
2004 Honorary Professor, Shanghai Second Medical University, Shanghai
2004 Röntgenplakette der Stadt Remscheid-Lennep
2004 Premio Città di Firenze sulle Scienze Molecolari, Florenz
2005 Honorary Professor, Shanghai Jiao Tong University, China
2005 ‘Lotte Distinguished Professorship’, Seoul National University, Korea
2006 Profesor Honorario de la Universidad de Sevilla
2009 Erice Prize- Premio Ettore Majorana
2009 Honorary Professor, Huaqiao University, Xiamen, China
2009 Honorary Director of the Nobel Life Science Research Center, Foshan, China
2010 Foreign Member of the Korean Academy of Science and Technology, Korea
2010 Dr. h.c. Universidad de Buenos Aires, Republica Argentina
1. Clausen, T., Kaiser, M., Huber, R. and Ehrmann, M. (2011). ”HTRA proteases: regulated proteolysis in protein quality control.” Nature Reviews Molecular Cell Biology 12,152-162.
2. Gräwert, M. A., Gallastegui, N., Stein, M., Schmidt, B., Kloetzel, P. M., Huber, R. and Groll, M. (2011). ”Elucidation of the a-keto-aldehyde binding mechanism: A lead structure motif for proteasome inhibition.” Angewandte Chemie Int. Ed. 50, 542-544.
3. Huber, R. (2010). ”Nobelpreisträger im Gespräch: Ich bin ins Innere der Moleküle gestiegen.” KontakTUM Magazin 2/2010, 6-11.
4. Groll, M., Gallastegui, N., Maréchal, X., Le Ravalec, V., Basse, N., Richy, N., Genin, E., Huber, R., Moroder, L., Vidal, J. and Reboud-Ravaux, M. (2010). [1188] ”20S Proteasome Inhibition: Designing noncovalent linear peptide mimics of the natural product TMC-95A.” ChemMedChem 5, 1701-1705.
5. Merdanovic, M., Mamant, N., Meltzer, M., Poepsel, S., Auckenthaler, A., Melgaard, R., Hauske, P., Nagel-Steger, L., Clarke, A. R., Kaiser, M., Huber, R. and Ehrmann, M. (2010). [1187] ”Determinants of structural and functional plasticity of a widely conserved protease chaperone complex.” Nat. Struct. Mol. Biol. 17, 837-843.
6. Krojer, T., Sawa, J., Huber, R. and Clausen, T. (2010). ”HtrA proteases have a conserved activation mechanism that can be triggered by distinct molecular cues.” Nat. Struct. Mol. Biol. 17, 844-852.
7. Ducka, A. M., Joel, P., Popowicz, G. M., Trybus, K. M., Schleicher, M., Noegel, A. A., Huber, R., Holak, T. A. and Sitar, T. (2010). [1185] ”Structures of actin-bound Wiskott-Aldrich syndrome protein homology 2 (WH2) domains of Spire and the implication for filament nucleation.” Proc. Natl. Acad. Sci. USA 107, 11757-11762.
8. Hasenbein, S., Meltzer, M., Hauske, P., Kaiser, M., Huber, R., Clausen, T. and Ehrmann, M. (2010). ”Conversion of a regulatory into a degradative protease.” J. Mol. Biol. 397, 957-966.
9. Ottmann, C., Rose, R., Huttenlocher, F., Cedzich, A., Hauske, P., Kaiser, M., Huber, R. and Schaller, A. (2009). ”Structural basis for Ca2+-independence and activation by homodimerization of tomato subtilase 3.” Proc. Natl. Acad. Sci. USA 106, 17223-17228.
10. Clerc, J., Florea, B. I., Kraus, M., Groll, M., Huber, R., Bachmann, A. S., Dudler, R., Driessen, C., Overkleeft, H. S. and Kaiser, M. (2009). [1182] ”Syringolin A selectively labels the 20 S proteasome in murine EL4 and wild-type and bortezomib-adapted leukaemic cell lines.” CHEMBIOCHEM 10, 2638-2643.
11. Meltzer, M., Hasenbein, S., Mamant, N., Merdanovic, M., Poepsel, S., Hauske, P., Kaiser, M., Huber, R., Krojer, T., Clausen, T. and Ehrmann, M. (2009). [1181] ”Structure, function and regulation of the conserved serine proteases DegP and DegS of Escherichia coli.” Res. Microbiol. 160, 660-666.
12. Breithaupt, C., Kurzbauer, R., Schaller, F., Stintzi, A., Schaller, A., Huber, R., Macheroux, P. and Clausen, T. (2009). ”Structural basis of substrate specificity of plant 12-oxophytodienoate reductases.” J. Mol. Biol. 392, 1266-1277.
13. Lee, J. H., Maskos, K. and Huber, R. (2009). ”Structural and Functional Studies of the Yeast Class II Hda1 Histone Deacetylase Complex.” J. Mol. Biol. 391, 744-757.
14. Wolschner, C., Giese, A., Kretzschmar, H. A., Huber, R., Moroder, L. and Budisa, N. (2009). ”Design of anti- and pro-aggregation variants to assess the effects of methionine oxidation in human prion protein.” Proc. Natl. Acad. Sci. USA 106, 7756-7761.
15. Clerc, J., Groll, M., Illich, D. J., Bachmann, A. S., Huber, R., Schellenberg, B., Dudler, R. and Kaiser, M. (2009). ”Synthetic and structural studies on syringolin A and B reveal critical determinants of selectivity and potency of proteasome inhibition.” Proc. Natl. Acad. Sci. USA 106, 6507-6512.
16. Buckel, P. and Huber, R. (2009). ”Technologietransfer Ausgründung: SuppreMol GmbH – Innovationen kann man nicht planen.” Max-Planck-Innovation, Connecting Science and Business 1/2009
17. Huber, R. (2009). Foreword. Oxidative Folding of Peptides and Proteins. J. Buchner and L. Moroder. The Royal Society of Chemistry, RSC Publishing, Cambridge, UK. Sanglas, L., Aviles, F. X., Huber, R., Gomis-Rüth, F. X. and Arolas, J. L. (2009). ”Mammalian metallopeptidase inhibition at the defense barrier of Ascaris parasite.” Proc. Natl. Acad. Sci. USA 106, 1743-1747.
18. Groll, M., Huber, R. and Moroder, L. (2009). ”The persisting challenge of selective and specific proteasome inhibition.” Journal of Peptide Science 15, 58-66.
19. Huber, R. (2008). Schönheit und Zweckmässigkeit der Bausteine des Lebens – über die Architektur der Proteine. Orden pour le Mérite, Reden und Gedenkworte, 2007-2008. Göttingen, Wallstein Verlag. 36: 15-45.
20. Huber, R. (2008). ”Brain Drain – Brain Gain, Forschungsstandort Deutschland.” E.ON Bayern Kulturmagazin ”Bayerns Beste” 01, 10-15.
21. Chatwell, L., Illarionova, V., Illarionov, B., Eisenreich, W., Huber, R., Skerra, A., Bacher, A. and Fischer, M. (2008). ”Structure of Lumazine Protein, an optical transponder of luminescent bacteria.” J. Mol. Biol. 382, 44-55.
22. Breithaupt, C., Schäfer, B., Pellkofer, H., Huber, R., Linington, C. and Jacob, U. (2008). ”Demyelinating myelin oligodendrocyte glycoprotein-specific autoantibody response is focused on one dominant conformational epitope region in rodents.” The Journal of Immunology 181, 1255-1263.
23. Krojer, T., Pangerl, K., Kurt, J., Sawa, J., Stingl, C., Mechtler, K., Huber, R., Ehrmann, M. and Clausen, T. (2008). ”Interplay of PDZ and protease domain of DegP ensures efficient elimination of misfolded proteins.” Proc. Natl. Acad. Sci. USA 105, 7702-7707.
24. Borelli, C., Ruge, E., Lee, J. H., Schaller, M., Vogelsang, A., Monod, M., Korting, H. C., Huber, R. and Maskos, K. (2008). ”X-ray structures of Sap1 and Sap5: Structural comparison of the secreted aspartic proteinases from Candida albicans.” Proteins 72, 1308-1319.
25. Groll, M., Schellenberg, B., Bachmann, A. S., Archer, C. R., Huber, R., Powell, T. K., Lindow, S., Kaiser, M. and Dudler, R. (2008). ”A plant pathogen virulence factor inhibits the eukaryotic proteasome by a novel mechanism.” Nature 452, 755-758.
26. Huber, R. and Sacharow-Ross, I. (2007). ] Ein Wissenschaftler und ein Künstler im Gespräch. Syntopia, Igor Sacharow-Ross. A. Niehaus and D. Ronte. Köln, Wienand Verlag: 128-137.
27. Debela, M., Hess, P., Magdolen, V., Schechter, N. M., Steiner, T., Huber, R., Bode, W. and Goettig, P. (2007). ”Chymotryptic specificity determinants in the 1.0 Å structure of the zinc-inhibited human tissue kallikrein 7.” Proc. Natl. Acad. Sci. USA 104, 16086-16091.
28. Debela, M., Goettig, P., Magdolen, V., Huber, R., Schechter, N. M. and Bode, W. (2007). ”Structural basis of the zinc inhibition of human tissue kallikrein 5.” J. Mol. Biol. 373, 1017-1031.
29. Velarde, M., Huber, R., Yanagisawa, S., Dennison, C. and Messerschmidt, A. (2007). ”Influence of loop shortening on the metal binding site of Cupredoxin Pseudoazurin.” Biochemistry 46, 9981-9991.
30. Schmidt, M., Patel, A., Zhao, Y. and Reuter, W. (2007). ”Structural basis for the photochemistry of alpha-phycoerythrocyanin.” Biochemistry 46, 416-423.
31. Tochowicz, A., Maskos, K., Huber, R., Oltenfreiter, R., Dive, V., Yiotakis, A., Zanda, M., Bode, W. and Goettig, P. (2007). ”Crystal structures of MMP-9 complexes with five inhibitors: Contribution of the flexible Arg424 side-chain to selectivity.” J. Mol. Biol. 371, 989-1006.
32. Borelli, C., Ruge, E., Schaller, M., Monod, M., Korting, H. C., Huber, R. and Maskos, K. (2007). ”The crystal structure of the secreted aspartic proteinase 3 from Candida albicans and its complex with pepstatin A.” Proteins 68, 738-748.
33. Kyrieleis, O. J., Huber, R., Ong, E., Oehler, R., Hunter, M., Madison, E. L. and Jacob, U. (2007). ”Crystal structure of the catalytic domain of DESC1, a new member of the type II transmembrane serine proteinase family.” FEBS J. 274, 2148-2160.
34. Steiner, T., Lamerz, A. C., Hess, P., Breithaupt, C., Krapp, S., Bourenkov, G., Huber, R., Gerardy-Schahn, R. and Jacob, U. (2007). ”Open and closed structures of the UDP-glucose pyrophosphorylase from Leishmania major.” J. Biol. Chem. 282, 13003-13010.
35. Keil, C., Maskos, K., Than, M., Hoopes, J. T., Huber, R., Tan, F., Deddish, P. A., Erdos, E. G., Skidgel, R. A. and Bode, W. (2007). ”Crystal structure of the human carboxypeptidase N (kininase I) catalytic domain.” J. Mol. Biol. 366, 504-516.
36. Li, C., Yanagisawa, S., Martins, B. M., Messerschmidt, A., Banfield, M. J. and Dennison, C. (2006). [ "Basic requirements for a metal-binding site in a protein: the influence of loop shortening on the cupredoxin azurin." Proc. Natl. Acad. Sci. USA 103, 7258-7263.
37. Schmidt, M., Krasselt, A. and Reuter, W. (2006). "Local protein flexibility as a prerequisite for reversible chromophore isomerization in alpha-phycoerythrocyanin." Biochim. Biophys. Acta. 1764, 55-62.
38. Bonn, S., Herrero, S., Breitenlechner, C., Erlbruch, A., Lehmann, W., Engh, R. A., Gassel, M. and Bossemeyer, D. (2006). "Structural Analysis of Protein Kinase A Mutants with Rho-kinase Inhibitor Specificity." J. Biol. Chem. 281, 24818-24830.
39. Breithaupt, C., Kurzbauer, R., Lilie, H., Schaller, A., Strassner, J., Huber, R., Macheroux, P. and Clausen, T. (2006). "Crystal structure of 12-oxophytodienoate reductase 3 from tomato: Self-inhibition by dimerization." Proc. Natl. Acad. Sci. USA 103, 14337-14342.
40. Tamulaitiene, G., Jakubauskas, A., Urbanke, C., Huber, R., Grazulis, S. and Siksnys, V. (2006). "The crystal structure of the rare-cutting restriction enzyme SdaI reveals unexpected domain architecture." Structure 14, 1389-1400.
41. Debela, M., Magdolen, V., Grimminger, V., Sommerhoff, C., Messerschmidt, A., Huber, R., Friedrich, R., Bode, W. and Goettig, P. (2006). "Crystal structures of human tissue kallikrein 4: activity modulation by a specific zinc binding site." J. Mol. Biol. 362, 1094-1107.
42. Sitar, T., Popowicz, G. M., Siwanowicz, I., Huber, R. and Holak, T. A. (2006). "Structural basis for the inhibition of insulin-like growth factors by insulin-like growth factor-binding proteins." Proc. Natl. Acad. Sci. USA 103, 13028-13033.
43. Kaiser, M., Groll, M., Siciliano, C., Götz, M., Assfalg-Machleidt, I., Kohno, J., Milbradt, A., Renner, C., Huber, R. and Moroder, L. (2005). Inhibition of yeast 20S proteasome by biaryl- ansbiaryl ether-cross-bridges tripeptide derivatives as TMC-95A analogs. Peptides, Biology and Chemistry. K. L. Liu and J. P. Tam. Monmouth Junction, Science Press USA Inc.
44. Chatwell, L., Krojer, T., Fidler, A., Römisch, W., Eisenreich, W., Bacher, A., Huber, R. and Fischer, M. (2006). "Biosynthesis of riboflavin: Structure and properties of 2,5-Diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate reductase of Methanocaldococcus jannaschii." J. Mol. Biol. 359, 1334-1351.
45. Groll, M., Huber, R. and Potts, B. C. (2006). "Crystal structures of Salinosporamide A (NPI-0052) and B (NPI-0047) in complex with the 20S proteasome reveal important consequences of b-lactone ring opening and a mechanism for irreversible binding." J. Am. Chem. Soc. 128, 5136-5141.
46. Mooser, D., Maneg, O., Corvey, C., Steiner, T., Malatesta, F., Karas, M., Soulimane, T. and Ludwig, B. (2005). "A four-subunit cytochrome bc1 complex complements the respiratory chain of Thermus thermophilus." Biochim. Biophys. Acta - Bioenergetics 1708, 262-274.
47. Jourdan, F., Kaiser, J. T. and Lowe, D. J. (2005). "Synthesis of New N-(5-Oxo-2,5-dihydro)pyrrol-3-yl Glycines and N-(5-Oxo-2,5-dihydro)pyrrol-3-yl Glycines Esters." Synthetic Communications 35, 2453-2466.
48. Visse, R., Bode, W., Maskos, K. and Nagase, H. (2005). "Structural basis for collagenolytic activity of matrix metalloproteinase-1 (collagenase1)." Int. J. of Experimental Pathology 86, A87-A88.
49. Groll, M., Larionov, O. V., Huber, R. and de Meijere, A. (2006). "Inhibitor-binding mode of homobelactosin C to proteasomes: New insights into class I MHC ligand generation." Proc. Natl. Acad. Sci. USA 103, 4576-4579.
50. Einsle, O., Niessen, H., Abt, D. J., Seiffert, G., Schink, B., Huber, R., Messerschmidt, A. and Kroneck, P. M. (2005). "Crystallization and preliminary X-ray analysis of the tungsten-dependent acetylene hydratase from Pelobacter acetylenicus." Acta Cryst. F61, 299-301.
51. Beaufort, N., Debela, M., Creutzburg, S., Kellermann, J., Bode, W., Schmitt, M., Pidard, D. and Magdolen, V. (2006). "Interplay of human tissue kallikrein 4 (hK4) with the plasminogen activation system: hK4 regulates the structure and functions of the urokinase-type plasminogen activator receptor (uPAR)." Biol. Chem. 387, 217-222.
52. Bode, W. (2006). "Structure and interaction modes of thrombin." Blood Cells Mol. Dis. 36, 122-130.
53. Zeslawska, E., Jacob, U., Stürzebecher, J. and Oleksyn, B. J. (2006). "The crystal structures of 3-TAPAP in complexes with the urokinase-type plasminogen activator and picrate." Bioorg. Med. Chem. Lett. 16, 228-234.
54. Rohr, K. B., Selwood, T., Marquardt, U., Huber, R., Schechter, N. M., Bode, W. and Than, M. E. (2005). "X-ray structures of free and leupeptin-complexed human aI-tryptase mutants: Indication for an a-->b-tryptase transition." J. Mol. Biol. 357, 195-209.
55. Kaiser, M., Groll, M., Götz, M., Siciliano, C., Assfalg-Machleidt, I., Weyher, E., Kohno, J., Milbradt, A., Renner, C., Huber, R. and Moroder, L. (2005). Structural determinants for 20S proteasome inhibition by TMC-95A. Peptides 2004. M. Flegel, M. Fridkin, C. Gilon and J. Slaninova. Geneve, Kenes International: 657-658.
56. Engel, M., Hoffmann, T., Manhart, S., Heiser, U., Chambre, S., Huber, R., Demuth, H. U. and Bode, W. (2006). "Rigidity and flexibility of Dipeptidyl Peptidase IV: Crystal structures of and docking experiments with DPIV." J. Mol. Biol. 355, 768-783.
57. Golbik, R., Yu, C., Weyher-Stingl, E., Huber, R., Moroder, L., Budisa, N. and Schiene-Fischer, C. (2005). "Peptidyl prolyl cis/trans-isomerases: comparative reactivities of cyclophilins, FK506-binding proteins, and parvulins with fluorinated oligopeptide and protein substrates." Biochemistry 44, 16026-16034.
58. Friedrich, R., Panizzi, P., Kawabata, S. I., Bode, W., Bock, P. E. and Fuentes-Prior, P. (2006). "Structural basis for reduced staphylocoagulase-mediated bovine prothrombin activation." J. Biol. Chem. 281, 1188-1195.
59. Panizzi, P., Friedrich, R., Fuentes-Prior, P., Richter, K., Bock, P. E. and Bode, W. (2006). "Fibrinogen substrate recognition by staphylocoagulase (pro)thrombin complexes." J. Biol. Chem. 281, 1179-1187.
60. Panizzi, P., Friedrich, R., Fuentes-Prior, P., Kroh, H. K., Briggs, J., Tans, G., Bode, W. and Bock, P. E. (2006). "Novel fluorescent prothrombin analogs as probes of staphylocoagulase-prothrombin interactions." J. Biol. Chem. 281, 1169-1178.
61. Bayes, A., Comellas-Bigler, M., Rodriguez de la Vega, M., Maskos, K., Bode, W., Aviles, F. X., Jongsma, M. A., Beekwilder, J. and Vendrell, J. (2005). "Structural basis of the resistance of an insect carboxypeptidase to plant protease inhibitors." Proc. Natl. Acad. Sci. USA 102, 16602-16607.
62. Ramsperger, A., Augustin, M., Schott, A. K., Gerhardt, S., Krojer, T., Eisenreich, W., Illarionov, B., Cushman, M., Bacher, A., Huber, R. and Fischer, M. (2006). "Crystal structure of an archaeal pentameric riboflavin synthase in complex with a substrate analog inhibitor: Stereochemical implications." J. Biol. Chem. 281, 1224-1232.
63. Grazulis, S., Manakova, E., Roessle, M., Bochtler, M., Tamulaitiene, G., Huber, R. and Siksnys, V. (2005). "Structure of the metal-independent restriction enzyme BfiI reveals fusion of a specific DNA-binding domain with a nonspecific nuclease." Proc. Natl. Acad. Sci. USA 102, 15797-15802.
64. Boll, M., Schink, B., Messerschmidt, A. and Kroneck, P. M. (2005). "Novel bacterial molybdenum and tungsten enzymes: three-dimensional structure, spectroscopy, and reaction mechanism." Biol. Chem. 386, 999-1006.
65. Buckel, W., Martins, B. M., Messerschmidt, A. and Golding, B. T. (2005). "Radical-mediated dehydration reactions in anaerobic bacteria." Biol. Chem. 386, 951-959.
66. D'Silva, L., Ozdowy, P., Krajewski, M., Rothweiler, U., Singh, M. and Holak, T. A. (2005). "Monitoring the effects of antagonists on protein-protein interactions with NMR spectroscopy." J. Am. Chem. Soc. 127, 13220-13226.
67. Than, M. E., Bourenkov, G., Henrich, S., Mann, K. and Bode, W. (2005). "The NC1 dimer of human placental basement membrane collagen IV: does a covalent crosslink exist?" Biol. Chem. 386, 759-766.
68. Breitenlechner, C. B., Kairies, N. A., Honold, K., Scheiblich, S., Koll, H., Greiter, E., Koch, S., Schafer, W., Huber, R. and Engh, R. A. (2005). "Crystal structures of active Src kinase domain complexes." J. Mol. Biol. 353, 222-231.
69. Groll, M. and Huber, R. (2005). "Purification, crystallization, and x-ray analysis of the yeast 20S proteasome." Methods in Enzymology 398, 329-336.
70. Arolas, J. L., Popowicz, G. M., Bronsoms, S., Aviles, F. X., Huber, R., Holak, T. A. and Ventura, S. (2005). "Study of a major intermediate in the oxidative folding of leech carboxypeptidase inhibitor: Contribution of the fourth disulfide bond." J. Mol. Biol. 352, 961-975.
71. Messerschmidt, A., Macieira, S., Velarde, M., Badeker, M., Benda, C., Jestel, A., Brandstetter, H., Neuefeind, T. and Blaesse, M. (2005). "Crystal structure of the catalytic domain of human atypical protein kinase C-iota reveals interaction mode of phosphorylation site in turn motif." J. Mol. Biol. 352, 918-931.
72. Locher, M., Lehnert, B., Krauss, K., Heesemann, J., Groll, M. and Wilharm, G. (2005). "Crystal structure of the Yersinia enterocolitica type III secretion chaperone SycT." J. Biol. Chem. 280, 31149-31155.
73. Kacprzak, M. M., Than, M. E., Juliano, L., Juliano, M. A., Bode, W. and Lindberg, I. (2005). "Mutations of the PC2 substrate binding pocket alter enzyme specificity." J. Biol. Chem. 280, 31850-31858.
74. Göttig, P. W., Brandstetter, H., Groll, M., Göhring, W., Konarev, P. V., Svergun, D. I., Huber, R. and Kim, J. S. (2005). "X-ray snapshots of peptide processing in mutants of tricorn interacting factor F1 thermoplasma acidophilum." J. Biol. Chem. 280, 33387-33396.
75. Riester, D., Wirsching, F., Salinas, G., Keller, M., Gebinoga, M., Kamphausen, S., Merkwirth, C., Goetz, R., Wiesenfeldt, M., Stürzebecher, J., Bode, W., Friedrich, R., Thurk, M. and Schwienhorst, A. (2005). "Thrombin inhibitors identified by computer-assisted multiparameter design." Proc. Natl. Acad. Sci. USA 102, 8597-8602.
76. Bode, W. (2005). "The structure of thrombin, a chameleon-like proteinase." J. Thromb. Haemost. 3, 2379-2388.
77. Arolas, J. L., Popowicz, G. M., Lorenzo, J., Sommerhoff, C. P., Huber, R., Aviles, F. X. and Holak, T. A. (2005). "The three-dimensional structures of tick carboxypeptidase inhibitor in complex with A/B carboxypeptidases reveal a novel double-headed binding mode." J. Mol. Biol. 350, 489-498.
78. Kyrieleis, O. J., Göttig, P., Kiefersauer, R., Huber, R. and Brandstetter, H. (2005). "Crystal structures of the tricorn interacting factor F3 from Thermoplasma acidophilum, a zinc aminopeptidase in three different conformations." J. Mol. Biol. 349, 787-800.
79. Mayewski, S. (2005). "A multibody, whole-residue potential for protein structures, with testing by Monte Carlo simulated annealing." Proteins: Structure, Function, and Bioinformatics 59, 152-169.
80. Abdulhussein, R., McFadden, C., Fuentes-Prior, P. and Vogel, W. F. (2004). "Exploring the collagen-binding site of the DDR1 tyrosine kinase receptor." J. Biol. Chem. 279, 31462-31470.
81. Schweinitz, A., Steinmetzer, T., Banke, I. J., Arlt, M. J., Stürzebecher, A., Schuster, O., Geissler, A., Giersiefen, H., Zeslawska, E., Jacob, U., Krüger, A. and Stürzebecher, J. (2004). "Design of novel and selective inhibitors of urokinase-type plasminogen activator with improved pharmacokinetic properties for use as antimetastatic agents." J. Biol. Chem. 279, 33613-33622.
82. Münster-Kühnel, A. K., Tiralongo, J., Krapp, S., Weinhold, B., Ritz-Sedlacek, V., Jacob, U. and Gerardy-Schahn, R. (2004). "Structure and function of vertebrate CMP-sialic acid synthetases." Glycobiology 14, 43R-51R.
83. Comellas-Bigler, M., Lang, R., Bode, W. and Maskos, K. (2005). "Crystal structure of the E.coli dipeptidyl carboxypeptidase Dcp: further indication of a ligand-dependant hinge movement mechanism." J. Mol. Biol. 349, 99-112.
84. Than, M. E., Henrich, S., Bourenkov, G. P., Bartunik, H. D., Huber, R. and Bode, W. (2005). "The endoproteinase furin contains two essential Ca 2+ ions stabilizing its N-terminus and the unique S1 specificity pocket." Acta Cryst. D61, 505-512.
85. Maskos, K. (2004). Pitrilysins/inverzincins. Handbook of Metalloproteins. A. Messerschmidt, M. Cygler and W. Bode. Chichester, England, John Wiley & Sons, Ltd. 3: 190-198.
86. Bode, W. and Maskos, K. (2004). Matrix metalloproteinases. Handbook of Metalloproteins. A. Messerschmidt, M. Cygler and W. Bode. Chichester, England, John Wiley & Sons, Ltd. 3: 130-147.
87. Maskos, K. (2005). "Crystal structures of MMPs in complex with physiological and pharmacological inhibitors." Biochimie 87, 249-263.
88. Wisniewska, M., Bossenmaier, B., Georges, G., Hesse, F., Dangl, M., Kunkele, K. P., Ioannidis, I., Huber, R. and Engh, R. A. (2005). "The 1.1Å resolution crystal structure of the p130cas SH3 domain and ramifications for ligand selectivity." J. Mol. Biol. 347, 1005-1014.
89. Bochtler, M., Groll, M., Brandstetter, H., Clausen, T. and Huber, R. (2005). Molecular machines for protein degradation. Protein Degradation. R. J. Mayer, A. Ciechanover and M. Rechsteiner. Weinheim, Wiley-VCH Verlag. 1: 248-287.
90. Fuentes-Prior, P. and Salvesen, G. S. (2004). "The protein structures that shape caspase activity, specificity, activation and inhibition." Biochem. J. 384, 201-232.
91. Pal, P. P., Bae, J. H., Azim, M. K., Hess, P., Friedrich, R., Huber, R., Moroder, L. and Budisa, N. (2005). "Structural and spectral response of Aequorea victoria green fluorescent proteins to chromophore fluorination." Biochemistry 44, 3663-3672.
92. Jauch, R., Humm, A., Huber, R. and Wahl, M. C. (2005). "Structures of Escherichia coli NAD synthetase with substrates and products reveal mechanistic rearrangements." J. Biol. Chem. 280, 15131-15140.
93. Hochleitner, E. O., Sondermann, P. and Lottspeich, F. (2004). "Determination of the stoichiometry of protein complexes using liquid chromatography with fluorescence and mass spectrometric detection of fluorescently labeled proteolytic peptides." Proteomics 4, 669-676.
94. Martins, B. M., Macedo-Ribeiro, S., Bresser, J., Buckel, W. and Messerschmidt, A. (2005). "Structural basis for stereo-specific catalysis in NAD(+)-dependent (R)-2-hydroxyglutarate dehydrogenase from Acidaminococcus fermentans." FEBS J. 272, 269-281.
95. Koch, M., Velarde, M., Harrison, M. D., Echt, S., Fischer, M., Messerschmidt, A. and Dennison, C. (2005). "Crystal structures of oxidized and reduced stellacyanin from horseradish roots." J. Am. Chem. Soc. 127, 158-166.
96. Groll, M., Bochtler, M., Brandstetter, H., Clausen, T. and Huber, R. (2005). "Molecular machines for protein degradation." CHEMBIOCHEM 6, 222-256.
97. Theodoratou, E., Huber, R. and Böck, A. (2005). "[NiFe]-Hydrogenase maturation endopeptidase: structure and function.” Biochem. Soc. Trans. 33, 108-111.
98. Siwanowicz, I., Popowicz, G. M., Wisniewska, M., Huber, R., Künkele, K. P., Lang, K., Engh, R. A. and Holak, T. A. (2005). ”Structural basis for the regulation of insulin-like growth factors by IGF binding proteins.” Structure 13, 155-167.
99. Jozic, D., Bourenkov, G., Lim, N. H., Visse, R., Nagase, H., Bode, W. and Maskos, K. (2005). ”X-ray structure of human proMMP-1: New insights into procollagenase activation and collagen binding.” J. Biol. Chem. 280, 9578-9585.
100. Breitenlechner, C. B., Friebe, W. G., Brunet, E., Werner, G., Graul, K., Thomas, U., Künkele, K. P., Schäfer, W., Gassel, M., Bossemeyer, D., Huber, R., Engh, R. A. and Masjost, B. (2005). ”Design and crystal structures of protein kinase B-selective inhibitors in complex with protein kinase A and mutants.” J. Med. Chem. 48, 163-170.
101. Henrich, S., Lindberg, I., Bode, W. and Than, M. E. (2005). ”Proprotein convertase models based on the crystal structures of furin and kexin: Explanation of their specificity.” J. Mol. Biol. 345, 211-227.
102. Panizzi, P., Friedrich, R., Fuentes-Prior, P., Bode, W. and Bock, P. E. (2004). ”The staphylocoagulase family of zymogen activator and adhesion proteins.” Cell. Mol. Life Sci. 61, 2793-2798.
103. Budisa, N. (2004). [1088] ”Prolegomena to future experimental efforts on genetic code engineering by expanding its amino acid repertoire.” Angew. Chem. Int. Ed. 43, 6426-6463.
104. Wenig, K., Chatwell, L., von Pawel-Rammingen, U., Bjorck, L., Huber, R. and Sondermann, P. (2004). ”Structure of the streptococcal endopeptidase IdeS, a cysteine proteinase with strict specificity for IgG.” Proc. Natl. Acad. Sci. USA 101, 17371-17376.
105. Groll, M. and Huber, R. (2004). ”Inhibitors of the eukaryotic 20S proteasome core particle: a structural approach.” Biochim. Biophys. Acta 1695, 33-44.
106. Budisa, N. and Pal, P. P. (2004). ”Designing novel spectral classes of proteins with a tryptophan-expanded genetic code.” Biol. Chem. 385, 893-904.
107. Paschos, A., Theodoratou, E., Fritsche, E., Böck, A. and Huber, R. (2004). Hydrogenase maturation endopeptidase. Handbook of Proteolytic Enzymes 2nd Edn, Elsevier Ltd.: 980-982.
108. Budisa, N., Pipitone, O., Siwanowicz, I., Rubini, M., Pal, P. P., Holak , T. A. and Gelmi, M. L. (2004). ”Efforts towards the design of ’Teflon’ proteins: In vivo translation with trifluorinated leucine and methionine analogues.” Chemistry & Biodiversity 1, 1465-1475.
109. Budisa, N. (2004). ”Adding new tools to the arsenal of expressed protein ligation.” CHEMBIOCHEM 5, 1176-1179.
110. Breitenlechner, C., Gaßel, M., Engh, R. A. and Bossemeyer, D. (2004). ”Structural insights into AGC kinase inhibition.” Oncol. Res. 14, 267-278.
111. Klein, C., Hesse, F., Dehner, A., Engh, R. A., Schwaiger, M. and Hansen, S. (2004). ”In vitro folding and characterization of the p53 DNA binding domain.” Biol. Chem. 385, 95-102.
112. Stanitzek, S., Augustin, M. A., Huber, R., Kupke, T. and Steinbacher, S. (2004). ”Structural basis of CTP-dependent peptide bond formation in coenzyme A biosynthesis catalyzed by Escherichia coli PPC synthetase.” Structure 12, 1977-1988.
113. Martins, B. M., Dobbek, H., Cinkaya, I., Buckel, W. and Messerschmidt, A. (2004). ”Crystal structure of 4-hydroxybutyryl-CoA dehydratase: Radical catalysis involving a [4Fe-4S] cluster and flavin.” Proc. Natl. Acad. Sci. USA 101, 15645-15649.
114. Kaiser, M., Milbradt, A. G., Renner, C., Assfalg-Machleidt, I., Groll, M., Huber, R. and Moroder, L. (2004). Cyclic Biphenyl Ether Tripeptides as Proteasome Inhibitors. Peptides. Peptide Revolution: Genomics, Proteomics & Therapeutics. M. Chorev and T. K. Sawyer. Cardiff, USA, American Chemical Society: 348-349.
115. Fischer, M., Schott, A. K., Römisch, W., Ramsperger, A., Augustin, M., Fidler, A., Bacher, A., Richter, G., Huber, R. and Eisenreich, W. (2004). ”Evolution of vitamin B2 biosynthesis. A novel class of riboflavin synthase in Archaea.” J. Mol. Biol. 343, 267-278.
116. Bonin, I., Mühlberger, R., Bourenkov, G. P., Huber, R., Bacher, A., Richter, G. and Wahl, M. C. (2004). ”Structural basis for the interaction of Escherichia coli NusA with protein N of phage l.” Proc. Natl. Acad. Sci. USA 101, 13762-13767.
117. Popowicz, G. M., Müller, R., Noegel, A. A., Schleicher, M., Huber, R. and Holak, T. A. (2004). ”Molecular structure of the rod domain of Dictyostelium filamin.” J. Mol. Biol. 342, 1637-1646.
118. Groll, M. and Huber, R. (2004). Structures of the Yeast Proteasome Core Particle in Complex with Inhibitors. Cancer Drug Discovery and Development: Proteasome Inhibitors in Cancer Therapy. J. Adams. Totowa, NJ, Humana Press Inc.: 39-46.
119. Kaiser, M., Groll, M., Siciliano, C., Assfalg-Machleidt, I., Weyher, E., Kohno, J., Milbradt, A. G., Renner, C., Huber, R. and Moroder, L. (2004). ”Binding mode of TMC-95A analogues to eukaryotic 20S proteasome.” CHEMBIOCHEM 5, 1256-1266.
120. Messerschmidt, A., Niessen, H., Abt, D., Einsle, O., Schink, B. and Kroneck, P. M. (2004). ”Crystal structure of pyrogallol-phloroglucinol transhydroxylase, an Mo enzyme capable of intermolecular hydroxyl transfer between phenols.” Proc. Natl. Acad. Sci. USA 101, 11571-11576.
121. Keil, C., Huber, R., Bode, W. and Than, M. E. (2004). ”Cloning, expression, crystallization and initial crystallographic analysis of the C-terminal domain of the amyloid precursor protein APP.” Acta Cryst. D60, 1614-1617.
122. Echt, S., Bauer, S., Steinbacher, S., Huber, R., Bacher, A. and Fischer , M. (2004). ”Potential anti-infective targets in pathogenic yeasts: structure and properties of 3,4-dihydroxy-2-butanone 4-phosphate synthase of Candida albicans.” J. Mol. Biol. 341, 1085-1096.
123. Bonin, I., Martins, B. M., Purvanov, V., Fetzner, S., Huber, R. and Dobbek, H. (2004). ”Active site geometry and substrate recognition of the molybdenum hydroxylase quinoline 2-oxidoreductase.” Structure 12, 1425-1435.
124. Koch, M., Breithaupt, C., Gerhardt, S., Haase, I., Weber, S., Cushman, M., Huber, R., Bacher, A. and Fischer, M. (2004). ”Structural basis of charge transfer complex formation by riboflavin bound to 6,7-dimethyl-8-ribityllumazine synthase.” Eur. J. Biochem. 271, 3208-3214.
125. Comellas-Bigler, M., Maskos, K., Huber, R., Oyama, H., Oda, K. and Bode, W. (2004). ”1.2 Å crystal structure of the serine carboxyl proteinase pro-kumamolisin; structure of an intact pro-subtilase.” Structure 12, 1313-1323.
126. Kacprzak, M. M., Peinado, J. R., Than, M. E., Appel, J., Henrich, S., Lipkind, G., Houghten, R. A., Bode, W. and Lindberg, I. (2004). ”Inhibition of furin by polyarginine-containing peptides: nanomolar inhibition by nona-D-arginine.” J. Biol. Chem. 279, 36788-36794.
127. Steinbacher, S., Schiffmann, S., Bacher, A. and Fischer, M. (2004). ”Metal sites in 3,4-dihydroxy-2-butanone 4-phosphate synthase from Methanococcus jannaschii in complex with the substrate ribulose 5-phosphate.” Acta Cryst. D60, 1338-1340.
128. Laupitz, R., Hecht, S., Amslinger, S., Zepeck, F., Kaiser, J., Richter, G., Schramek, N., Steinbacher, S., Huber, R., Arigoni, D., Bacher, A., Eisenreich, W. and Rohdich, F. (2004). ”Biochemical characterization of Bacillus subtilis type II isopentenyl diphosphate isomerase, and phylogenetic distribution of isoprenoid biosynthesis pathways.” Eur. J. Biochem. 271, 2658-2669.
129. Breitenlechner, C., Engh, R. A., Huber, R., Kinzel, V., Bossemeyer, D. and Gassel, M. (2004). ”The typically disordered N-Terminus of PKA can fold as a helix and project the myristoylation site into solution.” Biochemistry 43, 7743-7749.
130. Bauer, S., Schott, A. K., Illarionova, V., Bacher, A., Huber, R. and Fischer, M. (2004). ”Biosynthesis of tetrahydrofolate in plants: Crystal structure of 7,8-dihydroneopterin aldolase from Arabidopsis thaliana reveals a novel adolase class.” J. Mol. Biol. 339, 967-979.
131. Bader, G., Gomez-Ortiz, M., Haussmann, C., Bacher, A., Huber, R. and Fischer, M. (2004). ”Structure of the molybdenum-cofactor biosynthesis protein MoaB of Escherichia coli.” Acta Cryst. D60, 1068-1075.
132. Bae, J. H., Pal, P. P., Moroder, L., Huber, R. and Budisa, N. (2004). ”Crystallographic evidence for isomeric chromophores in 3-Fluorotyrosyl-Green fluorescent protein.” CHEMBIOCHEM 5, 720-722.
133. Budisa, N., Pal, P. P., Alefelder, S., Birle, P., Krywcun, T., Rubini, M., Wenger, W., Bae, J. H. and Steiner, T. (2004). ”Probing the role of tryptophans in Aequorea victoria green fluorescent proteins with an expanded genetic code.” Biol. Chem. 385, 191-202.
134. Reverter, D., Maskos, K., Tan, F., Skidgel, R. A. and Bode, W. (2004). ”Crystal structure of human carboxypeptidase M, a membrane-bound enzyme that regulates peptide hormone activity.” J. Mol. Biol. 338, 257-269.
135. Fritze, I. M., Linden, L., Freigang, J., Auerbach, G., Huber, R. and Steinbacher, S. (2004). ”The crystal structures of Zea mays and Arabidopsis 4-hydroxyphenylpyruvate dioxygenase.” Plant Physiol. 134, 1388-1400.
136. Koch, M., Breithaupt, C., Kiefersauer, R., Freigang, J., Huber, R. and Messerschmidt, A. (2004). ”Crystal structure of protoporphyrinogen IX oxidase: a key enzyme in haem and chlorophyll biosynthesis.” EMBO J. 23, 1720-1728.
137. Breitenlechner, C. B., Wegge, T., Berillon, L., Graul, K., Marzenell, K., Friebe, W. G., Thomas, U., Schumacher, R., Huber, R., Engh, R. A. and Masjost, B. (2004). ”Structure-based optimization of novel Azepane derivatives as PKB inhibitors.” J. Med. Chem. 47, 1375-1390.
138. Gaßel, M., Breitenlechner, C. B., König, N., Huber, R., Engh, R. A. and Bossemeyer, D. (2004). ”The protein kinase C inhibitor bisindolyl-maleimide II binds with reversed orientations to different conformations of PKA.” J. Biol. Chem. 279, 23679-23690.
139. Than, M. E., Helm, M., Simpson, D. J., Lottspeich, F., Huber, R. and Gietl, C. (2004). ”The 2.0 Å crystal structure and substrate specificity of the KDEL-tailed cysteine endopeptidase functioning in programmed cell death of Ricinus communis endosperm.” J. Mol. Biol. 336, 1103-1116.
140. Lang, R., Braun, M., Sounni, N. E., Noel, A., Frankenne, F., Foidart, J. M., Bode, W. and Maskos, K. (2004). ”Crystal structure of the catalytic domain of MMP-16/MT3-MMP: characterization of MT-MMP specific features.” J. Mol. Biol. 336, 213-225.
141. Saleh, M., Peng, W., Quinn-Allen, M. A., Macedo-Ribeiro, S., Fuentes-Prior, P., Bode, W. and Kane, W. H. (2004). ”The factor V C1 domain is involved in membrane binding: identification of functionally important amino acid residues within the C1 domain of factor V using alanine scanning mutagenesis.” Thrombosis and Haemostasis 91, 16-27.
142. Svetlitchnyi, V., Dobbek, H., Meyer-Klaucke, W., Meins, T., Thiele, B., Römer, P., Huber, R. and Meyer, O. (2004). ”A functional Ni-Ni-[4Fe-4S] cluster in the monomeric acetyl-CoA synthase from Carboxydothermus hydrogenoformans.” Proc. Natl. Acad. Sci. USA 101, 446-451.
143. Fischer, M. J., Schott, A. K., Kemter, K., Feicht, R., Richter, G., Illarionov, B., Eisenreich, W., Gerhardt, S., Cushman, M., Steinbacher, S., Huber, R. and Bacher, A. (2003). ”Riboflavin synthase of Schizosaccharomyces pombe. Protein dynamics revealed by 19F NMR protein perturbation experiments.” BMC Biochem. 4:18.
144. Kim, J. S., Kluskens, L. D., de Vos, W. M., Huber, R. and van der Oost, J. (2004). ”Crystal structure of fervidolysin from Fervidobacterium pennivorans, a keratinolytic enzyme related to subtilisin.” J. Mol. Biol. 335, 787-797.
145. Wenig, K. and Sondermann, P. (2003). ”Purification, crystallization and X-ray diffraction analysis of the extracellular part of the human Fc receptor for IgA, FcaRI (CD89).” Acta Cryst. D59, 2247-2250.
146. Breitenlechner, C., Gaßel, M., Hidaka, H., Kinzel, V., Huber, R., Engh, R. A. and Bossemeyer, D. (2003). ”Protein kinase A in complex with rho-kinase inhibitors Y-27632, fasudil, and H-1152P. Structural basis of selectivity.” Structure 11, 1595-1607.
147. Hofmann, A. and Huber, R. (2003). Liposomes in assessment of annexin-membrane interactions. Methods in Enzymology, Liposomes. N. Duzgunes. New York, Academic Press. 372: 186-216.
148. Krapp, S., Münster-Kühnel, A. K., Kaiser, J. T., Huber, R., Tiralongo, J., Gerardy-Schahn, R. and Jacob, U. (2003). ”The crystal structure of murine CMP-5-N-acetylneuraminic acid synthetase.” J. Mol. Biol. 334, 625-637.
149. Maskos, K. and Bode, W. (2003). ”Structural basis of matrix metalloproteinases and tissue inhibitors of metalloproteinases.” Molecular Biotechnology 25, 241-266.
150. Friedrich, R., Panizzi, P., Fuentes-Prior, P., Richter, K., Verhamme, I., Anderson, P. J., Kawabata, S., Huber, R., Bode, W. and Bock, P. E. (2003). ”Staphylocoagulase is a prototype for the mechanism of cofactor-induced zymogen activation.” Nature 425, 535-539.
151. Almeida, M. G., Macieira, S., Goncalves, L. L., Huber, R., Cunha, C. A., Romão, M. J., Costa, C., Lampreia, J., Moura, J. J. and I., M. (2003). ”The isolation and characterization of cytochrome c nitrite reductase subunits (NrfA and NrfH) from Desulfovibrio desulfuricans ATCC 27774.” Eur. J. Biochem. 270, 3904-3915.
152. Bode, W. (2003). Structural basis of matrix metalloproteinase function. Proteases and the Regulation of Biological Processes. J. Saklatvala, H. Nagase and G. S. Salvesen. London, Portland Press Ltd: 1-14.
153. Macieira, S., Martins, B. M. and Huber, R. (2003). ”Oxygen-dependent coproporphyrinogen-III oxidase from Escherichia coli: one-step purification and biochemical characterisation.” FEMS Microbiol. Lett. 226, 31-37.
154. Budisa, N. (2003). Expression of ’Tailor-Made’ proteins via incorporation of synthetic amino acids by using cell-free protein synthesis. Cell-Free Protein Expression. J. R. Swartz. Berlin, Springer Verlag: 89-98.
155. Ksiazek, D., Brandstetter, H., Israel, L., Bourenkov, G. P., Katchalova, G., Janssen, K. P., Bartunik, H. D., Noegel, A. A., Schleicher, M. and Holak , T. A. (2003). ”Structure of the N-terminal domain of the adenylyl cyclase-associated protein (CAP) from Dictyostelium discoideum.” Structure 11, 1171-1178.
156. Gaßel, M., Breitenlechner, C. B., Engh, R. A. and Bossemeyer, D. (2003). ”Crystal structure of an altered catalytic subunit of cAMP-dependent protein kinase in complex with the Pkc-kinase inhibitor Bisindolyl-Maleimide 2 in two different conformations – implications for selectivity.” Cellular & Molecular Biol. Lett. 8, 582.
157. Gaßel, M., Breitenlechner, C. B., De Vega S. H, Engh, R. A. and Bossemeyer, D. (2003). ”Structural insights into AGC-kinase inhibitor binding from studies with the workhorse PKA.” Cellular & Molecular Biol. Lett. 8, 508-509.
158. Barth, D., Kyrieleis, O., Frank, S., Renner, C. and Moroder, L. (2003). ”The role of cystine knots in collagen folding and stability, part II. Conformational properties of (Pro-Hyp-Gly)n model trimers with N- and C-terminal collagen type III cystine knots.” Chemistry 9, 3703-3714.
159. Engh, R. A. and Bossemeyer, D. (2002). ”Structural aspects of protein kinase control-role of conformational flexibility.” Pharmacology & Therapeutics 93, 99-111.
160. Kamionka, M., Rehm, T., Beisel, H. G., Lang, K., Engh, R. A. and Holak, T. A. (2002). ”In silico and NMR identification of inhibitors of the IGF-I and IGF-binding protein-5 interaction.” J. Med. Chem. 45, 5655-5660.
161. Regelsberger, G., Atzenhofer, W., Rüker, F., Peschek, G. A., Jakopitsch, C., Paumann, M., Furtmüller, P. G. and Obinger, C. (2002). ”Biochemical characterization of a membrane-bound manganese-containing superoxide dismutase from the cyanobacterium Anabaena PCC 7120.” J. Biol. Chem. 277, 43615-43622.
162. Worbs, M., Wahl, M. C., Lindahl, L. and Zengel, J. M. (2002). ”Comparative anatomy of a regulatory ribosomal protein.” Biochimie 84, 731-743.
163. Bertoldi, M., Cellini, B., Clausen, T. and Voltattorni, C. B. (2002). ”Spectroscopic and kinetic analyses reveal the pyridoxal 5’-phosphate binding mode and the catalytic features of Treponema denticola cystalysin.” Biochemistry 41, 9153-9164.
164. Abt, D. J., Einsle, O., Niessen, H., Krieger, R., Messerschmidt, A., Schink, B. and Kroneck, P. M. (2002). ”Crystallization and preliminary X-ray analysis of the molybdenum-dependent pyrogallol-phloroglucinol transhydroxylase of Pelobacter acidigallici.” Acta Cryst. D58, 343-345.
165. Lee, M. H., Verma, V., Maskos, K., Becherer, J. D., Knäuper, V., Dodds, P., Amour, A. and Murphy, G. (2002). ”The C-terminal domains of TACE weaken the inhibitory action of N-TIMP-3.” FEBS Lett. 520, 102-106.
166. Lee, M. H., Verma, V., Maskos, K., Nath, D., Knäuper, V., Dodds, P., Amour, A. and Murphy, G. (2002). ”Engineering N-terminal domain of tissue inhibitor of metalloproteinase (TIMP)-3 to be a better inhibitor against tumour necrosis factor-a-converting enzyme.” Biochem. J. 364, 227-234.
167. Rossoll, W., A.K., K., Ohndorf, U. M., Steegborn, C., Jablonka, S. and Sendtner, M. (2002). ”Specific interaction of Smn, the spinal muscular atrophy determining gene product, with hnRNP-R and gry-rbp/hnRNP-Q: a role for Smn in RNA processing in motor axons?” Hum. Mol. Genet. 11, 93-105. Jozic, D., Kaiser, J. T., Huber, R., Bode, W. and Maskos, K. (2003). ”X-ray structure of isoaspartyl dipeptidase from E.coli: a dinuclear zinc peptidase evolved from amidohydrolases.” J. Mol. Biol. 332, 243-256.
168. Gerhardt, S., Echt, S., Busch, M., Freigang, J., Auerbach, G., Bader, G., Martin, W. F., Bacher, A., Huber, R. and Fischer, M. (2003). ”Structure and properties of an engineered transketolase from maize.” Plant Physiology 132, 1941-1949.
169. Steinbacher, S., Schiffmann, S., Richter, G., Huber, R., Bacher, A. and Fischer, M. (2003). ”Structure of 3,4-dihydroxy-2-butanone 4-phosphate synthase from Methanococcus jannaschii in complex with divalent metal ions and the substrate ribulose 5-phosphate: Implications for the catalytic mechanism.” J. Biol. Chem. 278, 42256-42265.
170. Blaesse, M., Kupke, T., Huber, R. and Steinbacher, S. (2003). ”Structure of MrsD, an FAD-binding protein of the HFCD family.” Acta Cryst. D58, 1414-1421.
171. Breithaupt, C., Schubart, A., Zander, H., Skerra, A., Huber, R., Linington, C. and Jacob, U. (2003). ”Structural insights into the antigenicity of myelin oligodendrocyte glycoprotein.” Proc. Natl. Acad. Sci. USA 100, 9446-9451.
172. Bode, W. and Maskos, K. (2003). ”Structural basis of the matrix metalloproteinases and their physiological inhibitors, the tissue inhibitors of metalloproteinases.” Biol. Chem. 384, 863-872.
173. Wendt, K. S., Schall, I., Huber, R., Buckel, W. and Jacob, U. (2003). ”Crystal structure of the carboxyltransferase subunit of the bacterial sodium ion pump glutaconyl-coenzyme A decarboxylase.” EMBO J. 22, 3493-3502.
174. Hink-Schauer, C., Estebanez-Perpina, E., Kurschus, F. C., Bode, W. and Jenne, D. E. (2003). ”Crystal structure of the apoptosis-inducing human granzyme A dimer.” Nature Struct. Biol. 10, 535-540.
175. Gil-Parrado, S., Popp, O., Knoch, T. A., Zahler, S., Bestvater, F., Felgentrager, M., Holloschi, A., Fernandez-Montalvan, A., Auerswald, E. A., Fritz, H., Fuentes-Prior, P., Machleidt, W. and Spiess, E. (2003). [1015] ”Subcellular localization and in vivo subunit interactions of ubiquitous m-calpain.” J. Biol. Chem. 278, 16336-16346.
176. Henrich, S., Cameron, A., Bourenkov, G. P., Kiefersauer, R., Huber, R., Lindberg, I., Bode, W. and Than, M. E. (2003). ”The crystal structure of the proprotein processing proteinase furin explains its stringent specificity.” Nature Struct. Biol. 10, 520-526.
177. Gaßel, M., Breitenlechner, C. B., Rüger, P., Jucknischke, U., Schneider, T., Huber, R., Bossemeyer, D. and Engh, R. A. (2003). ”Mutants of protein kinase A that mimic the ATP-binding site of protein kinase B (AKT).” J. Mol. Biol. 329, 1021-1034.
178. Steinbacher, S., Kaiser, J., Gerhardt, S., Eisenreich, W., Huber, R., Bacher, A. and Rohdich, F. (2003). ”Crystal structure of the type II isopentenyl diphosphate:dimethylallyl diphosphate isomerase from Bacillus subtilis.” J. Mol. Biol. 329, 973-982.
179. Messerschmidt, A. (2001). Ascorbate oxidase. Handbook of Metalloproteins. A. Messerschmidt, R. Huber, T. Poulos and K. Wieghardt. Chichester, John Wiley & Sons,Ltd. 2: 1345-1358.
180. Dobbek, H., Gremer, L., Meyer, O. and Huber, R. (2001). CO dehydrogenase. Handbook of Metalloproteins. A. Messerschmidt, R. Huber, T. Poulos and K. Wieghardt. Chichester, John Wiley & Sons,Ltd. 2: 1136-1147.
181. Einsle, O. (2001). Cytochrome c nitrite redutase. Handbook of Metalloproteins. A. Messerschmidt, R. Huber, T. Poulos and K. Wieghardt. Chichester, John Wiley & Sons,Ltd. 1: 440-453.
182. Than, M. E. and Soulimane, T. (2001). ba3-Cytochrome c oxidase from Thermus thermophilus. Handbook of Metalloproteins. A. Messerschmidt, R. Huber, T. Poulos and K. Wieghardt. Chichester, John Wiley & Sons,Ltd. 1: 363-378.
183. Reuter, W. and Wiegand, G. (2001). Cytochrome c6. Handbook of Metalloproteins. A. Messerschmidt, R. Huber, T. Poulos and K. Wieghardt. Chichester, John Wiley & Sons,Ltd. 1: 87-99.
184. Declerck, N., Machius, M., Joyet, P., Wiegand, G., Huber, R. and Gaillardin, C. (2003). ”Hyperthermostabilization of bacillus licheniformis a-amylase and modulation of its stability over a 50oC temperature range.” Protein Engineering 1647, 287-293.
185. Garrido-Franco, M. (2003). ”Pyridoxine 5’-phosphate synthase: de novo synthesis of vitamin B6 and beyond.” Biochimica et Biophysica Acta 1647, 92-97.
186. Zeslawska, E., Jacob, U., Schweinitz, A., Coombs, G., Bode, W. and Madison, E. (2003). ”Crystals of urokinase type plasminogen activator complexes reveal the binding mode of peptidomimetic inhibitors.” J. Mol. Biol. 328, 109-118.
187. Bae, J. H., Rubini, M., Jung, G., Wiegand, G., Seifert, M. H., Azim, M. K., Kim, J. S., Zumbusch, A., Holak, T. A., Moroder, L., Huber, R. and Budisa, N. (2003). ”Expansion of the genetic code enables design of a novel ”Gold” class of green fluorescent proteins.” J. Mol. Biol. 328, 1071-1081.
188. Augustin, M. A., Reichert, A. S., Betat, H., Huber, R., Morl, M. and Steegborn, C. (2003). ”Crystal structure of the human CCA-adding enzyme: Insights into template-independent polymerization.” J. Mol. Biol. 328, 985-994.
189. Groll, M. and Huber, R. (2003). ”Substrate access and processing by the 20S proteasome core particle.” Int. J. of Biochem. & Cell Biol. 35, 606-616.
190. Engel, M., Hoffmann, T., Wagner, L., Wermann, M., Heiser, U., Kiefersauer, R., Huber, R., Bode, W., Demuth, H. U. and Brandstetter, H. (2003). ”The crystal structure of dipeptidyl peptidase IV (CD26) reveals its functional regulation and enzymatic mechanism.” Proc. Natl. Acad. Sci. USA 100, 5063-5068.
191. Messerschmidt, A., Worbs, M., Steegborn, C., Wahl, M. C., Huber, R., Laber, B. and Clausen, T. (2003). ”Determinants of enzymatic specificity in the Cys-Met-metabolism PLP-dependent enzymes family: Crystal structure of cystathionine g-lyase from yeast and intrafamiliar structure comparison.” Biol. Chem. 384, 373-386.
192. Song, H. K., Bochtler, M., Azim, M. K., Hartmann, C., Huber, R. and Ramachandran, R. (2003). ”Isolation and characterization of the prokaryotic proteasome homolog HslVU (ClpQY) from Thermotoga maritima and the crystal structure of HslV.” Biophys. Chem. 100, 437-452.
193. Steinbacher, S., Hernández-Acosta, P., Bieseler, B., Blaesse, M., Huber, R., Culiáñez-Macià, F. A. and Kupke, T. (2003). ”Crystal Structure of the plant PPC decarboxylase AtHAL3a complexed with an Ene-thiol reaction intermediate.” J. Mol. Biol. 327, 193-202.
194. Declerck, N., Machius, M., Joyet, P., Wiegand, G., Huber, R. and Gaillardin, C. (2002). ”Engineering the thermostability of Bacillus licheniformis a-amylase.” Biologia, Bratislava 57, 203-211.
195. Groll, M., Brandstetter, H., Bartunik, H., Bourenkow, G. and Huber, R. ”Investigations on the maturation and regulation of archaebacterial proteasomes.” J. Mol. Biol. 327, 75-83.
196. Steinbacher, S., Kaiser, J., Eisenreich, W., Huber, R., Bacher, A. and Rohdich, F. (2003). ”Structural basis of fosmidomycin action revealed by the complex with IspC:Implications for the catalytic mechanism and anti-malaria drug development.” J. Biol. Chem. 278, 18401-18407.
197. Cunha, C. A., Macieira, S., Dias, J. M., Almeida, G., Goncalves, L. L., Costa, C., Lampreia, J., Huber, R., Moura, J. J., I., M. and Romao, M. J. (2003). ”Cytochrome c nitrite reductase from Desulfovibrio desulfuricans ATCC 27774: the relevance of the two calcium sites in the structure of the catalytic subunit (NrfA).” J. Biol. Chem. 278, 17455-17465.
198. Soulimane, T., Kiefersauer, R. and Than, M. E. (2003). Ba3-Type cytochrome c oxidase from Thermus thermophilus: Purification, crystallization and crystal transformation. Membrane Protein Purification and Crystallization. C. Hunte, H. Schägger and G. v. Jagow. San Diego, Elsevier Science, USA: 229-251.
199. Lee, M. H., Dodds, P., Verma, V., Maskos, K., Knäuper, V. and Murphy, G. (2003). ”Tailoring tissue inhibitor of metalloproteinases-3 to overcome the weakening effects of the cysteine-rich domains of tumor necrosis factor-a converting enzyme.” Biochem. J. 371, 369-376.
200. Lee, M. H., Maskos, K., Knäuper, V., Dodds, P. and Murphy, G. (2002). ”Mapping and characterization of the functional epitopes of tissue inhibitor of metalloproteinases (TIMP)-3 using TIMP-1 as the scaffold: a new frontier in TIMP engineering.” Protein Science 11, 2493-2503.
201. Maskos, K., Huber-Wunderlich, M. and Glockshuber, R. (2003). ”DsbA and DsbC-catalyzed oxidative folding of proteins with complex disulfide bridge patterns in vitro and in vivo.” J. Mol. Biol. 325, 495-513.
202. Bauer, S., Kemter, K., Bacher, A., Huber, R., Fischer, M. and Steinbacher, S. (2003). ”Crystal structure of Schizosaccharomyces pombe riboflavin kinase reveals a novel ATP and riboflavin-binding fold.” J. Mol. Biol. 326, 1463-1473.
203. Fischer, M., Haase, I., Kis, K., Meining, W., Ladenstein, R., Cushman, M., Schramek, N., Huber, R. and Bacher, A. (2003). ”Enzyme catalysis via control of activation entropy: Site-directed mutagenesis of 6,7-Dimethyl-8-ribityllumazine synthase.” J. Mol. Biol. 326, 783-793.
204. Machius, M., Declerck, N., Huber, R. and Wiegand, G. (2003). ”Kinetic stabilization of Bacillus licheniformis a -amylase through introduction of hydrophobic residues at the surface.” J. Biol. Chem. 278, 11546-11553.
205. Rebelo, J., Auerbach, G., Bader, G., Bracher, A., Nar, H., Hösl, C., Schramek, N., Kaiser, J., Bacher, A., Huber, R. and Fischer, M. (2003). ”Biosynthesis of pteridines. Reaction mechanism of GTP cyclohydrolase I.” J. Mol. Biol. 326, 503-516.
206. Krapp, S., Mimura, Y., Jefferis, R., Huber, R. and Sondermann, P. (2003). ”Structural analysis of human IgG-Fc glycoforms reveals a correlation between glycosylation and structural integrity.” J. Mol. Biol. 325, 979-989.
207. Volpicella, M., Ceci, L. R., Cordewener, J., America, T., Gallerani, R., Bode, W., Jongsma, M. A. and Beekwilder, J. (2003). ”Properties of purified gut trypsin from Helicoverpa zea, adapted to proteinase inhibitors.” Eur. J. Biochem. 270, 10-19.
208. Fluhrer, R., Multhaup, G., Schlicksupp, A., Okochi, M., Takeda, M., Lammich, S., Willem, M., Westmeyer, G., Bode, W., Walter, J. and Haass, C. (2003). ”Identification of a b-secretase activity, which truncates amyloid b-peptide after its presenilin-dependent generation.” J. Biol. Chem. 278, 5531-5538.
209. Arlt, M., Kopitz, C., Pennington, C., Watson, K. L., Krell, H. W., Bode, W., Gansbacher, B., Khokha, R., Edwards, D. R. and Krüger, A. (2002). ”Increase in gelatinase-specificity of matrix metalloproteinase inhibitors correlates with antimetastatic efficacy in a T-cell lymphoma model.” Cancer Research 62, 5543-5550.
210. Hink-Schauer, C., Estebanez-Perpina, E., Wilharm, E., Fuentes-Prior, P., Klinkert, W., Bode, W. and Jenne, D. E. (2002). ”The 2.2-Å crystal structure of human Pro-granzyme K reveals a rigid zymogen with unusual features.” J. Biol. Chem. 277, 50923-50933.
211. Kim, J. S., Groll, M., Musiol, H. J., Behrendt, R., Kaiser, M., Moroder, L., Huber, R. and Brandstetter, H. (2002). ”Navigation inside a protease: substrate selection and product exit in the tricorn protease from Thermoplasma acidophilum.” J. Mol. Biol. 324, 1041-1050.
212. Dobbek, H., Gremer, L., Kiefersauer, R., Huber, R. and Meyer, O. (2002). ”Catalysis at a dinuclear [CuSMo(=O)OH] cluster in a CO dehydrogenase resolved at 1.1-Å resolution.” Proc. Natl. Acad. Sci. USA 99, 15971-15976.
213. Sichler, K., Kopetzki, E., Huber, R., Bode, W., Hopfner, K. P. and Brandstetter, H. (2003). ”Physiological fIXa activation involves a cooperative conformational rearrangement of the 99-loop.” J. Biol. Chem. 278, 4121-4126.
214. Wiegand, G., Parbel, A., Seifert, M. H., Holak, T. A. and Reuter, W. (2002). ”Purification, crystallization, NMR spectroscopy and biochemical analyses of a-phycoerythrocyanin peptides.” Eur. J. Biochem. 269, 5046-5055.
215. Rehm, T., Huber, R. and Holak, T. A. (2002). ”Application of NMR in structural proteomics: screening for proteins amenable to structural analysis.” Structure 10, 1613-1618.
216. Einsle, O., Messerschmidt, A., Huber, R., Kroneck, P. M. and Neese, F. (2002). ”Mechanism of the six-electron reduction of nitrite to ammonia by cytochrome c nitrite reductase.” J. Am. Chem. Soc. 124, 11737-11745.
217. Budisa, N., Rubini, M., Bae, J. H., Weyher, E., Wenger, W., Golbik, R., Huber, R. and Moroder, L. (2002). ”Global replacement of tryptophan with aminotryptophans generates non-invasive protein-based optical pH sensors.” Angew. Chem. Int. Ed. 41, 4066-4069.
218. Reverter, D., Braun, M., Fernandez-Catalan, C., Strobl, S., Sorimachi, H. and W., B. (2002). ”Flexibility analysis and structure comparison of two crystal forms of calcium-free human m-calpain.” Biol. Chem. 383, 1415-1422.
219. Sichler, K., Hopfner, K. P., Kopetzki, E., Huber, R., Bode, W. and Brandstetter, H. (2002). ”The influence of residue 190 in the S1 site of trypsin-like serine proteases on substrate selectivity is universally conserved.” FEBS Lett. 530, 220-224.
220. Kaiser, J. T., Bruno, S., Clausen, T., Huber, R., Schiaretti, F., Mozzarelli, A. and Kessler, D. (2003). ”Snapshots of the cystine lyase C-DES during catalysis – studies in solution and in the crystalline state.” J. Biol. Chem. 278, 357-365.
221. Gerhardt, S., Schott, A., Kairies, N., Cushman, M., Illarionov, B., Eisenreich, W., Bacher, A., Huber, R., Steinbacher, S. and Fischer, M. (2002). ”Studies on the reaction mechanism of riboflavin synthase: X-ray crystal structure of a complex with 6-carboxyethyl-7-oxo-8-ribityllumazine.” Structure 10, 1371-1381.
222. Saccà, B., Sinner, E. K., Kaiser, J. T., Lübken, C., Eble, J. A. and Moroder, L. (2002). ”Binding and docking of synthetic heterotrimeric collagen type IV peptides with a1b1 integrin.” CHEMBIOCHEM 3, 904-907.
223. Cushman, M., Yang, D., Mihalic, J. T., Chen, J., Gerhardt, S., Huber, R., Fischer, M., Kis, K. and Bacher, A. (2002). ”Incorporation of an amide into 5-phosphonoalkyl-6-D-ribitylaminopyrimidinedione lumazine synthase inhibitors results in an unexpected reversal of selectivity for riboflavin synthase vs lumazine synthase.” J. Org. Chem. 67, 6871-6877.
224. Göttig, P., Groll, M., Kim, J. S., Huber, R. and Brandstetter, H. (2002). ”Structures of the tricorn-interacting aminopeptidase F1 with different ligands explain its catalytic mechanism.” EMBO J. 21, 5343-5352.
225. Brandstetter, H., Kim, J. S., Groll, M., Göttig, P. and Huber, R. (2002). ”Structural basis for the processive protein degradation by Tricorn protease.” Biol. Chem. 383, 1157-1165.
226. Mueller, M. M., Sperl, S., Stürzebecher, J., Bode, W. and Moroder, L. (2002). ”(R)-3-Amidinophenylalanine-derived inhibitors of factor Xa with a novel active-site binding mode.” Biol. Chem. 383, 1185-1191.
227. Clausen, T., Southan, C. and Ehrmann, M. (2002). ”The HtrA family of proteases: implications for protein composition and cell fate.” Molecular Cell 10, 443-455.
228. Seifert, M. H. J., Dorota Ksiazek, D., Azim, M. K., Smialowski, P., Budisa, N. and Holak, T. A. (2002). ”Slow exchange in the chromophore of a green fluorescent protein variant.” J. Am. Chem. Soc. 124, 7932-7942.
229. Raaijmakers, H., Macieira, S., Dias, J. M., Teixeira, S., Bursakov, S., Huber, R., Moura, J. J. G., Moura, I. and Romão, M. J. (2002). ”Gene sequence and the 1.8 Å crystal structure of the tungsten-containing formate dehydrogenase from Desulfovibrio gigas.” Structure 10, 1261-1272.
230. Garrido-Franco, M., Laber, B., Huber, R. and Clausen, T. (2002). ”Enzyme-ligand complexes of pyridoxine 5’-phosphate synthase: implications for substrate binding and catalysis.” J. Mol. Biol. 321, 601-612.
231. Sichler, K., Banner, D. W., D’Arcy, A., Hopfner, K. P., Huber, R., Bode, W., Kresse, G. B., Kopetzki, E. and Brandstetter, H. (2002). ”Crystal structures of uninhibited factor VIIa link its cofactor and substrate-assisted activation to specific interactions.” J. Mol. Biol. 322, 591-603.
232. Fischer, M. J., Romisch, W., Schiffmann, S., Kelly, M., Oschkinat, H., Steinbacher, S., Huber, R., Eisenreich, W., Richter, G. and Bacher, A. (2002). ”Biosynthesis of riboflavin in Archaea. Studies on the mechanism of 3,4-dihydroxy-2-butanone 4-phosphate synthase of methanococcus jannaschii.” J. Biol. Chem. 277, 41410-41416.
233. Stabler, S. P., Steegborn, C., Wahl, M. C., Oliveriusova, J., Kraus, J. P., Allen, R. H., Wagner, C. and Mudd, S. H. (2002). ”Elevated plasma total homocysteine in severe methionine adenosyltransferase I/III deficiency.” Metabolism 51, 981-988.
234. Steiner, T., Kaiser, J. T., Marinkovic, S., Huber, R. and Wahl, M. C. (2002). ”Crystal structures of transcription factor NusG in light of its nucleic acid- and protein-binding activities.” EMBO J. 21, 4641-4653.
235. Schramek, N., Bracher, A., Fischer, M., Auerbach, G., Nar, H., Huber, R. and Bacher, A. (2002). ”Reaction mechanism of GTP cyclohydrolase I: single turnover experiments using a kinetically competent reaction intermediate.” J. Mol. Biol. 316, 829-837.
236. Sondermann, P. and Oosthuizen, V. (2002). ”X-ray crystallographic studies IgG-Fcg receptor interactions.” Biochem. Soc. Trans. 30, 481-486.
237. Gil-Parrado, S., Fernández-Montalván, A., Assfalg-Machleidt, I., Popp, O., Bestvater, F., Holloschi, A., Knoch, T. A., Auerswald, E. A., Welsh, K., Reed, J. C., Fritz, H., Fuentes-Prior, P., Spiess, E., Salvesen, G. S. and Machleidt, W. (2002). ”Ionomycin-activated calpain triggers apoptosis. A probable role for Bcl-2 family members.” J. Biol. Chem. 277, 27217-27226.
238. Jozic, D., Bourenkow, G., Bartunik, H., Scholze, H., Dive, V., Henrich, B., Huber, R., Bode, W. and Maskos, K. (2002). ”Crystal structure of the dinuclear zinc aminopeptidase PepV from Lactobacillus delbrueckii unravels its preference for dipeptides.” Structure 10, 1097-1106.
239. Mimura, Y., Ghirlando, R., Sondermann, P., Lund, J. and Jefferis, R. (2001). ”The molecular specificity of IgG-Fc interactions with Fcg receptors.” Adv. Exp. Med. Biol. 495, 49-53.
240. Fischer, M., Haase, I., Feicht, R., Richter, G., Gerhardt, S., Changeux, J. P., Huber, R. and Bacher, A. (2002). ”Biosynthesis of riboflavin 6,7-Dimethyl-8-ribityllumazine synthase of Schizosaccharomyces pombe.” Eur. J. Biochem. 269, 519-526.
241. Braun, N., Meining, W., Hars, U., Fischer, M., Ladenstein, R., Huber, R., Bacher, A., Weinkauf, S. and Bachmann, L. (2002). ”Formation of metal nanoclusters on specific surface sites of protein molecules.” J. Mol. Biol. 321, 341-353.
242. Marquardt, U., Zettl, F., Huber, R., Bode, W. and Sommerhoff, C. (2002). ”The crystal structure of human alpha1-tryptase reveals a blocked substrate-binding region.” J. Mol. Biol. 321, 491-502.
243. Atzenhofer, W., Regelsberger, G., Jacob, U., Peschek, G., Furtmuller, P., Huber, R. and Obinger, C. (2002). ”The 2.0Å resolution structure of the catalytic portion of a cyanobacterial membrane-bound manganese superoxide dismutase.” J. Mol. Biol. 321, 479-489.
244. Cushman, M., Yang, D., Gerhardt, S., Huber, R., Fischer, M., Kis, K. and Bacher, A. (2002). ”Design, synthesis, and evaluation of 6-carboxyalkyl and 6-phosphonoxyalkyl derivatives of 7-oxo-8-ribitylaminolumazines as inhibitors of riboflavin synthase and lumazine synthase.” J. Org. Chem. 67, 5807-5816.
245. Cha, H., Kopetzki, E., Huber, R., Lanzendörfer, M. and Brandstetter, H. (2002). ”Structural basis of the adaptive molecular recognition by MMP9.” J. Mol. Biol. 320, 1065-1079.
246. Renner, C., Schleicher, M., Moroder, L. and Holak, T. A. (2002). ”Practical aspects of the 2D 15N-{1H}-NOE experiment.” J. Biomol. NMR 23, 23-33.
247. Groll, M., Nazif, T., Huber, R. and Bogyo, M. (2002). ”Probing structural determinants distal to the site of hydrolysis that control substrate specificity of the 20S proteasome.” Chemistry & Biology 9, 655-662.
248. Schmidt, A. E., Padmanabhan, K., Underwood, M. C., Bode, W., Mather, T. and Bajaj, S. P. (2002). ”Thermodynamic linkage between the S1 site, the Na+ site, and the Ca2+ site in the protease domain of human activated protein C (APC).” J. Biol. Chem. 277, 28987-28995.
249. Fernandez, A. (2002). ”Time-resolved backbone desolvation and mutational hot spots in folding proteins.” Proteins: Structure, Function, and Genetics 47, 447-457.
250. Fernandez, A. (2002). ”Protein design from in silico dynamic information: the emergence of the ´turn-dock-lock´ motif.” Protein Engineering 15, 1-6.
251. Einsle, O., Stach, P., Messerschmidt, A., Klimmek, O., Simon, J., Kröger, A. and Kroneck, P. M. H. (2002). ”Crystallization and preliminary X-ray analysis of the membrane-bound cytochrome c nitrite reductase complex (NrfHA) from Wolinella succinogenes.” Acta Cryst. D58, 341-342.
252. Fuentes-Prior, P., Fujikawa, K. and Pratt, K. P. (2002). ”New insights into binding interfaces of coagulation factors V and VIII and their homologues – lessons from high resolution crystal structures.” Current Protein and Peptide Science 3, 313-339.
253. Azim, M. K. (2002). ”Dis-assembling factories in the cell: licenced to kill.” Humboldt Kosmos 79, 33-34.
254. Friedrich, R., Steinmetzer, T., Huber, R., Stürzebecher, J. and Bode, W. (2002). ”The methyl group of Na(Me)Arg-containing peptides disturbs the active-site geometry of thrombin, impairing efficient cleavage.” J. Mol. Biol. 316, 869-874.
255. Ramachandran, R., Hartmann, C., Song, H. K., Huber, R. and Bochtler, M. (2002). ”Functional interactions of HslV (ClpQ) with the ATPase HslU (ClpY).” Proc. Natl. Acad. Sci. USA 99, 7396-7401.
256. Comellas-Bigler, M., Fuentes-Prior, P., Maskos, M., Huber, R., Oyama, H., Uchida, K., Dunn, B. M., Oda, K. and Bode, W. (2002). ”The 1.4 Å crystal structure of kumamolysin: a thermostable serine-carboxyl-type proteinase.” Structure 10, 865-876.
257. Gerhardt, S., Haase, I., Steinbacher, S., Kaiser, J. T., Cushman, M., Bacher, A., Huber, R. and Fischer, M. (2002). ”The structural basis of riboflavion binding to Schizosaccharomyces pombe 6,7-Dimethyl-8-ribityllumazine synthase.” J. Mol. Biol. 318, 1317-1329.
258. Sondermann, P. and Oosthuizen, V. (2002). ”The structure of Fc receptor/Ig complexes: considerations on stoichiometry and potential inhibitors.” Immunology Letters 82, 51-56.
259. Than, M. E., Henrich, S., Huber, R., Ries, A., Mann, K., Kühn, K., Timpl, R., Bourenkov, G. P., Bartunik, H. D. and Bode, W. (2002). ”The 1.9-Å crystal structure of the noncollagenous (NC1) domain of human placenta collagen IV shows stabilization via a novel type of covalent Met-Lys cross-link.” Proc. Natl. Acad. Sci. USA 99, 6607-6612.
260. Seifert, M. H., Breitenlechner, C. B., Bossemeyer, D., Huber, R., Holak, T. A. and Engh, R. A. (2002). ”Phosphorylation and flexibility of cyclic-AMP-dependent protein kinase (PKA) using 31P NMR spectroscopy.” Biochemistry 41, 5968-5977.
261. Garrido-Franco, M., Ehlert, S., Messerschmidt, A., Marinkovic, S., Huber, R., Laber, B., Bourenkov, G. P. and Clausen, T. (2002). ”Structure and function of threonine synthase from yeast.” J. Biol. Chem. 277, 12396-12405.
262. Klein, C., Planker, E., Diercks, T., Kessler, H., Künkele, K. P., Lang, K., Hansen, S. and Schwaiger, M. (2001). ”NMR spectroscopy reveals the solution dimerization interface of p53 core domains bound to their consensus DNA.” J. Biol. Chem. 276, 49020-49027.
263. Wahl, M. C. and Möller, W. (2002). ”Structure and function of the acidic ribosomal stalk proteins.” Current Protein and Peptide Science 3, 93-106.
264. Renner, C., Moroder, L. and Holak, T. A. (2001). ”Analytical solution to the Lipari-Szabo model based on the reduced spectral density approximation offers a novel protocol for extracting motional parameters.” Journal of Magnetic Resonance 151, 32-39.
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266. Grams, F., Brandstetter, H., D’Alo, S., Geppert, D., Krell, H. W., Leinert, H., Livi, V., Menta, E., Oliva, A. and Zimmermann, G. (2001). ”Pyrimidine-2,4,6-triones: a new effective and selective class of matrix metalloproteinase inhibitors.” Biol. Chem. 383, 1277-1285.
267. Fernandez, A. (2001). ”Protein folding cooperativity in the correlated lattice.” Physics Letters A 290, 101-105.
268. Fernandez, A., Colubri, A. and Appignanesi, G. (2001). ”Semiempirical prediction of protein folds.” Physical Review E 64, art.no. 021901.
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272. Renner, C. and Holak, T. A. (2001). ”NMR 15N relaxation of the insulin-like growth factor (IGF)-binding domain of IGF binding protein-5 (IGFBP-5) determined free in solution and in complex with IGF-II.” Eur. J. Biochem. 268, 1058-1065.
273. Kupke, T., Hernández-Acosta, P., Steinbacher, S. and Culiáñez-Macià, F. A. (2001). ”Arabodopsis thaliana flavoprotein AtHAL3a catalyzes the decarboxylation of 4’-phosphopantothenoylcysteine to 4’-phosphopantetheine, a key step in coenzyme a biosynthesis.” J. Biol. Chem. 276, 19190-19196.
274. Imamura, T., Banbula, A., Pereira, P. J. B., Travis, J. and Potempa, J. (2001). ”Activation of human prothrombin by arginine-specific cysteine proteinases (Gingipains R) from Porphyromonas gingivalis.” J. Biol. Chem. 276, 18984-18991.
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276. Schröder, J., Henke, A., Wenzel, H., Brandstetter, H., Stammler, H. G., Stammler, A., Pfeiffer, W. D. and Tschesche, H. (2001). ”Structure-based design and synthesis of potent matrix metalloproteinase inhibitors derived from a 6H-1,3,4-thiadiazine scaffold.” J. Med. Chem. 44, 3231-3243.
277. Köhler, A., Bajorek, M., Groll, M., Moroder, L., Rubin, D. M., Huber, R., Glickmann, M. and Finley, D. (2001). ”The substrate translocation channel of the proteasome.” Biochimie 83, 325-332.
278. Dobbek, H. and Huber, R. (2002). The molybdenum and tungsten cofactors: a crystallographic view. metal ions in biological systems. A. Sigel and H. Sigel. New York, Marcel Dekker, Inc. 39: 227-263.
279. Krojer, T., Garrido-Franco, M., Huber, R., Ehrmann, M. and Clausen, T. (2002). ”Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine.” Nature 416, 455-459.
280. Kaiser, M., Groll, M., Renner, C., Huber, R. and Moroder, L. (2002). ”The core structure of TMC-95A is a promising lead for reversible proteasome inhibition.” Angew. Chem. Int. Ed. 41, 780-783.
281. van Amsterdam, I. M. C., Ubbink, M., Einsle, O., Messerschmidt, A., Merli, A., Cavazzini, D., Rossi, G. L. and Canters, G. W. (2002). ”Dramatic modulation of electron transfer in protein complexes by crosslinking.” Nature Struct. Biol. 9, 48-52.
282. Richardson, J. L., Fuentes-Prior, P., Sadler, J. E., Huber, R. and Bode, W. (2002). ”Characterization of the residues involved in the human a-thrombin-haemadin complex: an exosite II-binding inhibitor.” Biochemistry 41, 2535-2542.
283. Grazulis, S., Deibert, M., Rimseliene, R., Skirgaila, R., Sasnauskas, G., Lagunavicius, A., Repin, V., Urbanke, C., Huber, R. and Siksnys, V. (2002). ”Crystal structure of the Bse634I restriction endonuclease: comparison of two enzymes recognizing the same DNA sequence.” Nucleid Acids Research 30, 876-885.
284. Steinbacher, S., Kaiser, J., Wungsintaweekul, J., Hecht, S., Eisenreich, W., Gerhardt, S., Bacher, A. and Rohdich, F. (2002). ”Structure of 2C-Methyl-D-erythritol-2,4-cyclodiphosphate synthase involved in mevalonate-independent biosynthesis of isoprenoids.” J. Mol. Biol. 316, 79-88.
285. Friedrich, R., Fuentes-Prior, P., Ong, E., Coombs, G., Hunter, M., Oehler, R., Pierson, D., Gonzalez, R., Huber, R. and Bode, W. (2002). ”Catalytic domain structures of MT-SP1/matriptase, a matrix-degrading transmembrane serine proteinase.” J. Biol. Chem. 277, 2160-2168.
286. Riedl, S. J., Fuentes-Prior, P., Renatus, M., Kairies, N., Krapp, S., Huber, R., Salvesen, G. S. and Bode, W. (2001). ”Structural basis for the activation of human procaspase-7.” Proc. Natl . Acad. Sci. USA 98, 14790-14795.
287. Bader, G., Schiffmann, S., Herrmann, A., Fischer, M., Gütlich, M., Auerbach, G., Ploom, T., Bacher, A., Huber, R. and Lemm, T. (2001). ”Crystal structure of rat GTP cyclohydrolase I feedback regulatory protein, GFRP.” J. Mol. Biol. 312, 1051-1057.
288. Lang, R., Kocourek, A., Braun, M., Tschesche, H., Huber, R., Bode, W. and Maskos, K. (2001). ”Substrate specificity determinants of human macrophage elastase (MMP-12) based on the 1.1 Å crystal structure.” J. Mol. Biol. 312, 731-742.
289. Kairies, N., Beisel, H. G., Fuentes-Prior, P., Tsuda, R., Muta, T., Iwanaga, S., Bode, W., Huber, R. and Kawabata, S. (2001). ”The 2.0-Å crystal structure of tachylectin 5A provides evidence for the common origin of the innate immunity and the blood coagulation systems.” Proc. Natl. Acad. Sci. USA 98, 13519-13524.
290. Bochtler, M., Song, H. K., Hartmann, C., Ramachandran, R. and Huber, R. (2001). ”The quaternary arrangement of HslU and HslV in a cocrystal: a response to Wang, Yale.” J. Struct. Biol. 135, 281-293.
291. Mimura, Y., Sondermann, P., Ghirlando, R., Lund, J., Young, S., Goodall, M. and Jefferis, R. (2001). ”Role of oligosaccharide residues of IgG1-FcgRIIb binding.” J. Biol. Chem. 276, 45539-45547.
292. Maenaka, K., van der Merve, P. A., Stuart, D. I., Y., J. E. and Sondermann, P. (2001). ”The human low affinity Fcg receptors IIa, IIb, and III bind IgG with fast kinetics and distinct thermodynamic properties.” J. Biol. Chem. 276, 44898-44904.
293. Song, H. K., Mulrooney, S. B., Huber, R. and Hausinger, R. P. (2001). ”Crystal structure of Klebsiella aerogenes UreE, a nickel-binding metallochaperone for urease activation.” J. Biol. Chem. 276, 49359-49364.
294. Brandstetter, H., Kim, J. S., Groll, M. and Huber, R. (2001). ”Crystal structure of the tricorn protease reveals a protein disassembly line.” Nature 414, 466-470.
295. Macedo-Ribeiro, S., Martins, B. M., Pereira, P. J., Buse, G., Huber, R. and Soulimane, T. (2001). ”New insights into the thermostability of bacterial ferredoxins: high-resolution crystal structure of the seven-iron ferredoxin from Thermus thermophilus.” J Biol. Inorg. Chem.. 6, 663-674.
296. Martins, B. M., Grimm, B., Mock, H. P., Richter, G., Huber, R. and Messerschmidt, A. (2001). ”Tobacco uroporphyrinogen-III decarboxylase: characterization, crystallization and preliminary X-rax analysis.” Acta Cryst. Biological Crystallography D57, 1709-1711.
297. Martins, B. M., Grimm, B., Mock, H. P., Huber, R. and Messerschmidt, A. (2001). ”Crystal structure and substrate binding modeling of the uroporphyrinogen-III decarboxylase from Nicotiana tabacum.” J. Biol. Chem. 276, 44108-44116.
298. Steegborn, C., Danot, O., Huber, R. and Clausen, C. (2001). ”Crystal structure of transcription factor MaIT domain III: a novel helix repeat fold implicated in regulated oligomerization.” Structure 9, 1051-1060.
299. Ullrich, T. C. and Huber, R. (2001). ”The complex structures of ATP sulfurylase with thiosulfate, ADP and chlorate reveal new insights in inhibitory effects and the catalytic cycle.” J. Mol. Biol. 313, 1117-1125.
300. Estébanez-Perpiña, E., Bayés, A., Vendrell, J., Jongsma, M. A., Bown, D. P., Gatehouse, J. A., Huber, R., Bode, W., Avilés, F. X. and Reverter, D. (2001). ”Crystal structure of a novel mid-gut procarboxypeptidase from the cotton pest Helicoverpa armigera.” J. Mol. Biol. 313, 629-638.
301. Reverter, D., Sorimachi, H. and Bode, W. (2001). ”The structure of calcium-free human m-calpain. Implications for calcium activation and function.” Trends Cardiovasc. Med. 11, 222-229.
302. Klein, C., Georges, G., Künkele, K. P., Huber, R., Engh, R. A. and Hansen, S. (2001). ”High thermostability and lack of cooperative DNA binding distinguish the p63 core domain from the homologous tumor suppressor p53.” J. Biol. Chem. 276, 37390-37401.
303. Steinbacher, S. and Ditzel, L. (2001). ”Review: Nucleotide binding to the Thermoplasma Thermosome: implications for the functional cycle of group II chaperonins.” J. Struct. Biol. 135, 147-156.
304. Kawabata, S., Beisel, H. G., Huber, R., Bode, W., Gokudan, S., Muta, T., Tsuda, R., Koori, K., Kawahara, T., Seki, N., Mizunoe, Y., Wai, S. N. and Iwanaga, S. (2001). Role of tachylectins in host defense of the japanese horseshoe crab Tachypleus Tridentatus. Phylogenetic Perspectives on the Vertebrate Immune System. Beck, Kluwer Academic/Plenum Publishers: 195-202.
305. Groll, M., Koguchi, Y., Huber, R. and Kohno, J. (2001). ”Crystal structure of the 20 S proteasome: TMC-95A complex: a non-covalent proteasome inhibior.” J. Mol. Biol. 311, 543-548.
306. Groll, M. and Coux, O. (2001). Proteasomes. Proteinase and Peptidase Inhibition: Recent Potential Targets for Drug Development. H. J. Smith and C. Simons. Amsterdam, Harwood Academic Publishers.
307. Steegborn, C., Laber, B., Messerschmidt, A., Huber, R. and Clausen, T. (2001). ”Crystal structures of cystathionine g-synthase inhibitor complexes rationalize the increased affinity of a novel inhibitor.” J. Mol. Biol. 311, 789-801.
308. Golbik, R., Budisa, N., Renner, C., Weyher-Stingl, E., Rahfeld, J. U., Huber, R., Fischer, G. and Moroder, L. (2001). ”Studies on folding of fluoroproline-substituted variants of Barstar.” Nova Acta Leopoldina Supplementum 16, 59-60.
309. Wendt, K. S., Vodermaier, H. C., Jacob, U., Gieffers, C., Gmachl, M., Peters, J. M., Huber, R. and Sondermann, P. (2001). ”Crystal structure of the APC10/DOC1 subunit of the human anaphase-promoting complex.” Nature Struct. Biol. 8, 784-788.
310. Izumi, T., Kim, S. W., Greist, A., Macedo-Ribeiro, S., Fuentes-Prior, P., Bode, W., Kane, W. H. and Ortel, T. L. (2001). ”Fine mapping of inhibitory anti-factor V antibodies using factor V C2 domain mutants.” Thromb. Haemost. 85, 1048-1054.
311. Budisa, N., Alefelder, S., Bae, J. H., Golbik, R., Minks, C., Huber, R. and Moroder, L. (2001). ”Proteins with b-(thienopyrrolyl)alanines as alternative chromophores and pharmaceutically active amino acids.” Protein Science 10, 1281-1292.
312. Dobbek, H., Svetlitchnyi, V., Gremer, L., Huber, R. and Meyer, O. (2001). ”Crystal structure of a carbon monoxide dehydrogenase reveals a [Ni-4Fe-5S] cluster.” Science 293, 1281-1285.
313. Engh, R. A. and Huber, R. (2001). Structure quality and target parameters. International Tables for Crystallography, Volume F. Crystallography of Biological Macromolecules. M. G. Rossmann and E. Arnold. Dordrecht, The Netherlands, Kluwer Academic Publishers: 382-392.
314. Stubbs, M. T. and Huber, R. (2001). Isomorphous replacement. Locating heavy atom sites. International Tables for Crystallography, Volume F. Crystallography of Biological Macromolecules. M. G. Rossmann and E. Arnold. Dordrecht, The Netherlands, Kluwer Academic Publishers: 256-262.
315. Ohndorf, U. M., Steegborn, C., Knijff, R. and Sondermann, P. (2001). ”Contributions of the individual domains in human La Protein to its RNA 3’-end binding activity.” J. Biol. Chem. 276, 27188-27196.
316. Gabashvili, I. S., Gregory, S. T., Valle, M., Grassucci, R., Worbs, M., Wahl, M. C., Dahlberg, A. E. and Frank, J. (2001). ”The polypeptide tunnel system in the ribosome and its gating in Erythromycin resistance mutants of L4 and L22.” Molecular Cell 8, 181-188.
317. Bae, J. H., Alefelder, S., Kaiser, J. T., Friedrich, R., Moroder, L., Huber, R. and Budisa, N. (2001). [ "Incorporation of b-Selenolo[3,2-b]pyrrolyl-alanine into proteins for phase determination in protein X-ray crystallography.” J. Mol. Biol. 309, 925-936.
318. Einsle, O. (2001). ”Struktur und Funktion der Cytochrom c-Nitritreduktase.” Biospektrum 4/01, 361.
319. Sondermann, P., Kaiser, J. and Jacob, U. (2001). ”Molecular basis for immune complex recognition: a comparison of Fc-receptor structures.” J. Mol. Biol. 309, 737-749.
320. Breitinger, U., Clausen, T., Ehlert, S., Huber, R., Laber, B., Schmidt, F., Pohl, E. and Messerschmidt, A. (2001). ”The three-dimensional structure of cystathionine b-lyase from Arabidopsis and its substrate specificity.” Plant Physiology 126, 631-642.
321. Rester, U., Bode, W., Sampaio, C., Auerswald, E. and Lopes, A. (2001). ”Cloning, purification, crystallization and preliminary X-ray diffraction analysis of the antistasin-type inhibitor ghilanten (domain I) from Haementeria ghilianii in complex with porcine b-trypsin.” Acta Cryst. D57, 1038-1041.
322. Rebelo, J. M., Dias, J. M., Huber, R., Moura, J. J. G. and Romão, M. J. (2001). ”Structure refinement of the aldehyde oxidoreductase from Desulfovibrio gigas (MOP) at 1.28 Å.” J. Biol. Inorg. Chem 6, 791-800.
323. Reverter, D., Strobl, S., Fernandez-Catalan, C., Sorimachi, H., Suzuki, K. and Bode, W. (2001). ”Structural basis for possible calcium-induced activation mechanisms of calpains.” Biol. Chem. 382, 753-766.
324. Einsle, O., Foerster, S., Mann, K., Fritz, G., Messerschmidt, A. and Kroneck, P. M. H. (2001). ”Spectroscopic investigation and determination of reactivity and structure of the tetraheme cytochrome c3 from Desulvovibrio desulfuricans Essex 6.” Eur. J. Biochem. 268, 3028-3035.
325. Bode, W. and Maskos, K. (2001). Structural Studies on MMPs and TIMPs. Methods in Molecular Biology – Matrix Metalloproteinase Protocols. I. M. Clark. Totowa, New Jersey, Humana Press. 151: 45-77.
326. van Amsterdam, I., Ubbink, M., Jeuken, L., Verbeet, M., Einsle, O., Messerschmidt, A. and Canters, G. W. (2001). ”Effects of dimerization on protein electron transfer.” Chem. Eur. J. 7, 2398-2406.
327. Zeslawski, W., Beisel, H. G., Kamionka, M., Kalus, W., Engh, R. A., Huber, R., Lang, K. and Holak, T. A. (2001). ”The interaction of insulin-like growth factor-I with the N-terminal domain of IGFBP-5.” EMBO J. 20, 3638-3644.
328. Worbs, M., Bourenkov, G. P., Bartunik, H., Huber, R. and Wahl, M. C. (2001). ”An extended RNA binding surface through arrayed S1 and KH domains in transcription factor NusA.” Molecular Cell 7, 1177-1189.
329. Brandstetter, H., Grams, F., Glitz, D., Lang, A., Huber, R., Bode, W., Krell, H. W. and Engh, R. A. (2001). ”The 1.8- Å crystal structure of a matrix metalloproteinase 8-barbiturate inhibitor complex reveals a previously unobserved mechanism for collagenase substrate recognition.” J. Biol. Chem. 276, 17405-17412.
330. Breithaupt, C., Strassner, J., Breitinger, U., Huber, R., Macheroux, P., Schaller, A. and Clausen, T. (2001). ”X-ray structure of 12-oxophytodienoate reductase 1 provides structural insight into substrate binding and specificity within the family of OYE.” Structure 9, 419-429.
331. Schaschke, N., Loidl, G., Groll, M., Matschiner, G., Zettl, F., Sommerhoff, C. P., Marquardt, U., Bode, W., Huber, R. and Moroder, L. (2001). Multivalent Inhibition of Eukaryotic Proteasome and Human b-tryptase. Peptides 2000. J. Martinez and J. A. Fehrentz. Paris, EDK: 7-13.
332. Schaschke, N., Matschiner, G., Zettl, F., Marquardt, U., Bergner, A., Bode, W., Sommerhoff, C. P. and Moroder, L. (2001). ”Bivalent inhibition of human b-tryptase.” Chemistry & Biology 8, 313-327.
333. Dorowski, A., Hofmann, A., Steegborn, C., Boicu, M. and Huber, R. (2001). ”Crystal structure of paprika ferredoxin-NADP+ reductase.” J. Biol. Chem. 276, 9253-9263.
334. Stoll, R., Renner, C., Zweckstetter, M., Brüggert, M., Ambrosius, D., Palme, S., Engh, R. A., Golob, M., Breibach, I., Buettner, R., Voelter, W., Holak, T. A. and Bosserhoff, A. K. (2001). ”The extracellular human melanoma inhibitory activity (MIA) protein adopts an SH3 domain-like fold.” EMBO J. 20, 340-349.
335. Renner, C., Alefelder, S., Bae, J. H., Budisa, N., Huber, R. and Moroder, L. (2001). ”Fluoroprolines as tools for protein design and engineering.” Angew. Chem. Int. Ed. 40, 923-925.
336. Garrido-Franco, M., Laber, B., Huber, R. and Clausen, T. (2001). ”Structural basis for the function of pyridoxine 5’- phosphate synthase.” Structure 9, 245-253.
337. Ullrich, T. C., Blaesse, M. and Huber, R. (2001). ”Crystal structure of ATP sulfurylase from Saccharomyces cerevisiae, a key enzyme in sulfate activation.” EMBO J. 20, 316-329.
338. Steegborn, C. and Clausen, T. (2000). ”Specific inhibition of transsulfuration enzymes.” Recent Res. Devel. Biochem. 2, 191-207.
339. Stoll, R., Renner, C., Hansen, S., Palme, S., Klein, C., Belling, A., Zeslawski, W., Kamionka, M., Rehm, T., Mühlhahn, P., Schumacher, R., Hesse, F., Kaluza, B., Voelter, W., Engh, R. A. and Holak, T. A. (2001). ”Chalcone derivatives antagonize interactons between the human oncoprotein MDM2 and p53.” Biochemistry 40, 336-344.
340. Soulimane, T., Than, M. E., Dewor, M., Huber, R. and Buse, G. (2000). ”Primary structure of a novel subunit in ba3-cytochrome oxidase from Thermus thermophilus.” Protein Science 9, 2068-2073.
341. Auerbach, G., Herrmann, A., Bracher, A., Bader, G., Gütlich, M., Fischer, M., Neukamm, M., Garrido-Franco, M., Richardson, J., Nar, H., Huber, R. and Bacher, A. (2000). ”Zinc plays a key role in human and bacterial GTP cyclohydrolase I.” Proc. Natl. Acad. Sci. USA 97, 13567-13572.
342. Bochtler, M., Hartmann, C., Song, H. K., Ramachandran, R. and Huber, R. (2000). ”Docking of components in a bacterial complex – Reply.” Nature 408, 668-668.
343. Estébanez-Perpiñá, E., Fuentes-Prior, P., Belorgey, D., Braun, M., Kiefersauer, R., Maskos, K., Huber, R., Rubin, H. and Bode, W. (2000). ”Crystal structure of the caspase activator human granzyme B, a proteinase highly specific for an Asp-P1 residue.” Biol. Chem. 381, 1203-1214.
344. Augustin, M. A., Huber, R. and Kaiser, J. T. (2001). ”Crystal structure of a DNA-dependent RNA polymerase (DNA primase).” Nature Struct. Biol. 8, 57-61.
345. Einsle, O., Stach, P., Messerschmidt, A., Simon, J., Kröger, A., Huber, R. and Kroneck, P. (2000). ”Cytochrome c Nitrite Reductase from Wolinella succinogenes.” J. Biol. Chem. 275, 39608-39616.
346. Song, H. K., Hartmann, C., Ramachandran, R., Bochtler, M., Behrendt, R., Moroder, L. and Huber, R. (2000). ”Mutational studies on HslU and its docking mode with HslV.” Proc. Natl. Acad. Sci. USA 97, 14103-14108.
347. Minks, C., Alefelder, S., Moroder, L., Huber, R. and Budisa, N. (2000). ”Towards new protein engineering: In vivo building and folding of protein shuttles for drug delivery and targeting by the selective pressure incorporation (SPI) method.” Tetrahedron 56, 9431-9442.
348. Garbuglia, M., Verzini, M., Hofmann, A., Huber, R. and Donato, R. (2000). ”S100A1 and S100B interactions with annexins.” Biochimica et Biophysica Acta 1498, 192-206.
349. Blaesse, M., Kupke, T., Huber, R. and Steinbacher, S. (2000). ”Crystal structure of the peptidyl-cysteine decarboxylase EpiD complexed with a pentapeptide substrate.” EMBO J. 19, 6299-6310.
350. Einsle, O., Mehrabian, Z., Nalbandyan, R. and Messerschmidt, A. (2000). ”Crystal structure of plantacyanin, a basic blue cupredoxin from spinach.” J. Biol. Inorg. Chem. 5, 666-672.
351. Ottl, J., Gabriel, D., Bode, W. and Moroder, L. (2000). Heterotrimeric collagen peptides as substrates of metalloproteinases. 16th American Peptide Symposium-Peptides for the New Millennium, Minneapolis, Kluwer Academic Publishers Dordrecht.
352. Sperl, S., Bergner, A., Stürzebecher, J., Magdolen, V., Bode, W. and Moroder, L. (2000). [ "Urethanyl-3-amidinophenylalanine derivatives as inhibitors of factor Xa. X-ray crystal structure of a trypsin/inhibitor complex and modeling studies." Biol. Chem. 381, 321-329.
353. Sommerhoff, C. P., Bode, W., Matschiner, G., Bergner, A. and Fritz, H. (2000). "The human mast cell tryptase tetramer: a fascinating riddle solved by structure." Biochimica et Biophysica Acta 1477, 75-89.
354. Kim, S. W., Quinn-Allen, M. A., Camp, J. T., Macedo-Ribeiro, S., Fuentes-Prior, P., Bode, W. and Kane, W. H. (2000). "Identification of functionally important amino acid residues within the C2-domain of human factor V using alanine-scanning mutagenesis." Biochemistry 39, 1951-1958.
355. Messerschmidt, A. and Huber, R. (2000). X-ray Crystallography of Biological Macromolecules. Encyclopedia of Analytical Chemistry. R. A. Meyers. Cichester, John Wiley & Sons Ltd.: 6061-6107.
356. Groll, M., Bajorek, M., Köhler, A., Moroder, L., Rubin, D. M., Huber, R., Glickman, M. H. and Finley, D. (2000). "A gated channel into the proteasome core particle." Nature Struct. Biol. 7, 1062-1067.
357. Meyer, O., Gremer, L., Ferner, R., Ferner, M., Dobbek, H., Gnida, M., Meyer-Klaucke, W. and Huber, R. (2000). "The role of Se, Mo and Fe in the structure and function of carbon monoxide dehydrogenase." Biol. Chem. 381, 865-876.
358. Hänzelmann, P., Dobbek, H., Gremer, L., Huber, R. and Meyer, O. (2000). "The effect of intracellular molybdenum in Hydrogenophaga pseudoflava on the crystallographic structure of the seleno-molybdo-iron-sulfur flavoenzyme carbon monoxide dehydrogenase." J. Mol. Biol. 301, 1221-1235.
359. Richardson, J. L., Kröger, B., Hoeffken, W., Sadler, J. E., Pereira, P., Huber, R., Bode, W. and Fuentes-Prior, P. (2000). "Crystal structure of the human a-thrombin-haemadin complex: an exosite II-binding inhibitor." EMBO J. 19, 5650-5660.
360. Declerck, N., Machius, M., Wiegand, G., Huber, R. and Gaillardin, C. (2000). "Probing structural determinants specifying high thermostability in Bacillus licheniformis a-amylase." J. Mol. Biol. 301, 1041-1057.
361. Kupke, T., Uebele, M., Schmid, D., Jung, G., Blaesse, M. and Steinbacher, S. (2000). "Molecular characterization of lantibiotic-synthesizing enzyme EpiD reveals a function for bacterial Dfp proteins in coenzyme A biosynthesis." J. Biol. Chem. 275, 31838-31846.
362. Schaschke, N., Loidl, G., Groll, M., Matschiner, G., Sommerhoff, C. P., Bode, W., Huber, R. and Moroder, L. (2000). "Bivalent inhibition of multicatalytic enzyme complexes." 8th Akabori Conference Japanese-German Symposium on Peptide Science T. Shioiri, 159-164. Akabori Conference Association Nagoya, Japan.
363. Huber, R. (2000). "Gene: Rätsel ohne Ende?" Aviso 4/2000, 16-22.
364. Deibert, M., Grazulis, S., Sasnauskas, G., Siksnys, V. and Huber, R. (2000). "Structure of the tetrameric restriction endonuclease NgoMIV in complex with cleaved DNA." Nature Struct. Biol. 7, 792-799.
365. Kiefersauer, R., Than, M. E., Dobbek, H., Gremer, L., Melero, M., Strobl, S., Dias, J. M., Soulimane, T. and Huber, R. (2000). "A novel free-mounting system for protein crystals: transformation and improvement of diffraction power by accurately controlled humidity changes." J. Appl. Cryst. 33, 1223-1230.
366. Zeslawska, E., Schweinitz, A., Karcher, A., Sondermann, P., Sperl, S., Stürzebecher, J. and Jacob, U. (2000). "Crystals of the urokinase type plasminogen activator variant bc-uPa in complex with small molecule inhibitors open the way towards structure-based drug design." J. Mol. Biol. 301, 465-475.
367. Minks, C., Huber, R., Moroder, L. and Budisa, N. (2000). "Noninvasive tracing of recombinant proteins with "Fluorophenylalanine-Fingers"." Analytical Biochemistry 284, 29-34.
368. Sondermann, P., Huber, R., Oosthuizen, V. and Jacob, U. (2000). "The 3.2-Å crystal structure of the human IgG1 Fc fragment-FcgRIII complex." Nature 406, 267-273.
369. Garrido-Franco, M., Huber, R., Schmidt, F. S., Laber, B. and Clausen, T. (2000). "Crystallization and preliminary X-ray crystallographic analysis of PdxJ, the pyridoxine 5'-phosphate synthesizing enzyme." Acta Cryst. D56, 1045-1048.
370. Krupka, H. I., Huber, R., Holt, S. C. and Clausen, T. (2000). "Crystal structure of cystalysin from Treponema denticola: a pyridoxal 5'-phosphate-dependent protein acting as a haemolytic enzyme." EMBO J. 19, 3168-3178.
371. Soulimane, T., Buse, G., Bourenkov, G. P., Bartunik, H. D., Huber, R. and Than, M. E. (2000). "Structure and mechanism of the aberrant ba3-cytochrome c oxidase from Thermus thermophilus." EMBO J. 19, 1766-1776.
372. Clausen, T., Kaiser, J. T., Steegborn, T., Huber, R. and Kessler, D. (2000). "Crystal structure of the cystine C-S lyase from Synechocystis: Stabilization of cysteine persulfide for FeS cluster biosynthesis." Proc. Natl. Acad. Sci. USA 97, 3856-3861.
373. Theodoratu, E., Paschos, A., Magalon, A., Fritsche, E., Huber, R. and Böck, A. (2000). "Nickel serves as a substrate recognition motif for the endopeptidase involved in hydrogenase maturation." Eur. J. Biochem. 267, 1995-1999.
374. Sperl, S., Jacob, U., de Prada, N. A., Stürzebecher, J., Wilhelm, O. G., Bode, W., Magdolen, V., Huber, R. and Moroder, L. (2000). "(4-Aminomethyl)phenylguanidine derivatives as nonpeptidic highly selective inhibitors of human urokinase." Proc. Natl. Acad. Sci. USA 97, 5113-5118.
375. Huber, R. (2000). "Warum sind die Blätter an den Bäumen grün." SZ Magazin 20/2000, 20-21.
376. Worbs, M. and Wahl, M. C. (2000). "Expression, purification, crystallization and preliminary X-ray diffraction studies of bacterial and archaeal L4 ribosomal proteins." Acta Cryst. D56, 645-647.
377. Rester, U., Moser, M., Huber, R. and Bode, W. (2000). "L-Isoaspartate 115 of porcine b-trypsin promotes crystallization of its complex with bdellastasin." Acta Cryst. D56, 581-588.
378. Reverter, D., Fernandez-Catalan, C., Baumgartner, R., Pfänder, R., Huber, R., Bode, W., Vendrell, J., Holak, T. A. and Avilés, F. X. (2000). "Structure of a novel leech carboxypeptidase inhibitor determined free in solution and in complex with human carboxypeptidase A2." Nature Struct. Biol. 7, 322-328.
379. Fuentes-Prior, P., Iwanaga, Y., Huber, R., Pagila, R., Rumennik, G., Seto, M., Morser, J., Light, D. R. and Bode, W. (2000). "Structural basis for the anticoagulant activity of the thrombin-thrombomodulin complex." Nature 404, 518-525.
380. Loidl, G., Musiol, H. J., Budisa, N., Huber, R., Poirot, S., Fourmy, D. and Moroder, L. (2000). "Synthesis of b-(1-azulenyl)-L-alanine as a potential blue-colored fluorescent tryptophan analog and its use in peptide synthesis." J. Peptide Sci. 6, 139-144.
381. van Gastel, M., Canters, G. W., Krupka, H., Messerschmidt, A., de Waal, E. C., Warmerdam, G. C. M. and Groenen, E. J. J. (2000). "Axial ligation in blue-copper proteins. A w-band electron spin echo detected electron paramagnetic resonance study of the azurin mutant M121H." J. Am. Chem. Soc. 122, 2322-2328.
382. Hofmann, A., Raquénès-Nicol, C., Favier-Perron, B., Mesonero, J., Huber, R., Russo-Marie, F. and Lewit-Bentley, A. (2000). "The annexin A3-membrane interaction is modulated by an N-terminal tryptophan." Biochemistry 39, 7712-7721.
383. Dams, T., Auerbach, G., Bader, G., Jacob, U., Ploom, T., Huber, R. and Jaenicke, R. (2000). "The crystal structure of dihydrofolate reductase from thermotoga maritima: molecular features of thermostability." J. Mol. Biol. 297, 659-672.
384. Thöny, B., Auerbach, G. and Blau, N. (2000). "Tetrahydrobiopterin biosynthesis, regeneration and functions." Biochem. J. 347, 1-16.
385. Bode, W. and Huber, R. (2000). "Structural basis of the endoproteinase-protein inhibitor interaction." Biochimica et Biophysica Acta 1477, 241-252.
386. Weber, T., Baumgartner, R., Renner, C., Marahiel, M. A. and Holak, T. (2000). "Solution structure of PCP, a prototype for the peptidyl carrier domains of modular peptide synthetases." Structure with Folding & Design 8, 407-418.
387. Wahl, M., Huber, R., Marinkoviç, S., Weyher-Stingl, E. and Ehlert, S. (2000). "Structural investigations of the highly flexible recombinant ribosomal protein L12 from Thermotoga maritima." Biol. Chem. 381, 221-229.
388. Rebelo, J., Macieira , S., Dias, J. M., Huber, R., Ascenso, C. S., Rusnak, F., Moura, J. J. G., Moura, I. and Romão, M. (2000). "Gene sequence and crystal structure of the aldehyde oxidoreductase from Desulfovibrio desulfuricans ATCC 27774." J. Mol. Biol. 297, 135-146.
389. Huber, R. (2000). "Ufos im Körper. Kann die Chemie jede Krankheit heilen?" Kultur und Technik 2/2000, 16-19.
390. Bode, W., Brandstetter, H., Hopfner, K. P. and Stubbs, M. T. (2000). Three-dimensional structures of coagulation factors: pieces of a complicated puzzle. New Frontier in Vascular Biology; Thrombosis and Hemostasis. K. Suzuki, Y. Ikeda and I. Maruyama. Osaka, Eibun Press, Ltd.: 75-92.
391. Worbs, M., Huber, R. and Wahl, M. C. (2000). "Crystal structure of ribosomal protein L4 shows RNA-binding sites for ribosome incorporation and feedback control of the S10 operon." EMBO J. 19, 807-818.
392. Kaiser, J. T., Clausen, T., Bourenkov, G. P., Bartunik, H., Steinbacher, S. and Huber, R. (2000). "Crystal structure of a NifS-like protein from Thermotoga maritima: implications for iron sulphur cluster assembly." J. Mol. Biol. 297, 451-464.
393. Schuler, B., Fürst, F., Osterroth, F., Steinbacher, S., Huber, R. and Seckler, R. (2000). "Plasticity and steric strain in a parallel b-helix: rational mutations in the P22 tailspike protein." PROTEINS: Structure, Function, and Genetics 39, 89-101.
394. Clausen, T., Schlegel, A., Peist, R., Schneider, E., Steegborn, C., Chang, Y., Haase, A., Bourenkov, G. P., Bartunik, H. and Boos, W. (2000). "X-ray structure of MalY from Escherichia coli: a pyridoxal 5' -phosphate-dependent enzyme acting as a modulator in mal gene expression." EMBO J. 19, 831-842.
395. Hofmann, A., Proust, J., Dorowski, A., Schantz, R. and Huber, R. (2000). "Annexin 24 from Capsicum annuum." J. Biol. Chem. 275, 8072-8082.
396. Parry, M., Zhang, X. C. and Bode, W. (2000). "Molecular mechanisms of plasminogen activation: bacterial cofactors provide clues." TIBS 25, 53-59.
397. Groll, M., Kim, K. B., Kairies, N., Huber, R. and Crews, C. M. (2000). "Crystal structure of epoxomicin: 20S proteasome reveals a molecular basis for selectivity of a´, b´-epoxyketone proteasome inhibitors." J. Am. Chem. Soc. 122, 1237-1238.
398. Gremer, L., Kellner, S., Dobbek, H., Huber, R. and Meyer, O. (2000). "Binding of flavin adenine dinucleotide to molybdenum-containing carbon monoxide dehydrogenase from Oligotropha carboxidovorans." J. Biol. Chem. 275, 1864-1872.
399. Bochtler, M., Hartmann, C., Song, H. K., Bourenkov, G., Bartunik, H. and Huber, R. (2000). "The structure of HslU and the ATP-dependent protease HslU-HslV." Nature 403, 800-805.
400. Loidl, G., Musiol, H. J., Groll, M., Huber, R. and Moroder, L. (2000). "Synthesis of bivalent inhibitors of eucaryotic proteasomes." J. Peptide Sci. 6, 36-46.
401. Strobl, S., Fernandez-Catalan, C., Braun, M., Huber, R., Masumoto, H., Nakagawa, K., Irie, A., Sorimachi, H., Bourenkov, G., Bartunik, H., Suzuki, K. and Bode, W. (2000). [789] ”The crystal structure of calcium-free human m-calpain suggests an electrostatic switch mechanism for activation by calcium.” Proc. Natl. Acad. Sci. USA 97, 588-592.
402. Wahl, M. C., Bourenkov, G. P., Bartunik, H. and Huber, R. (2000). ”Flexibility, conformational diversity and two dimerization modes in complexes of ribosomal protein L12.” EMBO J. 19, 174-186.
403. Skirgaila, R., Grazulis, S., Bozic, D., Huber, R. and Siksnys, V. (1998). ”Structure-based redesign of the catalytic/metal binding site of Cfr10I restriction endonuclease reveals importance of spatial rather than sequence conservation of active centre residues.” J. Mol. Biol. 279, 473-481.
404. Wilharm, E., Parry, M., Friebel, R., Tschesche, H., Matschiner, G., Sommerhoff, C. P. and Jenne, D. E. (1999). ”Generation of catalytically active granzyme K from Escherichia coli inclusion bodies and identification of efficient granzyme K inhibitors in human plasma.” J. Biol. Chem. 274, 27331-27337.
405. Ottl, J., Gabriel, D., Murphy, G., Knäuper, V., Tominaga, Y., Nagase, H., Kröger, M., Tschesche, H., Bode, W. and Moroder, L. (2000). ”Recognition and catabolism of synthetic heterotrimeric collagen peptides by matrix metalloproteinases.” Chemistry & Biology 7, 119-132.
406. Deibert, M., Grazulis, S., Janulaitis, A., Siksnys, V. and Huber, R. (1999). ”Crystal structure of MunI restriction endonuclease in complex with cognate DNA at 1.7 Å resolution.” EMBO J. 18, 5805-5816.
407. Dekker, R. J., Eichinger, A., Stoop, A. A., Bode, W., Pannekoek, H. and Horrevoets, A. (1999). ”The variable region-1 from tissue-type plasminogen activator confers specificity for plasminogen activator inhibitor-1 to thrombin by facilitating catalysis: Release of a kinetic block by a heterologous protein surface loop.” J. Mol. Biol. 293, 613-627.
408. Masumoto, H., Nakagawa, K., Irie, S., Sorimachi, H., Suzuki, K., Bourenkov, G. P., Bartunik, H., Fernandez-Catalan, C., Bode, W. and Strobl, S. (2000). ”Crystallization and preliminary X-ray analysis of recombinant full-length human m-calpain.” Acta Cryst. D56, 73-75.
409. Macedo-Ribeiro, S., Bode, W., Huber, R., Quinn-Allen, M. A., Kim, S. W., Ortel, T. L., Bourenkov, G. P., Bartunik, H., Stubbs, M. T., Kane, W. H. and Fuentes-Prior, P. (1999). ”Crystal structures of the membrane-binding C2 domain of human coagulation factor V.” Nature 402, 434-439.
410. Hemrika, W., Renirie, R., Macedo-Ribeiro, S., Messerschmidt, A. and Wever, R. (1999). ”Heterologous expression of the vanadium-containing chloroperoxidase from Curvularia inaequalis in Saccharomyces cerevisiae and site-directed mutagenesis of the active site residues His496, Lys353, Arg360, and Arg490.” J. Biol. Chem. 274, 23820-23827.
411. Baxa, U., Steinbacher, S., Weintraub, A., Huber, R. and Seckler, R. (1999). ”Mutations improving the folding of phage p22 tailspike protein affect its receptor binding activity.” J. Mol. Biol. 293, 693-701.
412. Clausen, T., Wahl, M., Messerschmidt, A., Huber, R., Fuhrmann, J., Laber, B., Streber, W. and Steegborn, C. (1999). ”Cloning, purification and characterisation of cystathionine g-synthase from Nicotiana tabacum.” Biol. Chem. 380, 1237-1242.
413. Rester, U., Bode, W., Moser, M., Parry, M., Huber, R. and Auerswald, E. (1999). ”Structure of the complex of the antistasin-type inhibitor bdellastasin with trypsin and modelling of the bdellastasin-microplasmin system.” J. Mol. Biol. 293, 93-106.
414. Siksnys, V., Skirgaila, R., Sasnauskas, G., Urbanke, C., Cherny, D., Grazulis, S. and Huber, R. (1999). ”The Cfr10I restriction enzyme is functional as a tetramer.” J. Mol. Biol. 291, 1105-1118.
415. Steinbacher, S. (1999). ”Crystal structure of the post-chaperonin b-tubulin binding cofactor Rbl2p.” Nature Struct. Biol. 6, 1029-1032.
416. Eichinger, A., Beisel, H. G., Jacob, U., Huber, R., Medrano, F. J., Banbula, A., Potempa, J., Travis, J. and Bode, W. (1999). ”Crystal structure of gingipain R: an Arg-specific bacterial cysteine proteinase with a caspase-like fold.” EMBO J. 18, 5453-5462.
417. Sommerhoff, C., Bode, W., Pereira, P., Stubbs, M., Stürzebecher, J., Piechottka, G., Matschiner, G. and Bergner, A. (1999). ”The structure of the human bII-tryptase tetramer: Fo(u)r better or worse.” Proc. Natl. Acad. Sci. USA 96, 10984-10991.
418. Groll, M., Heinemeyer, W., Jäger, S., Ullrich, T., Bochtler, M., Wolf, D. H. and Huber, R. (1999). ”The catalytic sites of 20S proteasomes and their role in subunit maturation: A mutational and crystallographic study.” Proc. Natl. Acad. Sci. USA 96, 10976-10983.
419. Budisa, N., Moroder, L. and Huber, R. (1999). ”Structure and evolution of the genetic code viewed from the perspective of the experimentally expanded amino acid repertoire in vivo.” CMLS Cell. Mol. Life Sci. 55, 1626-1635.
420. Einsle, O., Messerschmidt, A., Stach, P., Bourenkov, G., Bartunik, H., Huber, R. and Kroneck, P. (1999). ”Structure of cytochrome c nitrite reductase.” Nature 400, 476-480.
421. Jäger, S., Groll, M., Huber, R., Wolf, D. and Heinemeyer, W. (1999). ”Proteasome b-type subunits: unequal roles of propeptides in core particle maturation and a hierarchy of active site function.” J. Mol. Biol. 291, 997-1013.
422. Pereira, P., Lozanov, V., Patthy, A., Huber, R., Bode, W., Pongor, S. and Strobl, S. (1999). ”Specific inhibition of insect a-amylases: yellow meal worm a-amylase in complex with the Amaranth a-amylase inhibitor at 2.0 Å resolution.” Structure 7, 1079-1088.
423. Steegborn, C., Messerschmidt, A., Laber, B., Streber, W., Huber, R. and Clausen, T. (1999). ”The crystal structure of cysthathionine g-synthase from Nicotiana tabacum reveals its substrate and reaction specificity.” J. Mol. Biol. 290, 983-996.
424. Schnackenberg, J., Than, M., Mann, K., Wiegand, G., Huber, R. and Reuter, W. (1999). ”Amino acid sequence, crystallization and structure determination of reduced and oxidized cytochrome c6 from the green alga Scenedesmus obliquus.” J. Mol. Biol. 290, 1019-1030.
425. Ottl, J., Gabriel, D., Müller, H., Musiol, H. J., Bode, W. and Moroder, L. (1999). Synthesis of disulfide-bridged heterotrimeric collagen peptides. Conformational properties and digestion by matrix metalloproeinases. Peptide Science Present and Future. Y. Shimonishi. Dordrecht, Kluwer Academic Publishers: 485-489.
426. Bode, W., Fernandez-Catalan, C., Grams, F., Gomis-Rüth, F. X., Nagase, H., Tschesche, H. and Maskos, K. (1999). Insights into MMP-TIMP interactions. Inhibition of Matrix Metalloproteinases. R. A. Greenwald, S. Zucker and L. M. Golub. New York, The New York Academy of Sciences. 878: 73-91.
427. Nagase, H., Meng, Q., Malinovskii, V., Huang, W., Chung, L., Bode, W., Maskos, K. and Brew, K. (1999). Engineering of selective TIMPs. Inhibition of Matrix Metalloproteinases. R. A. Greenwald, S. Zucker and L. M. Golub. New York, The New York Academy of Sciences. 878: 1-11.
428. Minks, C., Huber, R., Moroder, L. and Budisa, N. (1999). ”Atomic mutations at a single tryptophan residue of human recombinant annexin V: effects on structure, stability, and activity.” Biochemistry 38, 10649-10659.
429. Dobbek, H., Gremer, L., Meyer, O. and Huber, R. (1999). ”Crystal structure and mechanism of CO dehydrogenase, a molybdo iron-sulfur flavoprotein containing S-selanylcysteine.” Proc. Natl. Acad. Sci. USA 96, 8884-8889.
430. Bode, W., Fernandez-Catalan, C., Nagase, H. and Maskos, K. (1999). ”Endoproteinase-protein inhibitor interactions.” APMIS 107, 3-10.
431. Bochtler, M., Ditzel, L., Groll, M., Hartmann, C. and Huber, R. (1999). ”The proteasome.” Biophys. Biomol. Struct. 28, 295-317.
432. Ploom, T., Haußmann, C., Hof, P., Steinbacher, S., Bacher, A., Richardson, J. and Huber, R. (1999). ”Crystal structure of 7,8-dihydroneopterin triphosphate epimerase.” Structure 7, 509-516.
433. Hopfner, K. P., Lang, A., Karcher, A., Sichler, K., Kopetzki, E., Brandstetter, H., Huber, R., Bode, W. and Engh, R. (1999). ”Coagulation factor IXa: the relaxed conformation of Tyr99 blocks substrate binding.” Structure 7, 989-996.
434. Sondermann, P. and Jacob, U. (1999). ”Human Fcg receptor IIb expressed in Escherichia coli reveals IgG binding capability.” Biol. Chem. 380, 717-721.
435. Steegborn, C., Clausen, T., Sondermann, P., Jacob, U., Worbs, M., Marinkovic, S., Huber, R. and Wahl, M. (1999). ”Kinetics and inhibition of recombinant human cystathionine g-lyase.” J. Biol. Chem. 274, 12675-12684.
436. Schramm, H., de Rosny, E., Reboud-Ravaux, M., Büttner, J., Dick, A. and Schramm, W. (1999). ”Lipopeptides as dimerization inhibitors of HIV-1 Protease.” Biol. Chem. 380, 593-596.
437. Loidl, G., Musiol, H. J., Groll, M., Ditzel, L., Huber, R. and Moroder, L. (1999). Bivalent Inhibitors of the Yeast Proteasome. Peptides 1998. S. Bajusz and F. Hudecz. Budapest, Akadémiai Kiadó: 828-829.
438. Sondermann, P., Jacob, U., Kutscher, C. and Frey, J. (1999). ”Characterization and crystallization of soluble human Fcg receptor II (CD32) isoforms produced in insect cells.” Biochemistry 38, 8469-8477.
439. Fritsche, E., Paschos, A., Beisel, H. G., Böck, A. and Huber, R. (1999). ”Crystal structure of the hydrogenase maturating endopeptidase HYBD from Escherichia coli.” J. Mol. Biol. 288, 989-998.
440. Steinbacher, S., Hof, P., Eichinger, L., Schleicher, M., Gettemans, J., Vandekerckhove, J., Huber, R. and Benz, J. (1999). ”The crystal structure of the Physarum polycephalum actin-fragmin kinase: an atypical protein kinase with a specialized substrate-binding domain.” EMBO J. 18, 2923-2929.
441. Loidl, G., Groll, M., Musiol, H. J., Huber, R. and Moroder, L. (1999). ”Bivalency as a principle for proteasome inhibition.” Proc. Natl. Acad. Sci. USA 96, 5418-5422.
442. Macedo-Ribeiro, S., Hemrika, W., Renirie, R., Wever, R. and Messerschmidt, A. (1999). ”X-ray crystal structures of active site mutants of the vanadium-containing chloroperoxidase from the fungus Curvularia inaequalis.” JBIC 4, 209-219.
443. Zajc, A., Neuefeind, T., Prade, L., Reinemer, P., Huber, R. and Bieseler, B. (1999). ”Herbicide detoxification by gluthathione S-transferases as implicated from X-ray structures.” Pesticide Science 55, 248-252.
444. Bode, W., Fernandez-Catalan, C., Tschesche, H., Grams, F., Nagase, H. and Maskos, K. (1999). ”Structural properties of matrix metalloproteinases.” CMLS Cell. Mol. Life Sci. 55, 639-652.
445. Meng, Q., Malinovskii, V., Huang, W., Hu, Y., Chung, L., Nagase, H., Bode, W., Maskos, K. and Brew, K. (1999). ”Residue 2 of TIMP-1 is a major determinant of affinity and specificity for matrix metalloproteinases but effects of substitutions do not correlate with those of the corresponding P1’ residue of substrate.” J. Biol. Chem. 274, 10184-10189.
446. Beisel, H. G., Kawabata, S., Iwanaga, S., Huber, R. and Bode, W. (1999). ”Tachylectin-2: crystal structure of a specific GlcNAc/GalNAc-binding lectin involved in the innate immunity host defense of the Japanese horseshoe crab Tachypleus tridentatus.” EMBO J. 18, 2313-2322.
447. Hopfner, K. P., Eichinger, A., Engh, R. A., Laue, F., Ankenbauer, W., Huber, R. and Angerer, B. (1999). ”Crystal structure of a thermostable type B DNA polymerase from Thermococcus gorgonarius.” Proc. Natl. Acad. Sci. USA 96, 3600-3605.
448. Sondermann, P., Huber, R. and Jacob, U. (1999). ”Crystal structure of the soluble form of the human Fcg-receptor IIb: a new member of the immunoglobulin superfamily at 1.7 Å resolution.” EMBO J. 18, 1095-1103.
449. Pereira, P., Wang, Z. M., Rubin, H., Huber, R., Bode, W., Schechter, N. M. and Strobl, S. (1999). ”The 2.2 Å crystal structure of human chymase in complex with succinyl-ala-ala-pro-phe-chloromethylketone: structural explanation for its dipeptidyl carboxypeptidase specificity.” J. Mol. Biol. 286, 163-173.
450. Loidl, G., Groll, M., Musiol, H. J., Ditzel, L., Huber, R. and Moroder, L. (1999). ”Bifunctional inhibitors of the trypsin-like activity of eukaryotic proteasomes.” Chemistry & Biology 6, 197-204.
451. Huber, R. and Betz, M. (1999). Bakterienphotosynthese. Photosynthese. D. P. Häder. Stuttgart, Georg Thieme Verlag: 162-169.
452. Ploom, T., Thöny, B., Yim, J., Lee, S., Nar, H., Leimbacher, W., Richardson, J., Huber, R. and Auerbach, G. (1999). ”Crystallographic and kinetic investigations on the mechanism of 6-pyruvoyl tetrahydropterin synthase.” J. Mol. Biol. 286, 851-860.
453. Huber, R. (1999). ”Strukturanalyse großer Proteinkomplexe.” Naturw. Rdsch. 52, 85-87.
454. Prade, L., Huber, R. and Bieseler, B. (1998). ”Structures of herbicides in complex with their detoxifying enzyme glutathione S-transferase – explanations for the selectivity of the enzyme in plants.” Structure 6, 1445-1452.
455. Brandstetter, H., Engh, R. A., Roedern, E. G. v., Moroder, L., Huber, R., Bode, W. and Grams, F. (1998). ”Structure of malonic acid-based inhibitors bound to human neutrophil collagenase. A new binding mode explains apparently anomalous data.” Protein Science 7, 1303-1309.
456. Fritsche, E., Humm, A. and Huber, R. (1999). ”The ligand-induced structural changes of human L-Arginine: Glycine amidinotransferase.” J. Biol. Chem. 274, 3026-3032.
457. Reuter, W., Wiegand, G., Huber, R. and Than, E. (1999). ”Structural analysis at 2.2 Å of orthorhombic crystals presents the asymmetry of the allophycocyanin-linker complex, AP•Lc7.8, from phycobilisomes of Mastigocladus laminosus.” Proc. Natl. Acad. Sci. USA 96, 1363-1368.
458. Clausen, T., Huber, R., Prade, L., Wahl, M. and Messerschmidt, A. (1998). ”Crystal structure of Escherichia coli cystathione g-synthase at 1.5 Å resolution.” EMBO J. 17, 6827-6838.
459. Budisa, N., Minks, C., Alefelder, S., Wenger, W., Dong, F., Moroder, L. and Huber, R. (1999). ”Toward the experimental codon reassignment in vivo: protein building with an expanded amino acid repertoire.” FASEB J. 13, 41-51.
460. Tuuttila, A., Morgunova, E., Bergmann, U., Lindqvist, Y., Maskos, K., Fernandez-Catalan, C., Bode, W., Tryggvason, K. and Schneider, G. (1998). ”Three-dimensional structure of human tissue inhibitor of metalloproteinases-2 at 2.1 Å resolution.” J. Mol. Biol. 284, 1133-1140.
461. Dias, J., Than, M., Humm, A., Huber, R., Bourenkov, G., Bartunik, H., Bursakov, S., Calvete, J., Caldeira, J., Carneiro, C., Moura, J., Moura, I. and Romão, M. (1999). ”Crystal structure of the first dissimilatory nitrate reductase at 1.9 Å solved by MAD methods.” Structure 7, 65-79.
462. Gabriel, B., Stubbs, M., Bergner, A., Hauptmann, J., Bode, W., Stürzebecher, J. and Moroder, L. (1998). ”Design of benzamidine-type inhibitors of factor Xa.” J. of Medicinal Chemistry 41, 4240-4250.
463. Renatus, M., Bode, W., Huber, R., Stürzebecher, J. and Stubbs, M. (1998). ”Structural and functional analyses of benzamidine-based inhibitors in complex with trypsin: implications for the inhibition of factor Xa, tPa, and urokinase.” J. of Medicinal Chemistry 41, 5445-5456.
464. Fritsche, E., Bergner, A., Humm, A., Piepersberg, W. and Huber, R. (1998). ”Crystal structure of L-arginine: inosamine-phosphate amidinotransferase StrB1 from Streptomyces griseus: an enzyme involved in streptomycin biosynthesis.” Biochemistry 37, 17664-17672.
465. Kalus, W., Zweckstetter, M., Renner, C., Sanchez, Y., Georgescu, J., Grol, M., Demuth, D., Schumacher, R., Dony, C., Lang, K. and Holak, T. (1998). ”Structure of the IGF-binding domain of the insulin-like growth factor-binding protein-5 (IGFBP-5): implications for IGF and IGF-I receptor interactions.” EMBO J. 17, 6558-6572.
466. Renner, C., Baumgartner, R., Noegel, A. and Holak, T. (1998). ”Backbone dynamics of the CDK inhibitor p19INK4d studied by 15N NMR relaxation experiments at two field strengths.” J. Mol. Biol. 283, 221-229.
467. Jaquet , K., Lohmann, K., Czisch, M., Holak, T., Gulati, J. and Jaquet, R. (1998). ”A model for the function of the biphosphorylated heart-specific troponon-I N-terminus.” Journal of Muscle Research and Cell Motility 19, 647-659.
468. Schirra, H. J., Renner, C., Czisch, M., Huber-Wunderlich, M., Holak, T. and Glockshuber, R. (1998). ”Structure of reduced DsbA from Escherichia coli in solution.” Biochemistry 37, 6263-6276.
469. Schirra, H. J., Mühlhahn, P. and Holak, T. (1998). NMR-Spektroskopie von Biomolekülen. Bioanalytik. F. Lottspeich and H. Sorbas. Berlin, Spektrum akademischer Verlag.
470. Bode, W. and Stubbs, M. (1999). Struktur und Funktion des Thrombins. Hämostaseologie. G. Müller-Berghaus and B. Pötzsch. Heidelberg, Springer Verlag: 269-284.
471. Baumgartner, R., Fernandez-Catalan, C., Winoto, A., Huber, R., Engh, R. and Holak, T. (1998). ”Structure of human cyclin-dependent kinase inhibitor p19INK4d: comparison to known ankyrin-repeat-containing structures and implications for the dysfunction of tumor suppressor p16 INK4a.” Structure 6, 1279-1290.
472. Parry, M., Jacob, U., Huber, R., Wisner, A., Bon, C. and Bode, W. (1998). ”The crystal structure of the novel snake venom plasminogen activator TSV-PA: a prototype structure for snake venom serine proteinases.” Structure 6, 1195-1206.
473. Nussbaum, A., Dick, T., Keilholz, W., Schirle, M., Stefanovic, S., Dietz, K., Heinemeyer, W., Groll, M., Wolf, D., Huber, R., Rammensee, H. G. and Schild, H. (1998). ”Cleavage motifs of the yeast 20S proteasome b subunits deduced from digests of enolase 1.” Proc. Natl. Acad. Sci. USA 95, 12504-12509.
474. Parry, M., Fernandez-Catalan, C., Bergner, A., Huber, R., Hopfner, K. P., Schlott, B., Gührs, K. H. and Bode, W. (1998). ”The ternary microplasmin-staphylokinase-microplasmin complex is a proteinase-cofactor-substrate complex in action.” Nature Struct. Biol. 5, 917-923.
475. Fernandez-Catalan, C., Bode, W., Huber, R., Turk, D., Calvete, J. J., Lichte, A., Tschesche, H. and Maskos, K. (1998). ”Crystal structure of the complex formed by the membrane type 1-matrix metalloproteinase with the tissue inhibitor of metalloproteinases-2, the soluble progelatinase A receptor.” EMBO J. 17, 5238-5248.
476. Banbula, A., Potempa, J., Travis, J., Fernandez-Catalan, C., Mann, K., Huber, R., Bode, W. and Medrano, F. J. (1998). ”Amino-acid sequence and three-dimensional structure of the Staphylococcus aureus metalloproteinase at 1.72 Å resolution.” Structure 6, 1185-1193.
477. Hopfner, K. P., Kopetzki, E., Kreße, G. B., Bode, W., Huber, R. and Engh, R. (1998). ”New enzyme lineages by subdomain shuffling.” Proc. Natl. Acad. Sci. USA 95, 9813-9818.
478. Chang, J., Jin, J., Lollar, P., Bode, W., Brandstetter, H., Hamaguchi, N., Straight, D. and Stafford, W. (1998). ”Changing residue 338 in human factor IX from arginine to alanine causes in increase in catalytic activity.” J. Biol. Chem. 273, 12089-12094.
479. Auerbach, G., Ostendorp, R., Prade, L., Korndörfer, I., Dams, T., Huber, R. and Jaenicke, R. (1998). ”Lactate dehydrogenase from the hyperthermophilic bacterium : the crystal structure at 2.1 Å resolution reveals strategies for intrinsic protein stabilization.” Structure 6, 769-781.
480. Roedern, E. G. v., Brandstetter, H., Grams, F., Bode, W. and Moroder, L. (1998). Collagenase inhibitors with a malonic acid hydroxamate skeleton. Peptides 1996. R. Ramage and R. Epton, The European Peptide Society: 431-432.
481. Mühlhahn, P., Zweckstetter, M., Georgescu, J., Ciosto, C., Renner, C., Lanzendörfer, M., Lang, K., Ambrosius, D., Baier, M., Kurth, R. and Holak, T. A. (1998). [709] ”Structure of interleukin 16 resembles a PDZ domain with a peptide binding site.” Nature Struct. Biol. 5, 682-686.
482. Zweckstetter, M. and Holak, T. A. (1998). ”An adiabatic multiple spin-echo pulse sequence: removal of systematic errors due to pulse imperfections and off-resonance effects.” J. Magn. Resonance 133, 134-147.
483. Roedern, E. G. v., Brandstetter, H., Engh, R. A., Bode, W., Grams, F. and Moroder, L. (1998). ”Bis-substituted malonic acid hydroxamate derivatives as inhibitors of human neutrophil collagenase (MMP8).” J. Med. Chem. 41, 3041-3047.
484. Schramm, H. J., Quéré, L., Büttner, J., Wenger, T., Dick, A. and Schramm, W. (1998). ”Steroids as possible inhibitors of HIV-1 protease.” AIDS 12, 682-684.
485. Strobl, S., Maskos, K., Wiegand, G., Huber, R., Gomis-Rüth, F. X. and Glockshuber, R. (1998). ”A novel strategy for inhibition of a-amylases: yellow meal worm a-amylase in complex with the Ragi bifunctional inhibitor at 2.5 Å resolution.” Structure 6, 911-921.
486. Strobl, S., Maskos, K., Betz, M., Wiegand, G., Huber, R., Gomis-Rüth, F. X. and Glockshuber, R. (1998). ”Crystal structure of yellow meal worm a-amylase at 1.64 Å resolution.” J. Mol. Biol. 278, 617-628.
487. Glatigny, A., Hof, P., Romão, M. J., Huber, R. and Scazzocchio, C. (1998). ”Altered specificity mutations define residues essential for substrate positioning in xanthine dehydrogenase.” J. Mol. Biol. 278, 431-438.
488. Ditzel, L., Huber, R., Mann, K.-H., Heinemeyer, W., Wolf, D. H. and Groll, M. (1998). ”Conformational constraints for protein self-cleavage in the proteasome.” J. Mol. Biol. 279, 1187-1191.
489. Romão, M. J., Knäblein, J., Huber, R. and Moura, J. G. (1997). ”Structure and function of molybdopterin containing enzymes.” Prog. Biophys. Molec. Biol. 68, 121-144.
490. Messerschmidt, A. and Wever, R. (1998). ”X-ray structures of apo and tungstate derivatives of vanadium chloroperoxidase from the fungus Curvularia inaequalis.” Inorganica Chimica Acta 273, 160-166.
491. Budisa, N., Huber, R., Golbik, R., Minks, C., Weyer, E. and Moroder, L. (1998). ”Atomic mutations in annexin V. Thermodynamic studies of isomorphous protein variants.” Eur. J. Biochem. 253, 1-9.
492. Dams, T., Böhm, G., Auerbach, G., Bader, G., Schurig, H. and Jaenicke, R. (1998). ”Homo-dimeric recombinant dihydrofolate reductase from Thermotoga maritima shows extreme intrinsic stability.” Biol. Chem. 379, 367-371.
493. Maskos, K., Fernandez-Catalan, C., Huber, R., Bourenkov, G. P., Bartunik, H., Ellestad, G. A., Reddy, P., Wolfson, M. F., Rauch, C. T., Castner, B. J., Davis, R., Clarke, H. R. G., Petersen, M., Fitzner, J. N., Cerretti, D. P., March, C. J., Paxton, R. J., Black, R. A. and Bode, W. (1998). ”Crystal structure of the catalytic domain of human tumor necrosis factor-a-converting enzyme.” Proc. Natl. Acad. Sci. USA 95, 3408-3412.
494. Becker, M., Stubbs, M. T. and Huber, R. (1998). ”Crystallization of phycoerythrin 545 of Rhodomonas lens using detergents and unusual additives.” Protein Science 7, 580-586.
495. Messerschmidt, A., Prade, L., Kroes, S. J., Sanders-Loehr, J., Huber, R. and Canters, G. W. (1998). ”Rack-induced metal binding vs. flexibility: Met121His azurin crystal structures at different pH.” Proc. Natl. Acad. Sci. USA 95, 3443-3448.
496. Ditzel, L., Löwe, J., Stock, D., Stetter, K. O., Huber, H., Huber, R. and Steinbacher, S. (1998). ”Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT.” Cell 93, 125-138.
497. Machius, M., Declerck, N., Huber, R. and Wiegand, G. (1998). ”Activation of Bacillus licheniformis a-amylase through a disorder -> order transition of the substrate-binding site mediated by a calcium-sodium-calcium metal triad.” Structure 6, 281-292.
498. Pereira, P. J., Bergner, A., Macedo-Ribeiro, S., Huber, R., Matschiner, G., Fritz, H., Sommerhoff, C. P. and Bode, W. (1998). ”Human ß-tryptase is a ring-like tetramer with active sites facing a central pore.” Nature 392, 306-311.
499. Freund, C., Gehrig, P., Baici, A., Holak, T. A. and Plückthun, A. (1997). ”Parallel pathways in the folding of a short-term denatured scFv fragment of an antibody.” Folding and Design (Current Biology) 3, 39-49.
500. Gomis-Rüth, F. X., Gómez-Ortiz, M., Vendrell, J., Ventura, S., Bode, W., Huber, R. and Avilés, F. X. (1998). ”Cutting the right place. The importance of selective limited proteolysis in the activation of proproteinase E.” Eur. J. Biochem. 251, 839-844.
501. Voges, D. and Karshikoff, A. (1998). ”A model of a local dielectric constant in proteins.” J. Chem. Phys. 108, 2219-2227.
502. Stubbs, M. T., Renatus, M. and Bode, W. (1998). ”An active zymogen: unravelling the mystery of tissue-type plasminogen activator.” Biol. Chem. 379, 95-103.
503. Beermann, B., Hinz, H. J., Hofmann, A. and Huber, R. (1998). ”Acid induced equilibrium unfolding of annexin V wild type shows two intermediate states.” FEBS Lett. 423, 265-269.
504. Medrano, F. J., Alonso, J., García, J. L., Romero, A., Bode, W. and Gomis-Rüth, F. X. (1998). ”Structure of proline iminopeptidase from Xanthomonas campestris pv.citri: a prototype for the prolyl-oligopeptidase family.” EMBO J. 17, 1-9.
505. Danielsen, E., Kroes, S. J., Canters, G. W., Bauer, R., Hemmingsen, L., Singh, K. and Messerschmidt, A. (1997). ”Coordination geometries for monovalent and divalent metal ions in [His121] azurin.” Eur. J. Biochem 250, 249-259.
506. Hofmann, A., Escherich, A., Lewit-Bentley, A., Benz, J., Raguenes-Nico, C., Russo-Marie, F., Gerke, V., Moroder, L. and Huber, R. (1998). ”Interactions of benzodiazepine derivatives with annexins.” J. Biol. Chem. 5, 2885-2894.
507. Budisa, N., Minks, C., Medrano, F. J., Lutz, J., Huber, R. and Moroder, L. (1998). ”Residue-specific bioincorporation of non-natural, biologically active amino acids into proteins as possible drug carriers: structure and stability of the per-thiaproline mutant.” Proc. Natl. Acad. Sci. USA 95, 455-459.
508. Voityuk, A. A., Albert, K., Romão, M. J., Huber, R. and Rösch, N. (1998). ”Substrate oxidation in the active site of xanthine oxidase and related enzymes. A model density functional study.” Inorg. Chem. 37, 176-180.
509. Auerbach, G., Herrmann, A., Gütlich, M., Fischer, M., Jacob, U., Bacher, A. and Huber, R. (1997). ”The 1.25 Å crystal structure of sepiapterin reductase reveals its binding mode to pterins and brain neurotransmitters.” EMBO J. 16, 7219-7230.
510. Podobnik, M., Kuhelj, R., Turk, V. and Turk, D. (1997). ”Crystal structure of the wild-type human Procathepsin B at 2.5 Å resolution reveals the native active site of a papain-like Cysteine Protease Zymogen.” J. Mol. Biol. 271, 774-788.
511. Neuefeind, T., Huber, R., Reinemer, P., Knäblein, J., Prade, L., Mann, K. H. and Bieseler, B. (1997). ”Cloning, sequencing, crystallization and X-ray structure of glutathione S-transferase-III from Zea mays var, mutin: a leading enzyme in detoxification of maize herbicides.” J. Mol. Biol. 274, 577-587.
512. Neuefeind, T., Huber, R., Dasenbrock, H., Prade, L. and Bieseler, B. (1997). ”Crystal structure of herbicide-detoxifying maize glutathione S-transferase-I in complex with lactoylglutathione: evidence for an induced-fit mechanism.” J. Mol. Biol. 274, 446-453.
513. Blickling, S., Beisel, H. G., Bozic, D., Knäblein, J., Laber, B. and Huber, R. (1997). ”Structure of dihydrodipicolinate synthase of Nicotiana sylvestris reveals novel quaternary structure.” J. Mol. Biol. 274, 608-621.
514. Bode, W. and Renatus, M. (1997). ”Tissue-type plasminogen activator: variants and crystal solution structures demarcate structural determinants of function.” Current Opinion in Structural Biology 7, 865-872.
515. Auerbach, G., Huber, R., Grättinger, M., Zaiss, K., Schurig, H., Jaenicke, R. and Jacob, U. (1997). ”Closed structure of phosphoglycerate kinase from Thermotoga maritima reveals the catalytic mechanism and determinants of thermal stability.” Structure 5, 1475-1483.
516. Prade, L., Huber, R., Manoharan, T. H., Fahl, W. E. and Reuter, W. (1997). ”Structures of class pi glutathione S-transferase from human placenta in complex with substrate, transition-state analogue and inhibitor.” Structure 5, 1287-1295.
517. Prade, L., Engh, R. A., Girod, A., Kinzel, V., Huber, R. and Bossemeyer, D. (1997). ”Staurosporine-induced conformational changes of cAMP-dependent protein kinase catalytic subunit explain inhibitory potential.” Structure 5, 1627-1637.
518. Hopfner, K. P., Brandstetter, H., Karcher, A., Kopetzki, E., Huber, R., Engh, R. and Bode, W. (1997). ”Converting blood coagulation factor IXa into factor Xa: dramatic increase in amidolytic activity identifies important active site determinants.” EMBO J. 16, 6626-6635.
519. Bieseler, B., Fedtke, C., Neuefeind, T., Etzel, W., Prade, L. and Reinemer, P. (1997). ”Maisselektivität von FOE 5043: Abbau des Wirkstoffes durch Glutathion-S-Transferasen.” Pflanzenschutz-Nachrichten Bayer 50, 117-134.
520. Renatus, M., Stubbs, M. T., Huber, R., Bringmann, P., Donner, P., Schleuning, W. D. and Bode, W. (1997). ”Catalytic domain structure of vampire bat plasminogen activator: a molecular paradigm for proteolysis without activation cleavage.” Biochemistry 36, 13483-13493.
521. Hofmann, A., Benz, J., Liemann, S. and Huber, R. (1997). ”Voltage dependent binding of annexin V, annexin VI and annexin VII-core to acidic phospholipid membranes.” Biochimica et Biophysica Acta 1330, 254-264.
522. Messerschmidt, A. (1997). X-ray structure analyses of copper- and vanadium-containing proteins. DFG Bioinorganic Chemistry – Transition Metals in Biology and their Coordination Chemistry. A. X. Trautwein. Weinheim, Wiley-VCH.
523. Romão, M. J., Rösch, N. and Huber, R. (1997). ”The molybdenum site in the xanthine oxidase-related aldehyde oxidoreductase from Desulfovibrio gigas and a catalytic mechanism for this class of enzymes.” IBIC 2, 782-785.
524. Romão, M. J. and Huber, R. (1997). ”Structure and function of the xanthine-oxidase family of molybdenum enzymes.” Structure and Bonding 90, 69-95.
525. Fuentes-Prior, P., Noeske-Jungblut, C., Donner, P., Schleuning, W. D., Huber, R. and Bode, W. (1997). ”Structure of the thrombin complex with triabin, a lipocalin-like exocite-binding inhibitor derived from a triatomine bug.” Proc. Nat. Acad. Sci. USA 94, 11845-11850.
526. Messerschmidt, A. (1998). Copper Metalloenzymes. Comprehensive Biological Catalysis. M. Sinnot. London, Academic Press. III: 401-426.
527. Messerschmidt, A. (1997). ”Metal sites in small blue copper proteins, blue copper oxidases and vanadium-containing enzymes.” Structure and Bonding 90, 37-39.
528. Esmon, C. T., Fukudome, K., Mather, T., Bode, W., Esmon, N. L., Regan, L. M., Stearns-Kurosama, D. J. and Kurosawa, S. (1997). ”Inflammation: the protein C pathway.” Fibrinolysis and Proteolysis 11, 143-148.
529. Declerck, N., Machius, M., Chambert, R., Wiegand, G., Huber, R. and Gaillardin, C. (1997). ”Hyperthermostablemutants of Bacillus licheniformis a-amylase: thermodynamic studies and structural interpretation.” Protein Engineering 10, 541-549.
530. Clausen, T., Huber, R., Messerschmidt, A., Pohlenz, H. D. and Laber, B. (1997). ”Slow-binding inhibition of Escherichia coli cystathionine ß-lyase by L-aminoethoxyvinylglycine: a kinetic and X-ray study.” Biochemistry 36, 12633-12643.
531. Fischer, M., Bracher, A., Lutz, R., Herrmann, A., Auerbach, G., Grüneberg, S., Huber, R., Lottspeich, F., Bacher, A. and Gütlich, M. (1997). Heterologous expression of recombinant human GTP cyclohydrolase I. 11th Intern. Symp.on Pteridines and Folates, Berchtesgaden, Germany, June 15-20, 1997.
532. Haußmann, C., Richter, G., Rohdich, F., Bacher, A., Gomez-Ortiz, M., Grüneberg, S., Auerbach, G., Ploom, T. and Huber, R. (1997). Dihydroneopterin aldolase: properties and preliminary crys tallographic analysis. 11th Intern. Symp. on Pteridines and Folates, Berchtesgaden, Germany, June 15-20, 1997.
533. Haußmann, C., Rohdich, F., Eberhardt, S., Richter, G., Scheuring, J., Mackamul, S., Bacher, A., Ploom, T., Auerbach, G., Lottspeich, F. and Huber, R. (1997). Dihydroneopterin triphosphate epimerase: properties and preliminary crystallographic analysis. 11th Intern. Symp. on Pteridines and Folates, Berchtesgaden, Germany, June 15-20.
534. Auerbach, G., Huber, R., Herrmann, A., Gütlich, M., Fischer, M. and Bacher, A. (1997). The crystal structure of mouse sepiapterin reductase. 11th Intern. Symp. on Pteridines and Folates, Berchtesgaden, Germany, June 15-20,1997.
535. Budisa, N., Karnbrock, W., Steinbacher, S., Humm, A., Prade, L., Neuefeind, T., Moroder, L. and Huber, R. (1997). ”Bioincorporation of telluromethionine into proteins: a promising new approach for X-ray structure analysis of proteins.” J. Mol. Biol. 270, 616-623.
536. Gomis-Rüth, F. X., Stöcker, W. and Bode, W. (1997). Comparison of the crystallographic structure of rattlesnake venom adamalysin II with other members of the metzincin-superfamily and metalloendopeptidases and thermolysin. The Astacins: Structure and Function of a New Protein Family. R. Zwilling and W. Stöcker. Hamburg, Dr. Kovac.
537. Stöcker, W., Yiallouros, I., Köhler, D., Gredel, S., Zwilling, R., Dive, V., Bode, W., Gomis-Rüth, F. X. and Grams, F. (1997). Structural basis for the function of astacin and related zinc peptidases. The Astacins: Structure and Function of a New Protein Family. R. Zwilling and W. Stöcker. Hamburg, Dr. Kovac.
538. Bode, W., Grams, F., Reinemer, P., Gomis-Rüth, F. X., Baumann, U., McKay, D. B. and Stöcker, W. (1997). The metzincins: a new superfamily of zinc endopeptidases. The Astacins. Structure and Function of a New Protein Family. R. Zwilling and W. Stöcker. Hamburg, Dr. Kovac.
539. Grams, F., Stöcker, W., Yiallouros, I., Zwilling, R., Dive, V., Pieper, M., Tschesche, H. and Bode, W. (1997). Binding and transition state analogue and other inhibitors to astacin and related proteases. The Astacins. Structure and Function of a New Protein Family. R. Zwilling and W. Stöcker. Hamburg, Dr. Kovac.
540. Prade, L., Hof, P. and Bieseler, B. (1997). ”Dimer interface of glutathione S-transferase from Arabidopsis thaliana: influence of the G-site architecture on the dimer interface and implications for classification.” Biol. Chem. 378, 317-320.
541. Stürzebecher, J., Kopetzki, E., Bode, W. and Hopfner, K. P. (1997). ”Dramatic enhancement of the catalytic activity of coagula tion factor IXa by alcohols.” FEBS Lett. 412, 295-300.
542. Pieper, M., Betz, M., Budisa, N., Gomis-Rüth, F. X., Bode, W. and Tschesche, H. (1997). ”Expression, purification, characterization, and X-ray analysis of selenomethionine 215 variant of of leucocyte collagenase.” Journal of Protein Chemistry, 16, 637-650.
543. Romão, M. J. and Huber, R. (1997). ”Crystal structure and mechanism of action of the xanthine oxidase-related aldehyde oxidoreductase from Desulfovibrio gigas.” Biochemical Society Transactions 25, 755-758.
544. Freund, C., Gehrig, P., Holak, T. A. and Plückthun, A. (1997). ”Comparison of the amide proto exchange behavor of the rapidly formed folding intermediate and the native state of an antibody scFv fragment.” FEBS Lett. 407, 42-46.
545. Rosinke, B., Renner, C., Mayr, E. M., Jaenicke, R. and Holak, T. A. (1997). ”Ca2+-loaded spherulin 3a from Physarum polycephalum adopts the prototype g-crystallin fold in aqueous solution.” J. Mol. Biol. 271, 645-655.
546. Wahl, M., Huber, R., Prade, L., Marinkovic, S., Messerschmidt, A. and Clausen, T. (1997). ”Cloning, purification, crystallization, and preliminary X-ray diffraction analysis of cystathionine-g-synthase from E. coli.” FEBS Lett. 414, 492-496.
547. Avaeva, S., Kurilova, S., Nazarova, T., Rodina, E., Vorobyeva, N., Sklyankina, V., Grigorjeva, V., Harutyunyan, E., Oganessyan, V., Wilson, K., Dauter, Z., Huber, R. and Mather, T. (1997). ”Crystal structure of Escherichia coli inorganic pyrophosphatase complexed with SO42-. Ligand-induced molecular asymmetry.” FEBS Lett. 410, 502-508.
548. Harutyunyan, E. H., Oganessyan, V. Y., Oganessyan, N. N., Avaeva, S. M., Nazarova, T. I., Vorobyeva, N. N., Kurilova, S. A., Huber, R. and Mather, T. (1997). ”Crystal structure of holo inorganic pyrophosphatase from Escherichia coli at 1.9 Å resolution. mechanism of hydrolysis.” Biochemistry 36, 7754-7760.
549. Soulimane, T., von Walter, M., Hof, P., Than, M. E., Huber, R. and Buse, G. (1997). ”Cytochrome-c552 from Thermus thermophilus: a functional and crystallographic investigation.” Biochemical and Biophysical Research Communications 237, 572-576.
550. Gomis-Rüth, F. X., Gómez-Ortiz, M., Vendrell, J., Ventura, S., Bode, W., Huber, R. and X., A. F. (1997). ”Crystal structure of an oligomer of proteolytic zymogens: detailed conformational analysis of the bovine ternary complex and implications for their activation.” J. Mol. Biol. 269, 861-880.
551. Renatus, M., Bode, W., Huber, R., Stürzebecher, J., Prasa, D., Fischer, S., Kohnert, U. and Stubbs, M. T. (1997). ”Structural mapping of the active site specificity determinants of human tissue-type plasminogen activator. Implications for the design of low molecular weight substrates and inhibitors.” Journal of Biol. Chem. 272, 21713-21719.
552. Than, M. E., Hof, P., Huber, R., Bourenkov, G. P., Bartunik, H. D., Buse, G. and Soulimane, T. (1997). ”Thermus thermophilus cytochrome-c552: a new highly thermostable cytochrome-c structure obtained by MAD phasing.” J. Mol. Biol. 271, 629-644.
553. Tönsing, K., Kakorin, S., Neumann, E., Liemann, S. and Huber, R. (1997). ”Annexin V and vesicle membrane electroporation.” Eur. Biophys. J. 26, 307-318. Gomis-Rüth, F. X., Maskos, K., Betz, M., Bergner, A., Huber, R., Suzuki, K., N., Y., Nagase, H., Brew, K., Bourenkov, G. P., Bartunik, H. and Bode, W. (1997). ”Mechanisms of inhibition of the human matrix metallo-proteinase stromelysin-1 by TIMP-1.” Nature 389, 77-81.
554. Renatus, M., Engh, R. A., Stubbs, M. T., Huber, R., Fischer, S., Kohnert, U. and Bode, W. (1997). ”Lysine 156 promotes the anomalous proenzyme activity of tPA: X-ray crystal structure of single-chain human tPA.” EMBO J. 16, 4797-4805.
555. Escherich, A., Ditzel, L., Musiol, H. J., Groll, M., Huber, R. and Moroder, L. (1997). ”Synthesis, kinetic characterization and X-ray analysis of peptide aldehydes as inhibitors of the 20S proteasomes from Thermoplasma acidophilum and Saccharomyces cerevisiae.” Biological Chemistry 378, 893-898.
556. Morenweiser, R., Auerswald, E. A., van de Locht, A., Fritz, H., Stürzebecher, J. and Stubbs, M. T. (1997). ”Structure based design of a potent chimeric thrombin inhibitor.” J. Biol. Chem. 272, 19938-19942.
557. Stubbs, M. T., Morenweiser, R., Stürzebecher, J., Bauer, M., Bode, W., Huber, R., Piechottka, G. P., Matschiner, G., Sommerhoff, C. P., Fritz, H. and Auerswald, E. (1997). ”The three-dimensional structure of recombinant leech-derived tryptase inhibitor in complex with trypsin. Implications for the structure of human mast cell tryptase and its inhibition.” J. Biol. Chem. 272, 19931-19937.
558. Knäblein, J., Neuefeind, T., Schneider, F., Bergner, A., Messerschmidt, A., Löwe, J., Steipe, B. and Huber, R. (1997). ”Ta6Br2+12 a tool for phase determination of large biological assemblies by X-ray crystallography.” J. Mol. Biol. 270, 1-7.
559. Betz, M., Huxley, P., Davies, S. J., Mushtaq, Y., Pieper, M., Tschesche, H., Bode, W. and Gomis-Rüth, F. X. (1997). ”1.8 Å crystal structure of the catalytic domain of human neutrophil collagenase (matrix-metalloproteinase-8) complexed with a peptidomimetic hydroxamate primed-side inhibitor with a distinct selectivity profile.” Eur. J. Biochem. 247, 356-363.
560. Stubbs, M. T. (1996). ”Structural aspects of factor Xa inhibition.” Current Pharmaceutical Design 2, 543-552. Voityuk, A. A., Albert, K., Köstlmeier, S., Nasluzov, V. A., Neyman, K. M., Hof, P., Huber, R., Romão, M. J. and Rösch, N. (1997). ”Prediction of alternative structures of the molybdenum site in the xanthine oxido-related aldehyde oxido reductase.” J. Am. Chem. Soc. 119, 3159-3160.
561. Fritsche, E., Humm, A. and Huber, R. (1997). ”Substrate binding and catalysis by L-arginine:glycine amidinotransferase. A mutagenesis and crystallographic study.” Eur. J. Biochem. 247, 483-490.
562. Liemann, S., Bringemeier, I., Benz, J., Göttig, P., Hofmann, A., Huber, R., Noegel, A. A. and Jacob, U. (1997). ”Crystal structure of the C-terminal tetrad repeat from synexin (annexin VII) of Dictyostelium discoideum.” J. Mol. Biol. 270, 79-88.
563. Auerbach, G., Jacob, U., Grättinger, M., Schurig, H. and Jaenicke, R. (1997). ”Crystallographic analysis of phosphoglycerate kinase from the hyperthermophilic bacterium Thermotoga maritima.” Biol.Chem. 378, 327-329.
564. Strobl, S., Gomis-Rüth, F. X., Maskos, K., Frank, G., Huber, R. and Glockshuber, R. (1997). ”The a-amylase from the yellow meal worm: complete primary structure crystallization and preliminary X-ray analysis.” FEBS Lett. 409, 109-114.
565. Neuefeind, T., Reinemer, P. and Bieseler, B. (1997). ”Plant glutathione S-transferases and herbicide detoxification.” Biol. Chem. 378, 199-205.
566. Neuefeind, T., Bergner, A., Schneider, F., Messerschmidt, A. and Knäblein, J. (1997). ”The suitability of Ta6Br122+ for phasing in protein crystallography.” Biol. Chem. 378, 219-221.
567. Bochtler, M., Ditzel, L., Groll, M. and Huber, R. (1997). ”Crystal structure of heat shock locus V (HslV) from Escherichia coli.” Proc. Natl. Acad. Sci. USA 94, 6070-6074.
568. Burgering, M. J. M., Orbons, L. P. M., van der Doelen, A., Mulders, J., Theunissen, H. J. M., Grootenhuis, P. D. J., Bode, W., Huber, R. and Stubbs, M. T. (1997). ”The second Kunitz domain of human tissue faxtor pathway inhibitor: cloning, structure determination and interaction with Factor Xa.” J. Mol. Biol. 269, 395-407.
569. Coremans, J. W. A., Poluektov, O. G., Groenen, E. J. J., Canters, G. W., Nar, H. and Messerschmidt, A. (1997). ”A W-band electron spin echo envelope modulation study of a single crystal of azurin.” J. Am. Chem. Soc. 119, 4726-4731.
570. Humm, A., Fritsche, E., Steinbacher, S. and Huber, R. (1997). ”Crystal structure and mechanism of human L-arginine:glycine amidinotransferase: a mitochondrial enzyme involved in creatine biosynthesis.” EMBO J. 16, 3373-3385.
571. van de Locht, A., Bode, W., Huber, R., LeBonniec, B. F., Stone, S. R., Esmon, C. T. and Stubbs, M. T. (1997). ”The Thrombin E192Q-BPTI complex reveals gross structural rearrangements: implications for the interaction with antithrombin and thrombomodulin.” EMBO J. 16, 2977-2984.
572. Liemann, S. and Huber, R. (1997). ”Three-dimensional structure of annexins.” Cell.Mol.Life Sci. 53, 516-521.
573. Bode, W., Brandstetter, H., Mather, T. and Stubbs, M. T. (1997). ”Comparative analysis of haemostatic proteinases: structural aspects of thrombin, factor Xa, factor IXa and protein C.” Thrombosis and Haemostasis 78, 501-511.
574. Hammann, C., van Pouderoyen, G., Nar, H., Gomis-Rüth, F. X., Messerschmidt, A., Huber, R., den Blaauwen, T. and Canters, C. (1997). ”Crystal structures of modified apo-His117Gly and apo-His46Gly mutants of Pseudomonas aeruginosa azurin.” J. Mol. Biol. 266, 357-366.
575. Bergner, A., Muta, T., Iwanaga, I., Beisel, H. G., Delotto, R. and Bode, W. (1997). ”Horseshoe crab coagulation is an invertebrate protein with a nerve growth factor-like domain.” Biol. Chem. 378, 283-287.
576. Betz, M. (1997). ”One century of protein crystallography: the phycobiliproteins.” Biol. Chem. 378, 167-176.
577. Knäblein, J., Dobbek, H., Ehlert, S. and Schneider, F. (1997). ”Isolation, cloning, sequence analysis and X-ray structure of dimethyl sulfoxide/trimethylamine N-oxide reductase from Rhodobacter capsulatus.” Biol. Chem. 378, 293-302.
578. Knäblein, J., Dobbek, H. and Schneider, F. (1997). ”Organization of the DMSO respiratory operon of Rhodobacter capsulatus and its consequences for homologous expression of DMSOR/TMAOR.” Biol. Chem. 378, 303-308.
579. Blickling, S. and Knäblein, J. (1997). ”Feedback inhibition of dihydrodipicolinate synthase enzymes by L-lysine.” Biol.Chem. 378, 207-210.
580. Benz, J. and Hofmann, A. (1997). ”Annexins: from structure to function.” Biol. Chem. 378, 177-183.
581. Humm, A., Fritsche, E. and Steinbacher, S. (1997). ”Structure and reaction mechanism of L-arginine: glycine amidinotransferase.” Biol. Chem. 378, 193-197.
582. Messerschmidt, A., Prade, L. and Wever, R. (1997). ”Implications for the catalytic mechanism of the vanadium-containing enzyme chloroperoxidase from the fungus Curvularia inaequalis by X-ray structures of the native and peroxide form.” Biol. Chem. 378, 309-315.
583. Auerbach, G. and Nar, H. (1997). ”The pathway from GTP to tetrahydrobiopterin: three-dimensional structures of GTP cyclohydrolase I and 6-pyruvoyl tetrahydropterin synthase.” Biol. Chem. 378, 185-192.
584. Steinbacher, S., Miller, S., Baxa, U., Weintraub, A. and Seckler, R. (1997). ”Interaction of Salmonella phage P22 with its O-antigen receptor studies by X-ray crystallography.” Biol. Chem. 378, 337-343.
585. Ditzel, L., Stock, D. and Löwe, J. (1997). ”Structural investigation of proteasome inhibition.” Biol. Chem. 378, 239-247.
586. Bode, W. (1997). ”Robert Huber – a life devoted to protein structure.” Biol. Chem. 378, 119-122.
587. Bode, W., Grams, F., Reinemer, P., Gomis-Rüth, F. X., Baumann, U., McKay, D. B. and Stöcker, W. (1995). ”The metzinzins: a superfamily of structurally related metalloproteinases.” Zoology 99, 237-246.
588. Steinbacher, S., Miller, S., Baxa, U., Budisa, N., Weintraub, A., Seckler, R. and Huber, R. (1997). ”Phage P22 tailspike protein: crystal structure of the head-binding domain at 2.3 Å refined structure of the endorhamnosidase at 1.56 Å resolution, and the molecular basis of O-antigen recognition and cleavage.” J. Mol. Biol. 267, 865-880.
589. Groll, M., Ditzel, L., Löwe, J., Stock, D., Bochtler, M., Bartunik, H. D. and Huber, R. (1997). ”Structure of 20S proteasome from yeast at 2.4 Å resolution.” Nature 386, 463-471.
590. Humm, A., Fritsche, E., Mann, K. H., Göhl, M. and Huber, R. (1997). ”Recombinant expression and isolation of human L-arginine:glycine amidinotransferase and identification of its active-site cysteine residue.” Biochem. J. 322, 771-776.
591. Gomez-Ortiz, M., Gomis-Rüth, F. X., Huber, R. and Avilés, F. X. (1997). ”Inhibition of carboxypeptidase A by excess zinc: analysis of the structural determinants by X-ray crystallography.” FEBS Lett. 400, 336-340.
592. Jacob, U., Mack, M., Clausen, T., Huber, R., Buckel, W. and Messerschmidt, A. (1997). ”Glutaconate CoA-transferase from Acidaminococcus fermentans: the crystal structure reveals homology with other CoA-transferases.” Structure 5, 415-426.
593. Coremans, J. W. A., Poluektov, O. G., Groenen, E. J. J., Canters, G. W., Nar, H. and Messerschmidt, A. (1997). ”A W-band electron nuclear double resonance study of single crystals of 14N and 15N azurin.” J. Am. Chem. Soc. 118, 12141-12153.
594. Kalus, W., Baumgartner, R., Renner, C., Noegel, A., Chan, F. K. M., Winoto, A. and Holak, T. A. (1997). ”NMR structural characterization of the CDK inhibitor p19INK4d.” FEBS Lett. 401, 127-132.
595. Fucini, P., Renner, C., Heberhold, C., Noegel, A. A. and Holak, T. (1997). ”The repeating segments of the F-actin cross-linking gelation factor (ABP-120) have an immunoglobulin-like fold.” Nature Struct. Biol. 4, 223-230.
596. Ohage, E. C., Gramsl, W., Walter, M. M., Steinbacher, S. and Steipe, B. (1997). ”b-Turn propensities as paradigms for the analysis of structural motifs to engineer protein stability.” Protein Science 6, 233-241.
597. Ke, S. H., Tschias, K., Lamba, D., Bode, W. and Madison, E. L. (1997). ”Identification of a hydrophobic exosite on tissue type plasminogen activator that modulates specificity for plasminogen.” J. Biol. Chem. 272, 1811-1816.
598. Blickling, S., Renner, C., Laber, B., Pohlenz, H. D., Holak, T. A. and Huber, R. (1997). ”Reaction mechanism of Escherichia coli dihydrodipicolinate synthase investigated by X-ray crystallography and NMR spectroscopy.” Biochemistry 36, 24-33.
599. Medrano, F. J., Alonso, J., García, J. L., Bode, W. and Gomis-Rüth, F. X. (1997). ”Crystallization and preliminary X-ray diffraction analysis of proline iminopeptidase from Xanthomonas campestris pv. citri.” FEBS Lett. 400, 91-93.
600. Ottl, J., Battistuta, R., Pieper, M., Tschesche, H., Bode, W., Kühn, K. and Moroder, L. (1996). ”Design and synthesis of heterotrimeric collagen peptides with a built-in cystine-knot. Models for collagen catabolism by matrix-metalloproteases.” FEBS Lett. 398, 31-36.
601. Brandstetter, H., Kühne, A., Bode, W., Huber, R., von der Saal, W., Withensohn, K. and Engh, R. A. (1996). ”X-ray structure of active-site inhibited clotting Factor Xa.” J. Biol. Chem. 47, 29988-29992.
602. Coremans, J. W. A., Poluektov, O. G., Groenen, E. J. J., Warmerdam, G. C. M., Canters, G. W., Nar, H. and Messerschmidt, A. (1996). ”The Azurin mutant Met121Gln: A Blue-Copper protein with a strong axial ligand.” Journal of Physical Chemistry 100, 19706-19713.
603. Gomis-Rüth, F. X., Gohlke, U., Betz, M., Knäuper, V., Murphy, G., López-Otín, C. and Bode, W. (1996). ”The helping hand of Collagenase-3 (MMP-13): 2.7 Å crystal structure of its C-terminal Haemopexin-like domain.” J. Mol. Biol. 264, 556-566.
604. Bergner, A., Oganessyan, V., Muta, T., Iwanaga, S., Typke, D., Huber, R. and Bode, W. (1996). ”Crystal structure of coagulogen, the clotting protein from horseshoe crab: a structural homologue of nerve growth factor.” EMBO J. 15, 6789-6797.
605. Mather, T., Oganessyan, V., Hof, P., Huber, R., Foundling, S., Esmon, C. and Bode, W. (1996). ”The 2.8 Å crystal structure of Gla-domainless activated protein C.” EMBO J. 15, 6822-6831.
606. Schmidtke, G., Kraft, R., Kostka, S., Henklein, P., Frömmel, C., Löwe, J., Huber, R., Kloetzel, P. M. and Schmidt, M. (1996). [579] ”Analysis of mammalian 20S proteasome biogenesis: the maturation of b-subunits is an ordered two-step mechanism involving autocatalysis.” EMBO J. 15, 6887-6898.
607. Baxa, U., Steinbacher, S., Miller, S., Weintraub, A., Huber, R. and Seckler, R. (1996). ”Interactions of phage P22 tails with their cellular receptor, Salmonella O-antigen polysaccharide.” Biophysical Journal 71, 2040-2048.
608. Engh, R. A., Girod, A., Kinzel, V., Huber, R. and Bossemeyer, D. (1996). ”Crystal structure of catalytic subunit of cAMP-dependent protein kinase in complex with Isoquinolinesulfonyl protein kinase inhibitors H7, H8, and H89. Structural implications for selectivity.” J. Biol. Chem. 271, 26157-26164.
609. van de Locht, A., Stubbs, M. T., Bode, W., Friedrich, T., Bollschweiler, C., Höffken, W. and Huber, R. (1996). ”The ornithodorin-thrombin crystal structure, a key to the TAP enigma?” EMBO J. 15, 6011-6017.
610. Schramm, H. J., Boetzel, J., Büttner, J., Fritsche, E., Göhring, W., Jaeger, E., König, S., Thumfart, O., Wenger, T., Nagel, N. E. and Schramm, W. (1996). ”The inhibition of human immunodeficiency virus proteases by ’interface peptides’.” Antiviral Research 30, 155-170.
611. Quéré, L., Wenger, T. and Schramm, H. J. (1996). ”Triterpenes as potential dimerization inhibitors of HIV-1 protease.” Biochemical and Biophysical Research Communications 227, 484-488.
612. Messerschmidt, A. (1996). ”The multicopper-enzyme ascorbate oxidase.” Perspectives of Bioinorganic Chemistry 3, 151-197.
613. Schneider, F., Löwe, J., Huber, R., Schindelin, H., Kisker, C. and Knäblein, J. (1996). ”Crystal structure of dimethyl sulfoxide reductase from Rhodobacter capsulatus at 1.88Å resolution.” J. Mol. Biol. 263, 53-69.
614. Zajc, A., Romão, M. J., Turk, B. and Huber, R. (1996). ”Crystallographic and fluorescence studies of ligand binding to N-carbamoylsarcosine amidohydrolase from Arthrobacter-sp.” J. Mol. Biol. 263, 269-283.
615. Knäblein, J., Mann, K. H., Ehlert, S., Fonstein, M., Huber, R. and F., S. (1996). ”Isolation, cloning, sequence analysis and localization of the operon encoding dimethyl sulfoxide/trimethylamine N-oxide reductase from Rhodobacter capsulatus.” J. Mol. Biol. 263, 40-52.
616. Macedo-Ribeiro, S., Darimont, B., Sterner, R. and Huber, R. (1996). ”Small structural changes account for the high thermostability of 1 [4Fe-4S]ferrodoxin from the hyperthermophilic bacterium Thermotoga maritima.” Structure 4, 1291-1301.
617. Engh, R. A., Brandstetter, H., Sucher, G., Eichinger, A., Baumann, U., Bode, W., Huber, R., Poll, T., Rudolph, R. and von der Saal, W. (1996). ”Enzyme flexibility, solvent and ’weak’ interactions characterize thrombin-ligand interactions: implications for drug design.” Structure 4, 1353-1362.
618. Hof, P., Mayr, I., Huber, R., Korzus, E., Potempa, J., Travis, J., Powers, J. C. and Bode, W. (1996). ”The 1.8 Å crystal structure of human cathepsin G in complex with Suc-Val-Pro-PheP- (OPh)2: a Janus-faced proteinase with two opposite specificities.” EMBO J. 15, 5481-5491.
619. Pöschl, E., Mayer, U., Stetefeld, J., Baumgartner, R., Holak, T. A., Huber, R. and Timpl, R. (1996). ”Site-directed mutagenesis and structural interpretation of the nidogen binding site of the laminin g 1 chain.” EMBO J. 15, 5154-5159.
620. Steinbacher, S., Baxa, U., Miller, S., Weintraub, A., Seckler, R. and Huber, R. (1996). ”Crystal structure of phage P22 tailspike protein complexed with Salmonella sp. O-antigen receptors.” Proc. Natl. Acad. Sci. USA 93, 10584-10588.
621. Kiefersauer, R., Stetefeld, J., Gomis-Rüth, F. X., Romão, M. J., Lottspeich, F. and Huber, R. (1996). ”Protein-crystal density by volume measurement and amino-acid analysis.” J. Appl. Cryst. 29, 311-317.
622. Huber, R., Hof, P., Duarte, R. O., Moura, J. G., Moura, I., Liu, M. Y., LeGall, J., Hille, R., Archer, M. and Romão, M. J. (1996). ”A structure-based catalytic mechanism for the xanthine oxidase family of molybdenum enzymes.” Proc. Natl. Acad. Sci. USA 93, 8846-8851.
623. Clausen, T., Huber, R., Laber, B., Pohlenz, H. D. and Messerschmidt, A. (1996). ”Crystal structure of the pyridoxal-5`-phosphate dependent cystathionine b-lyase from Escherichia coli at 1.83 Å.” J. Mol. Biol. 262, 202-224.
624. Kroes, S. J., Hoitink, K. W. G., Andrew, C. R., Ai, J., Sanders-Loehr, J., Messerschmidt, A., Hagen, W. R. and Canters, G. W. (1996). ”The mutation Met121 -> His creates a type-1.5 copper site in Alcaligenes denitrificans azurin.” Eur. J. Biochem. 240, 342-351.
625. Grams, F., Dive, V., Yiotakis, A., Yiallouros, I., Vassiliou, S., Zwilling, R., Bode, W. and Stöcker, W. (1996). ”Structure of astacin with a transition-state analogue inhibitor.” Nature Structural Biology 2, 671-675.
626. Simons, B. H., Barnett, P., Vollenbroek, E. G. M., Dekker, H. L., Muijsers, A. O., Messerschmidt, A. and Wevers, R. (1995). ”Primary structure and characterization of the vanadium chloroperoxidase from the fungus Curvularia inaequalis.” Eur. J. Biochem. 229, 566-574.
627. Stock, D., Nederlof, P. M., Seemüller, E., Baumeister, W., Huber, R. and Löwe, J. (1996). ”Proteasome: from structure to function.” Current Opinion in Biotechnology 7, 376-385.
628. Machius, M., Vértesy, L., Huber, R. and Wiegand, G. (1996). ”Carbohydrate and protein-based inhibitors of porcine pancreatic a-amylase: structure analysis and comparison of their binding characteristics.” J. Mol. Biol. 260, 409-421.
629. Benz, J., Bergner, A., Hofmann, A., Demange, P., Göttig, P., Liemann, S., Huber, R. and Voges, D. (1996). ”The structure of recombinant human annexin VI in crystals and membrane-bound.” J. Mol. Biol. 260, 638-643.
630. Bode, W., Lollar, P., Bauer, M., Huber, R. and Brandstetter, H. (1996). ”Crystal structure of the antihaemophilic clotting factor IXa: explanation for its activity enhancement towards factor X upon complex formation with factor VIIIa.” Jap. J. Thromb. Hemost. 7, 165-175.
631. Stock, D., Ditzel, L., Baumeister, W., Huber, R. and Löwe, J. (1995). Catalytic mechanism of the 20S proteasome of Thermoplasma acidophilum revealed by X-ray crystallography. Cold Spring Harbor Symposia on Quantitative Biology, Cold Spring Harbor Laboratory Press.
632. Stubbs, M. T., Nar, H., Löwe, J., Huber, R., Ladenstein, R., Spangfort, M. D. and Svensson, L. A. (1996). ”Locating a local symmetry axis from patterson map cross vectors: application to crystal data from GroEL, GTP cyclohydrolase I and the proteasome.” Acta Cryst. D52, 447-452.
633. Liemann, S., Benz, J., Burger, A., Voges, D., Hofmann, A., Huber, R. and Göttig, P. (1996). ”Structural and functional characterisation of the voltage sensor in the ion channel human annexin V.” J. Mol. Biol. 258, 555-561.
634. Lamba, D., Bauer, M., Huber, R., Fischer, S., Rudoph, R., Kohnert, U. and Bode, W. (1996). ”The 2.3 Å Crystal structure of the catalytic domain of recombinant two-chain human tissue-type plasminogen activator.” J. Mol. Biol. 258, 117-135.
635. Baumgartner, R., Czisch, M., Mayer, U., Pöschl, E., Huber, R., Timpl, R. and Holak, T. (1996). ”Structure of the nidogen binding LE module of the laminin g1 chain in solution.” J. Mol. Biol. 257, 658-668.
636. Stetefeld, J., Mayer, U., Timpl, R. and Huber, R. (1996). ”Crystal structure of three consecutive laminin-type epidermal growth factor-like (LE) modules of Laminin g1 chain harboring the nidogen binding site.” J. Mol. Biol. 257, 644-657.
637. Bode, W., Grams, F., Reinemer, P., Gomis-Rüth, F. X., Baumann, U., McKay, D. B. and Stöcker, W. (1996). The metzincin-superfamily of zinc-peptidases. Advances in Experimental Medicine and Biology.Intracellular Protein Catabolism. K. Suzuki and J. S. Bond. 389: 1-11.
638. Burger, A., Berendes, R., Liemann, S., Benz, J., Hofmann, A., Göttig, P., Huber, R., Gerke, V., Thiel, C., Römisch, J. and Weber, K. (1996). ”The crystal structure and ion channel activity of human annexin II, a peripheral membrane protein.” J. Mol. Biol. 257, 839-847.
639. van de Locht, A., Stubbs, M. T., Bauer, M. and Bode, W. (1996). ”Crystallographic evidence that the F2 Kringle catalytic domain linker of prothrombin does not cover the fibrinogen recognition exosite.” J. Biol. Chem. 271, 3413-3416.
640. Karnbrock, W., Weyher, E., Budisa, N., Huber, R. and Moroder, L. (1996). ”A new efficient synthesis of acetyltelluro- and acetylselenomethionine and their use in the biosynthesis of heavy-atom protein analogs.” J. Am. Chem. Soc. 118, 913-914.
641. Messerschmidt, A. and Wever, R. (1996). ”X-ray structure of a vanadium-containing enzyme: chloroperoxidase from fungus Curvularia inaequalis.” Proc. Natl. Acad. Sci. USA 93, 392-396.
642. Auerswald, E. A., Nägler, D. K., Gross, S., Assfalg-Machleidt, I., Stubbs, M. T., Eckerskorn, C., Machleidt, W. and Fritz, H. (1996). ”Hybrids of chicken cystatin with human kininogen domain 2 sequences exhibit novel inhibition of calpain, improved inhibition of actinidin and impaired inhibition of papain, cathepsin L and cathepsin B.” Eur. J. Biochem. 235, 534-542.
643. Laber, B., Clausen, T., Huber, R., Messerschmidt, A., Egner, U., Müller-Fahrnow, A. and Pohlenz, H. D. (1996). ”Cloning, purification, and crystallization of Escherichia coli cystathionine b-lyase.” FEBS Lett. 379, 94-96.
644. Hammann, C., Messerschmidt, A., Huber, R., Nar, H., Gilardi, G. and Canters, G. W. (1996). ”X-ray crystal structure of the two site-specific mutants Ile7Ser and PheSer of azurin from Pseudomonas aeruginosa.” J. Mol. Biol. 255, 362-366.
645. Bozic, D., Grazulis, S., Siksnys, V. and Huber, R. (1996). ”Crystal structure of Citrobacter freundii restriction endonuclease Cfr10I at 2.15 Å resolution.” J. Mol. Biol. 255, 176-186.
646. Gohlke, U., Gomis-Rüth, F. X., Crabbe, T., Murphy, G., Docherty, A. J. P. and Bode, W. (1996). ”The C-terminal (haemopexin-like) domain structure of human gelatinase A (MMP2): structural implications for its function.” FEBS Lett. 378, 126-130.
647. Reinemer, P., Prade, L., Hof, P., Neuefeind, T., Huber, R., Zettl, R., Palme, K., Schell, J., Koelln, I., Bartunik, H. D. and Bieseler, B. (1996). ”Three-dimensional structure of glutathione S-tranferase from Arabidopsis thaliana at 2.2 Å resolution: structural characterization of herbicide-conjugating plant glutathione s-transferases and a novel active site architecture.” J. Mol. Biol. 255, 289-309.
648. Bode, W. (1996). The three dimensional structure of human neutrophil elastase. Lung Biology in Health and Disease. ”Alpha 1-Antitrypsin Deficiency”. R. G. Crystal. New York, Marcel Dekker Inc. 88: 97-117.
649. Engh, R. A. and Bode, W. (1996). The three-dimensional structure of a-1AT. Lung Biology in Health and Disease. ”Alpha 1-Antitrypsin Deficiency”. R. G. Crystal. New York, Marcel Dekker Inc. 88: 77-95.
650. Romão, M. J., Archer, M., Moura, I., Moura, J. J. G., LeGall, J., Engh, R. A., Schneider, M., Hof, P. and Huber, R. (1995). ”Crystal structure of the xanthine oxidase-related aldehyde oxido-reductase from D. gigas.” Science 270, 1170-1176.
651. Huber, R. (1995). ”Strukturen des Lebens im Brennpunkt der modernen Wissenschaft. Erkenntnisse der Proteinkristallographie.” Technische Mitteilungen 88 3, 114-120.
652. Oppliger, T., Thöny, B., Nar, H., Bürgisser, D., Huber, R., Heizmann, C. W. and Blau, N. (1995). ”Structural and functional consequences of mutations in 6-pyruvoyltetrahydropterin synthase causing hyperphenylalaninemia in humans. Phosphorylation is a requirement for in vivo activity.” J. Biol. Chem. 270, 29498-29506.
653. König, S., Ugi, I. and Schramm, H. J. (1995). ”Facile syntheses of C2-symmetrical HIV-1 protease inhibitors.” Archiv der Pharmazie. Pharmaceutical and Medicinal Chemistry. 328, 689-740.
654. Grams, F., Crimmin, M., Hinnes, L., Huxley, P., Pieper, M., Tschesche, H. and Bode, W. (1995). ”Structure determination and analysis of human neutrophil collagenase complexed with a hydroxamate inhibitor.” Biochemistry 34, 14012-14020.
655. van de Locht, A., Lamba, D., Bauer, M., Huber, R., Friedrich, T., Kröger, B., Höffken, W. and Bode, W. (1995). ”Two heads are better than one: crystal structure of the insect derived double domain Kazal inhibitor rhodniin in complex with thrombin.” EMBO J. 14, 5149-5157.
656. Engh, R. A., Huber, R., Bode, W. and Schulze, A. J. (1995). ”Divining the serpin inhibition mechanism: a suicide substrate ’springe’?” Trends in Biotechnology 13, 503-510.
657. Voges, D., Berendes, R., Demange, P., Benz, J., Göttig, P., Liemann, S., Huber, R. and Burger, A. (1995). Structure and function of the ion channel model system annexin V. Advances in Enzymology and Related Areas of Molecular Biology. A. Meister, John Wiley & Sons, Inc. 71.
658. Gomis-Rüth, F. X., Fita, I., Kiefersauer, R., Huber, R., Avilés, F. X. and Navaza, J. (1995). ”Determination of hemihedral twinning and initial structural-analysis of crystals of the procarboxypeptidase-a ternary complex.” Acta Crystallographica D51, 819-823.
659. Brandstetter, H., Bauer, M., Huber, R., Lollar, P. and Bode, W. (1995). ”X-ray structure of clotting factor IXa – active-site and module structure related to Xase activity and hemophilia-b.” Proc. Natl. Acad. Sci, USA 92, 9796-9800.
660. Bürgisser, D. M., Thöny, B., Redweik, U., Hess, D., Heizmann, C. W., Huber, R. and Nar, H. (1995). ”6-pyruvoyl tetrahydropterin synthase. An enzyme with a novel type of active site involving both zinc binding and an intersubunit catalytic triad motif; site-directed mutagenesis of the proposed active center, characterization of the metal binding site and modelling of substrate binding.” J. Mol. Biol. 253, 358-369.
661. Meining, W., Bacher, A., Bachmann, L., Schmid, C., Weinkauf, S., Huber, R. and Nar, H. (1995). ”Elucidation of crystal packing by X-ray diffraction and freeze-etching electron microscopy. Studies on GTP cyclohydrolase I of Escherichia coli.” J. Mol. Biol. 253, 208-218.
662. Ritsert, K., Huber, R., Turk, D., Ladenstein, R., Schmidt-Bäse, K. and Bacher, A. (1995). ”Studies of the lumazine synthase/riboflavin synthase complex of Bacillus subtilis: crystal structure analysis of reconstituted, icosahedral b-subunit capsids with bound substrate analogue inhibitor at 2.4 Å resolution.” J. Mol. Biol. 253, 151-167.
663. Gomis-Rüth, F. X., Gómez, M., Bode, W., Huber, R. and Avilés, F. X. (1995). ”The three-dimensional structure of the native ternary complex of bovine pancreatic procarboxypeptidase A with proproteinase E and chymotrypsinogen C.” EMBO J. 14, 4387-4394.
664. Ascenzi, P., Amiconi, G., Bode, W., Bolognesi, M., Coletta, M. and Menegatti, E. (1995). ”Proteinase inhibitors from the European medicinal leech Hirudo medicinalis: structural, functional and biomedical aspects.” Mol. Aspects Med. 16, 215-313.
665. Stubbs, M. T., Huber, R. and Bode, W. (1995). ”Crystal structures of factor Xa specific inhibitors in complex with trypsin: structural grounds for inhibition of factor Xa and selectivity against thrombin.” FEBS Lett. 375, 103-107.
666. Archer, M., Huber, R., Tavares, P., Moura, I., Moura, J. J. G., Corrondo, M. A., Sieker, L. C., LeGall, J. and Romão, M. J. (1995). ”Crystal structure of desulforedoxin from Desulfovibrio gigas determined at 1.8 Å resolution: a novel non-heme iron protein structure.” J. Mol. Biol. 251, 690-702.
667. Stubbs, M. T. and Bode, W. (1995). ”Structure and specificity in coagulation and its inhibition.” TCM 5, 157-166.
668. Turk, D., Podobnik, M., Popovic, T., Katunuma, N., Bode, W., Huber, R. and Turk, V. (1995). ”Crystal structure of cathepsin B inhibited with CA030 at 2.0 Å resolution: a basis for the design of specific epoxysuccinyl inhibitors.” Biochemistry 34, 4791-4797.
669. Nar, H., Huber, R., Auerbach, G., Fischer, M., Hösl, C., Ritz, H., Bracher, A., Meining, W., Eberhardt, S. and Bacher, A. (1995). ”Active site topology and reaction mechanism of GTP cyclohydrolase I.” Proc. Natl. Acad. Sci. USA 92, 12120-12125.
670. Schröder, K., Graumann, P., Schnuchel, A., Holak, T. A. and Marahiel, M. A. (1995). ”Mutational analysis of the putative nucleic acid-binding surface of the cold-shock domain, CspB, revealed an essential role of aromatic and basic residues in binding of single-stranded DNA containing the Y-box motif.” Molecular Microbiology 16, 699-708.
671. Stöcker, W. and Bode, W. (1995). ”Structural features of a superfamily of zinc-endopeptidases: the metzincins.” Current Opinion in Structural Biology 5, 383-390.
672. Soulimane, T., Gohlke, U., Huber, R. and Buse, G. (1995). ”Three-dimensional crystals of cytochrome-c oxidase from Thermus thermophilus diffracting to 3.8 Å resolution.” FEBS Lett. 368, 132-134.
673. Strobl, S., Mühlhahn, P., Bernstein, R., Wiltscheck, R., Maskos, K., Wunderlich, M., Huber, R., Glockhuber, R. and Holak, T. (1995). ”Determination of the three-dimensional structure of the bifunctional a-amylase/trypsin inhibitor from Ragi seeds by NMR spectroscopy.” Biochemistry 34, 8281-8293.
674. Budisa, N., Steipe, B., Demange, P., Eckerskorn, C., Kellermann, J. and Huber, R. (1995). ”High-level biosynthetic substitution of methionine in proteins by its analogs 2-aminohexanoic acid, selenomethionine, telluromethionine and ethionine in Escherichia coli.” Eur. J. Biochem. 230, 788-796.
675. Stöcker, W., Grams, F., Baumann, U., Reinemer, P., Gomis-Rüth, F. X., McKay, D. B. and Bode, W. (1995). ”The metzincins – topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a superfamily of zinc-peptidases.” Protein Science 4, 823-840.
676. Reinemer, P., Dirr, H. W. and Huber, R. (1995). ”X-ray structure methods for glutathione binding.” Methods in Enzymology 251, 243-254.
677. Seemüller, E., Lupas, A., Stock, D., Löwe, J., Huber, R. and Baumeister, W. (1995). ”Proteasome from Thermoplasma acidophilum: a threonine protease.” Science 268, 579-582.
678. Brejc, K., Ficner, R., Huber, R. and Steinbacher, S. (1995). ”Isolation, crystallization, crystal structure analysis and refinement of allophycocyanin from the cyanobacterium Spirulina platensisat 2.3 Å resolution.” J. Mol. Biol. 249, 424-440.
679. Baumann, U., Bauer, M., Létoffé, S., Delepelaire, P. and Wandersman, C. (1995). ”Crystal structure of a complex between Serratia marcescens metallo-protease and an inhibitor from Erwinia chrysanthemi.” J. Mol. Biol. 248, 653-661.
680. Beißinger, M., Lee, S. C., Steinbacher, S., Reinemer, P., Huber, R., Yu, M. H. and Seckler, R. (1995). ”Mutations that stabilize folding intermediates of phage P22 tailspike protein: folding in vivo and in vitro, stability, and structural context.” J. Mol. Biol. 249, 185-194.
681. Bode, W. (1995). ”A helping hand for collagenases: the haemopexin-like domain.” Structure 3, 527-530.
682. Nar, H., R., H., Meining, W., Schmid, C., Weinkauf, S. and Bacher, A. (1995). ”Atomic structure of GTP cyclohydrolase I.” Structure 3, 459-466.
683. Reinemer, P. and Huber, R. (1995). Röntgenstrahlen in der Biochemie. Forschung mit Röntgenstrahlen. Bilanz eines Jahrhunderts 1895-1995. F. H. W. Heuck and E. Macherauch. Heidelberg, Springer Verlag: 402-426.
684. Auerswald, E. A., Nägler, D. K., Assfalg-Machleidt, I., Stubbs, M. T., Machleidt, W. and Fritz, H. (1995). ”Hairpin loop mutations of chicken cystatin have different effects on the inhibition of cathepsin B, cathepsin L and papain.” FEBS Lett. 361, 179-184.
685. Bode, W. and Stubbs, M. T. (1995). ”Die Raumstruktur des Thrombins: Ein Wegweiser zu seinen vielfältigen Funktionen.” Hämostaseologie 15, 1-13.
686. Bergner, A., Bauer, M., Brandstetter, H., Stürzebecher, J. and Bode, W. (1995). ”The X-ray crystal structure of thrombin in complex with Na-2-naphtylsulfonyl-L-3-amidino-phenylalanyl-4-methylpiperidide: the beneficial effect of filling out an empty cavity.” J. Enzyme Inhibition 9, 101-110.
687. Löwe, J., Stock, D., Jap, B., Zwickl, P., Baumeister, W. and Huber, R. (1995). ”Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 Å resolution.” Science 268, 533-539.
688. Machleidt, W., Nägler, D. K., Assfalg-Machleidt, I., Stubbs, M. T., Fritz, H. and Auerswald, E. A. (1995). ”Temporary inhibition of papain by hairpin loop mutants of chicken cystatin.” FEBS Lett. 361, 185-190.
689. Coremans, J. W. A., van Gastel, M., Poluektov, O. G., Groenen, E. J. J., den Blauween, T., van Pouderoyen, G., Canters, G. W., Nar, H., Hammann, C. and Messerschmidt, A. (1995). ”An ENDOR and ESEEM study of the blue copper protein azurin.” Chemical Physics Letters 235, 202-210.
690. Wiegand, G., Epp, O. and Huber, R. (1995). ”The crystal structure of porcine pancreatic a-amylase in complex with the microbial inhibitor tendamistat.” J. Mol. Biol. 247, 99-110.
691. Liemann, S. and Lewit-Bentley, A. (1995). ”Annexins: a novel family of calcium- and membrane-binding proteins in search of a function.” Structure 3, 233-237.
692. Kungl, A. J., Machius, M., Huber, R., Schwer, C., Lam, C., Aschauer, H., Ehn, G., Lindley, I. J. D. and Auer, M. (1994). [491 519] ”Purification, crystallization and preliminary X-ray diffraction analysis of recombinant human neutrophil-activating peptide 2 (rhNAP-2).” FEBS Lett. 347, 300-303.
693. Mühlhahn, P., Czisch, M., Morenweiser, R., Habermann, B., Engh, R. A., Sommerhoff, C. P., Auerswald, E. A. and Holak, T. A. (1994). ”Structure of leech derived tryptase inhibitor (LDTI-C) in solution.” FEBS Lett. 355, 290-296.
694. Schnuchel, A., Wiltscheck, R., Eichinger, L., Schleicher, M. and Holak, T. A. (1995). ”Structure of severin domain 2 in solution.” J. Mol. Biol. 247, 21-27.
695. Grams, F., Reinemer, P., Powers, J. C., Kleine, T., Pieper, M., Tschesche, H., Huber, R. and Bode, W. (1995). ”X-ray structures of human neutrophil collagenase complexed with peptide hydrocamate and peptide thiol inhibitors. Implications for substrate binding and rational drug design.” Eur. J. Biochem. 228, 830-841.
696. Stubbs, M. T. and Bode, W. (1995). ”The clot thickens: clues provided by thrombin structure.” TIBS 20, 23-28.
697. Deisenhofer, J., Epp, O., Sinning, I. and Michel, H. (1995). ”Crystallographic refinement at 2.3 Å resolution and refined model of the photoynthetic reaction centre from Rhodopseudomonas viridis.” J. Mol. Biol. 246, 429-457.
698. Machius, M., Wiegand, G. and Huber, R. (1995). ”Crystal structure of calcium-depleted Bacillus licheniformis a-amylase at 2.2 Å resolution.” J. Mol. Biol. 246, 545-559.
699. Korndörfer, I., Steipe, B., Huber, R., Tomschy, A. and Jaenicke, R. (1995). ”The crystal structure of holo-glyceraldehyde-3-phosphate dehydrogenase from the hypermophilic bacterium Thermotoga maritima at 2.5 Å resolution.” J. Mol. Biol. 246, 511-521.
700. Mirwaldt, C., Korndörfer, I. and Huber, R. (1995). ”The crystal structure of dihydrodipicolinate synthase from Escherichia coli at 2.5. Å resolution.” J. Mol. Biol. 246, 227-239.
701. Musiol, H. J., Grams, F., Rudolph-Böhner, S. and Moroder, L. (1994). ”On the synthesis of phosphonamidate peptides.” The Journal of Organic Chemistry, 59, 6144-6146.
702. Danielsen, E., Bauer, R., Hemmingsen, L., Andersen, M. L., Bjerrum, M. J., Butz, T., Tröger, W., Canters, G. W., Hoitink, C. W. G., Karlsson, G., Hansson, Ö. and Messerschmidt, A. (1995). ”Structure of metal site in azurin, Met121 mutants of azurin and stellacyanin investigated by 111m Cd perturbed angular correlation (PAC).” J. Biol. Chem. 270, 573-580.
703. Stubbs, M. T. and Bode, W. (1994). ”Coagulation factors and their inhibitors.” Current Opinion in Structural Biology 4, 823-832.
704. Zhang, D., Botos, I., Gomis-Rüth, F. X., Doll, R., Blood, C., Njoroge, F. G., Fox, J. W., Bode, W. and Meyer, E. F. (1994). ”Structural interaction of natural and synthetic inhibitors with the venom metalloproteinase, atrolysin C (form d).” Prot. Natl. Acad. Sci. 91, 8447-8451.
705. Klinkert, M. Q., Cioli, D., Shaw, E., Turk, V., Bode, W. and Butler, R. (1994). ”Sequence and structure similarities of cathepsin B from the parasite Schistosoma mansoni and human liver.” FEBS Lett. 351, 397-400.
706. Dirr, H., Reinemer, P. and Huber, R. (1994). ”Refined crystal structure of porcine class pi glutathione S-transferase (pGST P1-1) at 2.1 Å resolution.” J. Mol. Biol. 243, 72-92.
707. Tschesche, H., Knäuper, V., Kleine, T., Reinemer, P., Schnierer, S., Grams, F. and Bode, W. (1994). ”Function and structure of human leucocyte collagenase.” J. Prot. Chem. 13 , No 5, 460-461.
708. Bode, W., Kress, L. F., Meyer, E. F. and Gomis-Rüth, F. X. (1994). ”The crystal structure of adamalysin II, a zinc-endopeptidase from the snake venom of the Eastern diamondback rattlesnake Crotalus adamanteus.” Brazilian J. Med. Biol. Res. 27, 2049-2068.
709. Stubbs, M. T. and Bode, W. (1995). The structural basis for thrombin inhibition by hirudin and serpins. Thrombin, Its Key Role in Thrombogenesis – Implications for Its Inhibition Clinically. M. R. Buchanan, St. J. Brister and Fr. A. Ofosu, CRC Press, Inc.
710. Grziwa, A., Maack, S., Pühler, G., Wiegand, G., Baumeister, W. and Jaenicke, R. (1994). ”Dissociation and reconstitution of the Thermoplasma proteasome.” Eur. J. Biochem. 223, 1061-1067.
711. Bacher, A., Ritsert, K., Kis, K., Schmidt-Bäse, K., Huber, R., Ladenstein, R., Scheuring, J., Weinkauf, S. and Cushman, M. (1994). Studies of the biosynthesis of flavins. Structure and mechanism of 6.7-dimethyl-8-ribityllumazine synthase. Flavins and Flavoproteins 1993. Berlin, Walter de Gruyter and Co.
712. Daenke, S., Schramm, H. J. and Bangham, C. R. M. (1994). ”Analysis of substrate cleavage by recombinant protease of human T cell leukaemia virus type 1 reveals preferences and specificity of binding.” Journal of General Virology 75, 2233-2239.
713. Hoppe, E., Berne, P. F., Stock, D., Rasmussen, J. S., Møller, N. P. H., Ullrich, A. and Huber, R. (1994). ”Expression,purification and crystallization of human phosphotyrosine phosphatase 1B.” Eur. J. Biochem. 223, 1069-1077.
714. Bode, W. and Huber, R. (1994). ”Proteinase-protein inhibitor interactions.” Fibrinolysis 8, 161-171.
715. Steipe, B., Schiller, B., Plückthun, A. and Steinbacher, S. (1994). ”Sequence statistics reliably predict stabilizing mutations in a protein domain.” J. Mol. Biol. 240, 188-192.
716. Ladenstein, R., Ritsert, K., Huber, R., Richter, G. and Bacher, A. (1994). ”The lumazine synthase/riboflavin synthase complex of Bacillus subtilis. X-ray structure analysis of hollow reconstituted b-subunit capsids.” Eur. J. Biochem. 223, 1007-1017.
717. Schiffer, C. A., Huber, R., Wüthrich, K. and van Gunsteren, W. F. (1994). ”Simultaneous refinement of the structure of BPTI against NMR data measured in solution and X-ray diffraction data measured in single crystals.” J. Mol. Biol. 241, 588-599.
718. Tschesche, H., Bläser, J., Kleine, T., Bode, W., Reinemer, P., Grams, F., Schnierer, S., Thomssen, C., Schmitt, M., Pache, L., Jänicke, F. and Graeff, H. (1994). Structure and function of matrix metalloproteinases and their significance in breast cancer. ”International Congress Series 1050”, Prospects in Diagnosis and Treatment of Breast Cancer. M. Schmitt, H. Graeff, G. Kindermannet al, Elsevier Science B.V. Excerpta Medica/1994.
719. Schramm, H. J., Billich, A., Jaeger, E., Rücknagel, K. P., Arnold, G. and Schramm, W. (1993). ”The inhibition of HIV-1 protease by interface peptides.” Biochem. and Biophys. Res. Commun. 194, 595-600.
720. Schramm, H. J., Breipohl, G., Hansen, J., Henke, S., Jaeger, E., Meichsner, C., Rieß, G., Ruppert, D., Rücknagel, K. P., Schäfer, W. and Schramm, W. (1992). ”Inhibition of HIV-1 protease by short peptides derived from the terminal segments of the protease.” Biochem. and Biophys. Res. Commun. 184, 1980-1985.
721. Steinbacher, S., Seckler, R., Miller, S., Steipe, B., Huber, R. and Reinemer, P. (1994). ”Crystal structure of P22 tailspike protein: interdigitated subunits in a thermostable trimer.” Science 265, 383-386.
722. Gomis-Rüth, F. X., Grams, F., Yiallouros, I., Nar, H., Küsthardt, U., Zwilling, R., Bode, W. and Stöcker, W. (1994). ”Crystal structures, spectroscopic features, and catalytic properties of cobalt(II), copper(II), nickel (II), and mercury (II) derivatives of the zinc endopeptidase astacin.” J. Biol. Chem. 269, 17111-17117.
723. Demange, P., Voges, D., Benz, J., Liemann, S., Göttig, P., Berendes, R., Burger, A. and Huber, R. (1994). ”Annexin V: the key to understanding ion selectivity and voltage regulation?” TIBS 19, 272-276.
724. Gomis-Rüth, F. X., Kress, L. F., Kellermann, J., Mayr, I., Lee, X., Huber, R. and Bode, W. (1994). ”Refined 2.0 Å X-ray crystal structure of the snake venom zinc endopeptidase adamalysin II.” J. Mol. Biol. 239, 513-544.
725. Romero, A., Nar, H., Huber, R., Messerschmidt, A., Kalverda, A. P., Canters, G. W., Durley, R. and Matthews, F. S. (1994). ”Crystal structure analysis and refinement at 2.15 Å resolution of amycyanin, a type I blue copper protein, from Thiobacillus versutus.” J. Mol. Biol. 236, 1196-1211.
726. Stubbs, M. T. and Bode, W. (1994). ”Crystal structure of thrombin and thrombin complexes as a framework for antithrombotic drug design.” Perspectives in Drug Discovery and Design 1, 431-452.
727. Schulze, A. J., Huber, R., Bode, W. and Engh, R. A. (1994). ”Structural aspects of serpin inhibition.” FEBS Lett. 344, 117-124.
728. Voges, D., Berendes, R., Burger, A., Demange, P., Baumeister, W. and Huber, R. (1994). ”Three-dimensional structure of membrane-bound annexin V. A correlative electron microscopy-X-ray crystallography study.” J. Mol. Biol. 238, 199-213.
729. Schulze, A. J., Degryse, E., Speck, D., Huber, R. and Bischoff, R. (1994). ”Expression of a1-proteinase inhibitor in Escherichia coli: effects of single amino acid substitutions in the active site loop on aggregate formation.” Journal of Biotechnology 32, 231-238.
730. Bazan, J. F., Weaver, L. H., Roderick, S. L., Huber, R. and Matthews, B. W. (1994). ”Sequence and structure comparison suggest that methionine aminopeptidase, prolidase, aminopeptidase P, and creatinase share a common fold.” Proc. Natl. Acad. Sci. USA 91, 2473-2477.
731. Burger, A., Voges, D., Demange, P., Ruiz-Perez, C., Huber, R. and Berendes, R. (1994). ”Structural and electrophysiological analysis of annexin V mutants mutagenesis of human annexin V, an in vitro voltage-gated calcium channel, provides information about the structural features of the ion pathway, the voltage sensor and the ion selectivity filter.” J. Mol. Biol. 237, 479-499.
732. Turk, V. and Bode, W. (1994). Human cysteine proteinases and their inhibitors, stefins and cystatins. Biological Functions of Proteases and Inhibitors. N. Katunuma, K. Suzuki, J. Travis and H. Fritz. Tokyo, Japan Scientific Societies Press S. Karger AG, Basel.
733. Bode, W., Musil, D., Zucic, D., Turk, D., Engh, R. A., Huber, R., Kos, J., Popovic, T., Towatari, T., Katunuma, N. and Turk, V. (1994). The refined X-ray crystal structures of human and rat liver cathepsin B. Biological Functions of Proteases and Inhibitors. N. Katunuma, K. Suzuki, J. Travis and H. Fritz. Tokyo, Japan Scientific Societies Press S. Karger AG, Basel.
734. Tröger, T., Butz, T., Danielsen, E., Bauer, R., Thoenes, U., Messerschmidt, A., Huber, R., Canters, G. W. and den Blaauwen, T. (1993). ”Nuclear quadrupole interaction of 111Cd on type-1 Cu-sites in blue copper proteins.” Hyperfine Interactions 80, 1133-1141.
735. Thoenes, U., Flores, O. L., Neves, A., Devreese, B., Van Beeumen, J. J., Huber, R., Romão, M. J., LeGall, J., Moura, J. J. G. and Rodrigues-Pousada, C. (1994). [447] ”Molecular cloning and sequence analysis of the gene of the molybdenumcontaining aldehyde oxido-reductase of Desulfovibrio gigas.” Eur. J. Biochem. 220, 901-910.
736. Bode, W., Reinemer, P., Huber, R., Kleine, T., Schnierer, S. and Tschesche, H. (1994). ”The X-ray crystal structure of the catalytic domain of human neutrophil collagenase inhibited by a substrate analogue reveals the essentials for catalysis and specificity.” EMBO J. 13, 1263-1269.
737. Dirr, H., Reinemer, P. and Huber, R. (1994). ”X-ray crystal structures of cytosolic glutathione S-transferases. Implications for protein architecture, substrate recognition and catalytic function.” Eur. J. Biochem. 220, 645-661.
738. Nar, H., Huber, R., Heizmann, C. W., Thöny, B. and Bürgisser, D. (1994). ”Three-dimensional structure of 6-pyruvoyl tetrahydropterinsynthase, an enzyme involved in tetrahydropterin biosynthesis.” EMBO J. 13, 1255-1262.
739. Humm, A., Huber, R. and Mann, K. H. (1994). ”The amino acid sequences of human and pig L-arginine: glycine amidinotransferase.” FEBS Lett. 339, 101-107.
740. Reinemer, P., Grams, F., Huber, R., Kleine, T., Schnierer, S., Pieper, M., Tschesche, H. and Bode, W. (1994). ”Structural implications for the role of the N terminus in the ’superactivation’ of collagenases.” FEBS Lett. 338, 227-233.
741. Bode, W. (1993). X-ray crystal structures of thrombin in complex with D-Phe-Pro-Arg and with small benzamidine- and arginine-based ”non-peptidic” inhibitors. The Design of Synthetic Inhibitors of Thrombin. Advances in Experimental Medicine and Biology. G. Claeson. New York, Plenum Press. 340: 15-26.
742. Bode, W. and Stubbs, M. (1993). Crystal structure of thrombin as signposts to its multiple functions. Paul Ehrlich Lecture (Association de Recherches Scientifiques Paul Neumann). Actual. Chim. Thér. -.
743. Berendes, R., Voges, D., Demange, P., Huber, R. and Burger, A. (1993). ”Structure-function analysis of the ion channel selectivity in human annexin V.” Science 262, 427-430.
744. Messerschmidt, A. (1993). ”Blue copper oxidases.” Advances in Inorganic Chemistry 40, 121-185.
745. Bode, W., Gomis-Rüth, F. X., Zwilling, R. and Stöcker, W. (1993). The three dimensional structure of astacin: implications for the structure of astacins and for the zinc ligation of other metalloproteinases. Proteolysis and Protein Turnover. J. S. Bond and A. J. Barrett. Brookfield, USA, Portland Press Inc.: 13-24.
746. Bauer, M., Brandstetter, H., Turk, D., Stürzebecher, J. and Bode, W. (1993). ”Crystallographic determination of thrombin complexes with small synthetic inhibitors as a starting point for the receptor-based design of antithrombotics.” Seminars in Thrombosis and Hemostasis 19, 352-360.
747. Stubbs, M. T. and Bode, W. (1993). ”A Model for the specificity of fibrinogen cleavage by thrombin.” Seminars in Thrombosis and Hemostasis 19, 344-351.
748. Karshikov, A. and Bode, W. (1993). ”Electrostatic properties of thrombin: importance for structural stabilization and ligand binding.” Seminars in Thrombosis and Hemostasis 19, 334-343.
749. Bode, W. and Stubbs, M. T. (1993). ”Spatial structure of thrombin as a guide to its multiple sites of interaction.” Seminars in Thrombosis and Hemostasis 19, 321-333.
750. Engh, R. A., Schulze, A. J., Huber, R. and Bode, W. (1993). ”Serpin structures.” Behring Inst. Mitteilungen 93, 41-62.
751. Messerschmidt, A. (1993). Macromolecular data processing for area detectors with program system MADNES. Crystallographic Computing 6: A Window on Modern Crystallography. H. D. Flack, L. Párkányi and K. Simon, International Union of Crystallography Oxford University Press.
752. Engh, R. A., Dieckmann, T., Bode, W., Auerswald, E. A., Turk, V., Huber, R. and Oschkinat, H. (1993). ”Conformational variability of chicken cystatin. Comparison of structures determined by X-ray diffraction and NMR spectroscopy.” J. Mol. Biol. 234, 1060-1069.
753. Jap, B., Pühler, G., Lücke, H., Typke, D., Löwe, J., Stock, D., Huber, R. and Baumeister, W. (1993). ”Preliminary X-ray crystallographic study of the proteasome from Thermoplasma acidophilum.” J. Mol. Biol. 234, 881-884.
754. Butz, T., Tröger, W., Messerschmidt, A., Thoenes, U. and Huber, R. (1993). ”199mHg-derivatives of ascorbate oxidase and laccase: selective depletion and blocking of Cu-sites.” Hyperfine Interactions 80,
755. Turk, V. and Bode, W. (1993). Lysosomal cysteine proteinases and their inhibitors cystatins. Innovations in Proteinases and their Inhibitors. F. X. Avilés. Berlin, Walter de Gruyter.
756. Bode, W. (1993). The crystal structure of thrombin as a starting point for designing inhibitors. Innovations in Proteinases and their Inhibitors. F. X. Avilés. Berlin, Walter de Gruyter.
757. Bode, W. and Huber, R. (1993). Structural basis of the proteinase-protein inhibitor interaction. Innovations in Proteinases and their Inhibitors. F. X. Avilés. Berlin, Walter de Gruyter.
758. Stürzebecher, J., Prasa, D., Bretschneider, E., Bode, W., Bauer, M., Brandstetter, H., Wikström, P. and Vieweg, H. (1993). New developments in the field of benzamidine-derived thrombin inhibitors. DIC, Pathogenesis, Diagnosis and Therapy of Disseminated Intravascular Fibrin Formation. G. Müller-Berghaus, Elsevier Science Publishers.
759. Grams, F., Huber, R., Kress, L. F., Moroder, L. and Bode, W. (1993). ”Activation of snake venom metalloproteinases by a cysteine switch-like mechanism.” FEBS Lett. 335, 76-80.
760. Ficner, R. and Huber, R. (1993). ”Refined crystal structure of phycoerythrin from Porphyridium cruentum at 0.23-nm resolution and localization of the g subunit.” Eur. J. Biochem. 218, 103-106.
761. Gomis-Rüth, F. X., Kress, L. F. and Bode, W. (1993). ”First structure of a snake venom metalloproteinase: a prototype for matrix metalloproteinases/collagenases.” EMBO J. 12, 4151-4157.
762. Bode, W., Gomis-Rüth, F. X. and Stöcker, W. (1993). ”Astacis, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the ’metzincins’.” FEBS Lett. 331, 134-140.
763. Reinemer, R., Dirr, H. W. and Huber, R. (1993). The three-dimensional structure of class p glutathione S-transferase. Structure and Function of Glutathione Transferases. K. D. Tew, C. B. Pickett, T. J. Mantle, B. Mannervik and J. D. Hayes. Boca Raton, CRC Press: 65-74.
764. Padmanabhan, K., Padmanabhan, K. P., Tulinsky, A., Park, C. H., Bode, W., Huber, R., Blankenship, D. T., Cardin, A. D. and Kisiel, W. (1993). ”Structure of human des (1-45) factor Xa at 2.2 Å resolution.” J. Mol. Biol. 232, 947-966.
765. Mikkelsen, K. V., Skov, L. K., Nar, H. and Farver, O. (1993). ”Electron self-exchange in azurin: calculation of the superexchange electron tunneling rate.” Proc. Natl. Acad. Sci. USA 90, 5443-5445.
766. Romão, M. J., Barata, B. A. S., Archer, M., Lobeck, K., Moura, I., Carrondo, M. A., LeGall, J., Lottspeich, F., Huber, R. and Moura, J. J. G. (1993). ”Subunit composition, crystallization and preliminary crystallographic studies of the Desulfovibrio gigas aldehyde oxidoreductase containing molybdenum and [2Fe-2S] centers.” Eur. J. Biochem. 215, 729-732.
767. Sjölin, L., Tsai, L. C., Langer, V., Pascher, T., Karlsson, G., Nordling, M. and Nar, H. (1993). ”Structure of Pseudomonas aeruginosa zinc-azurin mutant Asn47Asp at 2.4 Å resolution.” Acta. Cryst. D49, 449-457.
768. Messerschmidt, A. (1993). [414] Ascorbate oxidase structure and chemistry. Bioinorganic Chemistry of Copper. K. D. Karlin and Z. Tyeklár. New York, Chapman and Hall.
769. Burger, A., Berendes, R., Voges, D., Huber, R. and Demange, P. (1993). ”A rapid and efficient purification method for recombinant annexin V for biophysical studies.” FEBS Lett. 329, 25-28.
770. Karshikoff, A., Reinemer, P., Huber, R. and Ladenstein, R. (1993). ”Electrostatic evidence for the activation of the glutathione thiol by Tyr7 in p-class glutathione transferases.” Eur. J. Biochem. 215, 663-670.
771. Sinning, I., Kleywegt, G. J., Cowan, S. W., Reinemer, P., Dirr, H. W., Huber, R., Gilliland, G. L., Armstrong, R. N., Ji, X., Board, P. G., Olin, B., Mannervik, B. and Jones, T. A. (1993). ”Structure determination and refinement of human a Class Glutathione Transferase A1-1, and a comparison with the µ and p class enzymes.” J.Mol.Biol. 232, 192-212.
772. Xia, C., Meyer, D. J., Chen, H., Reinemer, P., Huber, R. and Ketterer, B. (1993). ”Chemical modification of GSH transferase P1-1 confirms the presence of Arg-13, Lys-44 and one carboxylate group in the GSH-binding domain of the active site.” Biochem. J. 293, 357-362.
773. Meyer, D. J., Xia, C., Coles, B., Chen, H., Reinemer, P., Huber, R. and Ketterer, B. (1993). ”Unusual reactivity of Tyr-7 of GSH transferase P1-1.” Biochem. J. 293, 351-356.
774. Stöcker, W., Gomis-Rüth, F. X., Bode, W. and Zwilling, R. (1993). ”Implications of the three-dimensional structure of astacin for the structure and function of the astacin family of zinc-endopeptidases.” Eur. J. Biochem. 214, 215-231.
775. Bewley, M. C., Boustead, C. M., Walker, J. H., Waller, D. A. and Huber, R. (1993). ”Structure of chicken annexin V at 2.25 Å resolution.” Biochemistry 32, 3923-3929.
776. Weng, X., Luecke, H., Song, I. S., Kang, D. S., Kim, S. H. and Huber, R. (1993). ”Crystal structure of human annexin I at 2.5 Å resolution.” Protein Science 2, 448-458.
777. Messerschmidt, A., Luecke, H. and Huber, R. (1993). ”X-ray structures and mechanistic implications of three functional derivatives of ascorbate oxidase from zucchini. Reduced, peroxide and azide forms.” J. Mol. Biol. 230, 997-1014.
778. Lin, G., Bode, W., Huber, R., Chi, C. and Engh, R. (1993). ”The 0.25-nm X-ray structure of the Bowman-Birk-type inhibitor from mung bean in ternary complex with porcine trypsin.” Eur. J. Biochem. 212, 549-555.
779. Avilés, F. X., Vendrell, J., Guasch, A., Coll, M. and R., a. H. (1993). ”Advances in metallo-procarboxypeptidases. Emerging details on the inhibition mechanism and on the activation process.” Eur. J. Biochem. 211, 381-389.
780. Stubbs, M. T. and Bode, W. (1993). ”A player of many parts: the spotlight falls on thrombin’s structure.” Thrombosis Research 69, 1-58.
781. Bossemeyer, D., Engh, R. A., Kinzel, V., Ponstingl, H. and Huber, R. (1993). ”Phosphotransferase and substrate binding mechanism of the cAMP-dependent protein kinase catalytic subunit from porcine heart as deduced from the 2.0 Å structure of the complex with Mn2+ adenylyl imidodiphosphate and inhibitor peptide PKI (5-24).” EMBO J. 12, 849-859.
782. Romero, A., Hoitink, C. W. G., Nar, H., Huber, R., Messerschmidt, A. and Canters, G. W. (1993). ”X-ray analysis and spectroscopic characterization of M121Q azurin. A copper site model for stellacyanin.” J. Mol. Biol. 229, 1007-1021.
783. Gomis-Rüth, F. X., Stöcker, W., Huber, R., Zwilling, R. and Bode, W. (1993). ”Refined 1.8 Å X-ray crystal structure of astacin, a zinc-endopeptidase from the crayfish Astacus astacus. Structure determination, refinement, molecular structure and comparison with thermolysin.” J. Mol. Biol. 229, 945-968.
784. Kyritsis, P., Messerschmidt, A., Huber, R., Salmon, G. A. and Sykes, A. G. (1993). ”Pulse-radiolysis studies on the oxidized form of the multicopper enzyme ascorbate oxidase: evidence for two intramolecular electron-transfer steps.” J. Chem. Soc. Dalton Trans.731-735.
785. Mann, K., Schäfer, W., Thoenes, U., Messerschmidt, A., Mehrabian, Z. and Nalbandyan, R. (1992). ”The amino acid sequence of a type I copper protein with an unusual serine- and hydroxyproline-rich C-terminal domain isolated from cucumber peelings.” FEBS Lett. 314, 220-223.
786. Schmid, C., Ladenstein, R., Luecke, H., Huber, R. and Bacher, A. (1992). ”Crystallization and preliminary crystallographic characterization of GTP cyclohydrolase I from Escherichia coli.” J. Mol. Biol. 226, 1279-1281.
787. Berendes, R., Burger, A., Voges, D., Demange, P. and Huber, R. (1993). ”Calcium influx through annexin V ion channels into large unilamellar vesicles measure with fura-2.” FEBS Lett. 317, 131-134.
788. Szyperski, T., Güntert, P., Stone, S. R., Tulinsky, A., Bode, W., Huber, R. and Wüthrich, K. (1992). ”Impact of protein-protein contacts on the conformation of thrombin-bound hirudin studied by comparison with the nuclear magnetic resonance solution structure of hirudin (1-51).” J. Mol. Biol. 228, 1206-1211.
789. Huber, R. (1992). Allosteric effects in protein subunits and at protein membrane interfaces. The Robert A. Welch Foundation Conference on Chemical Research: XXXVI, Houston, Texas.
790. Ficner, R., Lobeck, K., Schmidt, G. and Huber, R. (1992). ”Isolation, crystallization, crystal structure analysis and refinement of B-phycoerythrin from the red alga Porphyridium sordidum at 2.2 Å resolution.” J. Mol. Biol. 228, 935-950.
791. Laber, B., Gomis-Rüth, F. X., Romão, M. J. and Huber, R. (1992). ”Escherichia coli dihydrodipicolinate synthase. identification of the active site and crystallization.” Biochem. J. 288, 691-695.
792. Huber, R., Berendes, R., Burger, A., Luecke, H. and Karshikov, A. (1992). Annexin V: crystal structure and its implications on function. The Annexins. S. E. Moss, Portland Press Research Monograph.
793. Bode, W. and Huber, R. (1992). A structural basis for proteinase-protein inhibitor interaction. Medicinal Chemistry for the 21st Century. C.G. Wermuth, N. Koga, H. König and B. W. Metcalf. Oxford, Blackwell Scientific Publications: 73-104.
794. Bode, W., Huber, R., Rydel, T. J. and Tulinsky, A. (1992). X-ray crystal structures of human a-thrombin and of the human thrombin-hirudin complex. Thrombin: Structure and Function. L. J. Berliner, Plenum Publ.Corp: 3-61.
795. Lewit-Bentley, A., Morera, S., Huber, R. and Bodo, G. (1992). ”The effect of metal binding on the structure of annexin V and implications for membrane binding.” Eur. J. Biochem. 210, 73-77.
796. Messerschmidt, A., Steigemann, W., Huber, R., Lang, G. and Kroneck, P. M. H. (1992). ”X-ray crystallographic characterisation of type-2-depleted ascorbate oxidase from zucchini.” Eur. J. Biochem. 209, 597-602.
797. Vendrell, J., Guasch, A., Coll, M., Villegas, V., Billeter, M., Wider, G., Huber, R., Wüthrich, K. and Avilés, F. X. (1992). ”Pancreatic procarboxypeptidases: their activation processes related to the structural features of the zymogens and activation segments.” Biol. Chem. Hoppe-Seyler 373, 387-392.
798. van de Kamp, M., Canters, G. W., Wijmenga, S. S., Lommen, A., Hilbers, C. W., Nar, H., Messerschmidt, A. and Huber, R. (1992). ”Complete sequential 1H and 15N nuclear magnetic resonance assignment and solution secondary structure of the blue copper protein azurin from Pseudomonas aeruginosa.” Biochemistry 31, 10194-10207.
799. Karshikov, A., Bode, W., Tulinsky, A. and Stone, S. R. (1992). ”Electrostatic interactions in the association of proteins: an analysis of the thrombin-hirudin complex.” Protein Science 1, 727-735.
800. Stürzebecher, J., Vieweg, H., Wikström, P., Turk, D. and Bode, W. (1992). ”Interactions of thrombin with benzamidine-based inhibitors.” Biol. Chem. Hoppe-Seyler 373, 491-496.
801. Schulze, A. J., Frohnert, P. W., Engh, R. A. and Huber, R. (1992). ”Evidence for the extent of insertion of the active site loop of intact a1-proteinase inhibitor in b-sheet A.” Biochemistry 31, 7560-7565.
802. Reinemer, P., Dirr, H. W., Ladenstein, R., Huber, R., Lo Bello, M., Federici, G. and Parker, M. W. (1992). ”Three-dimensional structure of class p glutathione S-transferase from human placenta in complex with S-hexylglutathione at 2.8 Å resolution.” J. Mol. Biol. 227, 214-226.
803. Bar-Shavit, R., Benezra, M., Sabbah, V., Bode, W. and Vlodavsky, I. (1992). ”Thrombin as a multifunctional protein: induction of cell adhesion and proliferation.” Am. J. Respir. Cell Mol. Biol. 6, 123-130.
804. Brandstetter, H., Turk, D., Hoeffken, H. W., Grosse, D., Stürzebecher, J., Martin, P. D., Edwards, B. F. P. and Bode, W. (1992). ”Refined 2.3 Å X-ray crystal structure of bovine thrombin complexes formed with the benzamidine and arginine-based thrombin inhibitors NAPAP, 4-TAPAP and MQPA.” J. Mol. Biol. 226, 1085-1099.
805. Baumann, U., Bode, W., Huber, R., Travis, J. and Potempa, J. (1992). ”Crystal structure of cleaved equine leucocyte elastase inhibitor determined at 1.95 Å resolution.” J. Mol. Biol. 226, 1207-1218.
806. Romão, M. J., Turk, D., Gomis-Rüth, F. X., Huber, R., Schumacher, G., Möllering, H. and Rüssmann, L. (1992). ”Crystal structure analysis, refinement and enzymatic reaction mechnism of N-carbamoylsarcosine amidohydrolase from Arthrobacter sp. at 2.0 Å resolution.” J. Mol. Biol. 226, 1111-1130.
807. Nar, H., Messerschmidt, A., Huber, R., van de Kamp, M. and Canters, G. W. (1992). ”Crystal structure of Pseudomonas aeruginosa apo-azurin at 1.85 Å resolution.” FEBS Lett. 306, 119-124.
808. Manoharan, T. H., Gulick, A. M., Reinemer, P., Dirr, H. W., Huber, R. and Fahl, W. E. (1992). ”Mutational substitution of residues implicated by crystal structure in binding the substrate glutathione to human glutathione-S-transferase p.” J. Mol. Biol. 226, 319-322.
809. Bode, W., Gomis-Rüth, F. X., Huber, R., Zwilling, R. and Stöcker, W. (1992). ”Structure of astacin and implications for activation of astacins and zinc-ligation of collagenases.” Nature 358, 164-167.
810. Bacher, A., Weinkauf, S., Bachmann, L., Ritsert, K., Baumeister, W., Huber, R. and Ladenstein, R. (1992). ”Electron microscopy of decorated crystals for the determination of crystallographic rotation and translation parameters in large protein complexes.” J. Mol. Biol. 225, 1065-1073.
811. Bode, W., Turk, D. and Karshikov, A. (1992). ”The refined 1.9 Å X-ray crystal structure of D-Phe-Pro-Arg chloromethylketone-inhibited human a-thrombin: structure analysis, overall structure, electrostatic properties, detailed active-site geometry, and structure-function relationships.” Protein Science 1, 426-471.
812. Messerschmidt, A. (1992). ”Structural studies on copper containing plant oxidases.” Biochemical Society Transactions 20, 364-368.
813. Steipe, B., Plückthun, A. and Huber, R. (1992). ”Refined crystal structure of a recombinant immunoglobulin domain and a complementarity-determining region 1-grafted mutant.” J. Mol. Biol. 225, 739-753.
814. Stubbs, M. T., Oschkinat, H., Mayr, I., Huber, R., Angliker, H., Stone, S. R. and Bode, W. (1992). ”The interaction of thrombin with fibrinogen.” Eur. J. Biochem. 206, 187-195.
815. Nar, H., Huber, R., Messerschmidt, A., Filippou, A. C., Barth, M., Jaquinod, M., van de Kamp, M. and Canters, G. W. (1992). ”Characterization and crystal structure of zinc azurin, a by-product of heterologous expression in Escherichia coli of Pseudomonas aeruginosa copper azurin.” Eur. J. Biochem. 205, 1123-1129.
816. Huber, R. (1992). ”Proteinstrukturen, Grundlagen für Biophysik, Biochemie und Medikament-Design.” Nova acta Leopoldina 281, 249-250.
817. Huber, R., Berendes, R., Burger, A., Luecke, H. and Karshikov, A. (1992). ”Annexin V – crystal structure and its implications on function.” Behring Inst. Mitt. 91, 107-125.
818. Martin, P. D., Robertson, W., Turk, D., Huber, R., Bode, B. and Edwards, B. F. P. (1992). ”The structure of residues 7-16 of the Aa-chain of human fibrinogen bound to bovine thrombin at 2.3 Å resolution.” J. Biol. Chem. 267, 7911-7920.
819. Messerschmidt, A., Ladenstein, R., Huber, R., Bolognesi, M., Avigliano, L., Petruzzelli, R., Rossi, A. and Finazzi, A. (1992). ”Refined crystal structure of ascorbate oxidase at 1.9 Å resolution.” J. Mol. Biol. 224, 179-205.
820. Guasch, A., Coll, M., Avilés, F. X. and Huber, R. (1992). ”Three-dimensional structure of porcine pancreatic procarboxypeptidase A. A comparison of the A and B zymogens and their determinants for inhibition and activation.” J. Mol. Biol. 224, 141-157.
821. Bode, W. and Huber, R. (1992). ”Natural protein proteinase inhibitors and their interaction with proteinases.” Eur. J. Biochem. 204, 433-451.
822. Billeter, M., Vendrell, G., Wider, G., Avilés, F. X., Coll, M., Guasch, A., Huber, R. and Wüthrich, K. (1992). ”Comparison of the NMR solution structure with the X-ray crystal structure of the activation domain from procarboxypeptidase B.” Journal of Biomolecular NMR 2, 1-10.
823. Huber, R., Berendes, R., Burger, A., Schneider, M., Karshikov, A., Luecke, H., Römisch, J. and Paques, E. (1992). ”Crystal and molecular structure of human annexin V after refinement.” J. Mol. Biol. 223, 683-704.
824. Karshikov, A., Berendes, R., Burger, A., Cavalié, A., Lux, H. D. and Huber, R. (1992). ”Annexin V membrane interaction: an electrostatic potential study.” Eur. Biophys. J. 20, 337-344.
825. Schulze, A. J., Huber, R., Degryse, E., Speck, D. and Bischoff, R. (1991). ”Inhibitory activity and conformational transition of a1-proteinase inhibitor variants.” Eur. J. Biochem. 202, 1147-1155.
826. Bode, W. and Huber, R. (1991). Proteinase-protein inhibitor interaction. 42. Colloquium Mosbach, Springer-Verlag Berlin Heidelberg.
827. Kessler, H., Mronga, S., Müller, G., Moroder, L. and Huber, R. (1991). ”Conformational analysis of a IgG1 hinge peptide derivate in solution determined by NMR spectroscopy and refined by restrained molecular dynamics simulations.” Biopolymers 31, 1189-1204.
828. Dirr, H. W. and Reinemer, P. (1991). ”Equilibrium unfolding of class p glutathione S-transferase.” Biochemical and Biophysical Research Communications 180, 294-300.
829. Nar, H., Messerschmidt, A., Huber, R., van de Kamp, M. and Canters, G. W. (1991). ”Crystal structure analysis of oxidized Pseudomonas aeruginosa azurin at pH 5.5 and pH 9.0 A pH-induced conformational transition involves a peptide bond flip.” J. Mol. Biol. 221, 765-772.
830. Rydel, T. J., Tulinsky, A., Bode, W. and Huber, R. (1991). ”Refined structure of the hirudin-thrombin complex.” J. Mol. Biol. 221, 583-601.
831. Bode, W. and Huber, R. (1991). ”Proteinase-protein inhibitor interaction.” Biomed. Biochim. Acta 50, 437-446.
832. Weinkauf, S., Bacher, A., Baumeister, W., Ladenstein, R., Huber, R. and Bachmann, L. (1991). ”Correlation of metal decoration and topochemistry on protein surfaces.” J. Mol. Biol. 221, 637-645.
833. Daube, H., Billich, A., Mann, K. and Schramm, H. J. (1991). ”Cleavage of phosphorylase kinase and calcium-free calmodulin by HIV-1 protease.” Biochem. and Biophys. Research Communications, 178, 892-898.
834. Stubbs, M. T. and Huber, R. (1991). ”An analytical packing function employing fourier transforms.” Acta Cryst. A47, 521-526.
835. Karshikov, A., Duerring, M. and Huber, R. (1991). ”Role of electrostatic interaction in the stability of the hexamer of constitutive phycocyanin from Fremyella diplosiphon.” Protein Engineering 4, 681-690.
836. Turk, V. and Bode, W. (1991). ”The cystatins: protein inhibitors of cysteine proteinases.” FEBS Lett. 285, 213-219.
837. Turk, D., Stürzebecher, J. and Bode, W. (1991). ”Geometry of binding of the Na-tosylated piperidides of m-amidino- and p-guanidino phenylalanine to thrombin and trypsin. X-ray crystal structures of their trypsin complexes and modeling of their thrombin complexes.” FEBS Lett. 287, 133-138.
838. Musil, D., Zucic, D., Turk, D., Engh, R. A., Mayr, I., Huber, R., Popovic, T., Turk, V., Towatari, T., Katunuma, N. and Bode, W. (1991). [344] ”The refined 2.15 Å X-ray crystal structure of human liver cathepsin B: the structural basis for its specificity.” EMBO J. 10, 2321-2330.
839. Musil, D., Bode, W., Huber, R., Laskowski, M., Lin, T. Y. and Ardelt, W. (1991). ”Refined X-ray crystal structures of the reactive site modified ovomucoid inhibitor third domains from silver pheasant (OMSVP3*) and from Japanese quail (OMJPQ3*).” J. Mol. Biol. 220, 739-755.
840. Brisson, A., Mosser, G. and Huber, R. (1991). ”Structure of soluble and membrane-bound human annexin V.” J. Mol. Biol. 220, 199-203.
841. Mann, K., Schlenkrich, T., Bauer, M. and Huber, R. (1991). ”The amino-acid sequence of three proteins of photosystem I of the cyanobacterium Fremyella diplosiphon (Calothrix sp PCC 7601).” Biol. Chem. Hoppe-Seyler 372, 519-524.
842. Engh, R. A. and Huber, R. (1991). ”Accurate bond and angle parameters for X-ray protein structure refinement.” Acta. Cryst. A47, 392-400.
843. Reinemer, P., Dirr, H. W., Ladenstein, R., Schäffer, J., Gallay, O. and Huber, R. (1991). ”The three-dimensional structure of class p glutathione S-transferase in complex with glutathione sulfonate at 2.3. Å resolution.” EMBO J. 10, 1997-2005.
844. Holak, T. A., Habazettl, J., Oschkinat, H. and Otlewski, J. (1991). ”Structures of proteins in solution derived from homonuclear three-dimensional NOE-NOE nuclear magnetic resonance spectroscopy. High-resolution structure of squash trypsin inhibitor.” J. Am. Chem. Soc. 113, 3196-3198.
845. Nilges, M., Habazettl, J., Brünger, A. T. and Holak, T. A. (1991). ”Relaxation matrix refinement of the solution structure of squash trypsin inhibitor.” J. Mol. Biol. 219, 499-510.
846. Baumann, U., Huber, R., Bode, W., Grosse, D., Lesjak, M. and Laurell, C. B. (1991). ”Crystal structure of cleaved human a1-antichymotrypsin at 2.7 Å resolution and its comparison with other serpins.” J. Mol. Biol. 218, 595-606.
847. Nar, H., Messerschmidt, A., Huber, R., van de Kamp, M. and Canters, G. W. (1991). ”X-ray crystal structure of the two site-specific mutants His35Gln and His35Leu of azurin from Pseudomonas aeruginosa.” J. Mol. Biol. 218, 427-447.
848. Dirr, H. W., Mann, K. H., Huber, R., Ladenstein, R. and Reinemer, P. (1991). ”Class p glutathione-S-transferase from pig lung. Purification, biochemical characterization, primary structure and crystallization.” Eur. J. Biochem. 196, 693-698.
849. Bode, W. and Huber, R. (1991). ”Ligand binding: proteinase-protein inhibitor interactions.” Current Opinion in Structural Biology 1, 45-52.
850. Huber, R. (1990). ”Proteinstrukturforschung,Wege zu einer besseren Chemie?” TUM 2/312.
851. Duerring, M., Schmidt, G. B. and Huber, R. (1991). ”Isolation, crystallization, crystal structure analysis and refinement of constitutive C-phycocyanin from the chromatically adapting cyanobacterium Fremyella diplosiphon at 1.66 Å resolution.” J. Mol. Biol. 217, 577-592.
852. Wiegand, G. (1990). How do you get large protein crystals? Two familiar laboratory methods improved and simplified. Modern methods in protein-and nucleic acid Research. H. Tschesche. Berlin, New York, Walter de Gruyter.
853. Coll, M., Guasch, A., Avilés, F. X. and Huber, R. (1991). ”Three-dimensional structure of porcine procarboxypeptidase B: a structural basis of its inactivity.” EMBO J. 10, 1-9.
854. Schulze, A. J., Baumann, U., Knof, S., Jaeger, E., Huber, R. and Laurell, C. B. (1990). ”Structural transition of a1-antitrypsin by a peptide sequentially similar to b-strand s4A.” Eur. J. Biochem. 194, 51-56.
855. Huber, R. (1990). Proteinstrukturforschung – Wege zu einer besseren Chemie ? Chemie + Fortschritt. Mitgliederversammlung 1990.
856. Huber, R., Schneider, M., Mayr, I., Römisch, J. and Paques, E. (1990). ”The calcium binding sites in human annexin V by crystal structure analysis at 2.0 Å resolution.” FEBS Lett. 275, 15-21.
857. Huber, R., Römisch, J. and Paques, E. (1990). ”The crystal and molecular structure of human annexin V, an anticoagulant protein that binds to calcium and membranes.” EMBO J. 9, 3867-3874.
858. Chow, M. M., Meyer, E. F., Jr., Bode, W., Kam, C. M., Radhakrishnan, R., Vijayalakshmi and Powers, J. C. (1990). ” The 2.2 Å resolution X-ray crystal structure of the complex of trypsin inhibited by 4-chloro-3-ethoxy-7-guanidinoisocoumarin: a proposed model of the thrombin-inhibitor complex.” J. Am. Chem. Soc. 112, 7783-7789.
859. Bode, W., Turk, D. and Stürzebecher, J. (1990). ” Geometry of binding of the benzymidine- and arginine-based inhibitors Na-(2-naphtyl-sulphonyl-glycyl)-DL-p-amidinophenylalanyl-piperidine (NAPAP) and (2R, 4R)-4-methyl-1-[Na-(3-methyl-1,2,3,4-tetrahydro-8-quinolinesulphonyl)-L-arginyl]-2-piperidine carboxylic acid (MQPA) to human a-thrombin.” Eur. J. Biochem. 193, 175-182.
860. Grütter, M. G., Priestle, J. P., Rahuel, J., Grossenbacher, H., Bode, W., Hofsteenge, J. and Stone, S. R. (1990). ” Crystal structure of the thrombin-hirudin complex: a novel mode of serine protease inhibition.” EMBO J. 9, 2361-2365.
861. Messerschmidt, A., Schneider, M. and Huber, R. (1990). ”ABSCOR: a scaling and absorption correction program for the FAST area detector diffractometer.” J. Appl. Cryst. 23, 436-439.
862. Bode, W. (1990). ”The structure of the cysteine proteinase inhibitor cystatin and its probable mode of interaction with cysteine proteinases.” Zeszyty Naukowe Uniwersytetu Jagiellonskiego Prace Z Biologii Molekularnej Z. CMLXXXVI, 139-144.
863. Bode, W. (1990). ”Structural requirements for efficient inhibition of human leukocyte elastase by native and modified inhibitors.” Zeszyty Naukowe Uniwersytetu Jagiellonskiego Prace Z Biologii Molekularnej Z. CMLXXXVI, 33-38.
864. Schott, K., Ladenstein, R., König, A. and Bacher, A. (1990). ”The lumazine synthase-riboflavin synthase complex of Bacillus subtilis. Crystallization of reconstituted icosahedral b-subunit capsids.”
865. The Journal of Biol. Chem. 265, 12686-12689. Bacher, A., Schott, K., Volk, R. and Ladenstein, R. (1989). Pteridines in riboflavin biosynthesis. Ninth international Symposium on Pteridines and Folic acid Derivates – Chemical, Biological and Clinical aspects, Zurich, Switzerland, Sept. 3-8, 1989, Walter de Gruyter, Berlin.
866. Weinkauf, S., Bacher, A., Schott, K., Ladenstein, R., Baumeister, W. and Bachmann, L. (1989). High resolution electron microscopy in crystals of the icosahedral lumazine synthase/riboflavin synthase complex. Ninth international Symposium on Pteridines and Folic acid Derivates – Chemical, Biological and Clinical aspects, Zurich, Switzerland, Sept. 3-8, 1989, Walter de Gruyter, Berlin.
867. Schott, K., Ladenstein, R., König, A. and Bacher, A. (1989). Structure of the lumazine synthase/riboflavinsynthase complex of Bacillus subtilis: crystallization of hollow reconstituted b60 capsids. Ninth international Symposium on Pteridines and Folic acid Derivates – Chemical, Biological and Clinical aspects, Zurich, Switzerland, Sept. 3-8, 1989, Walter de Gruyter, Berlin.
868. Coll, M., Knof, S. H., Ohga, Y., Messerschmidt, A., Huber, R., Moellering, H., Rüssmann, L. and Schumacher, G. (1990). ”Enzymatic mechanism of creatine amidinohydrolase as deduced from crystal structures.” J. Mol. Biol. 214, 597-610.
869. Rydel, T., Ravichandran, K. G., A., T., Bode, W., Huber, R., Fenton, J. W. and Roitsch, C. (1990). ”The structure of a complex of recombinant hirudin and human a-thrombin.” Science 249, 277-280.
870. Glockshuber, R., Steipe, B., Huber, R. and Plückthun, A. (1990). ”Crystallization and preliminary X-ray studies of the VL domain of the antibody McPC603 produced in Escherichia coli.” J. Mol. Biol. 213, 613-615.
871. Bode, W., Engh, R., Musil, D., Laber, B., Stubbs, M. T., Huber, R. and Turk, V. (1990). ”Mechanism of interaction of cysteine proteinases and their protein inhibitors as compared to the serine proteinase-inhibitor interaction.” Biol. Chem. Hoppe-Seyler 371, 111-118.
872. Engh, R. A., Wright, H. T. and Huber, R. (1990). ”Modeling the intact form of the a1-proteinase inhibitor.” Protein Engineering 3, 469-477.
873. Stubbs, M. T., Laber, B., Bode, W., Huber, R., Jerala, R., Lenarcic, B. and Turk, V. (1990). ”The refined 2.4 Å X-ray crystal structure of recombinant human stefin B in complex with the cysteine proteinase papain: a novel type of proteinase inhibitor interaction.” EMBO J. 9, 1939-1947.
874. Wright, H. T., Qian, H. X. and Huber, R. (1990). ”Crystal structure of plakalbumin, a proteolytically nicked form of ovalbumin. Its relationship to the structure of cleaved a1-proteinase inhibitor.” J. Mol. Biol. 213, 513-528.
875. Ladenstein, R. and Bacher, A. (1989). Exploitation of geometric redundancies as a source of phase information in X-ray structure analysis of symmetric protein assemblies. Protein Structure and Engineering. O. Jardetzky, Plenum Publishing Corporation: 3-33.
876. Stubbs, M., Summers, L., Mayr, I., Schneider, M., Bode, W., Huber, R., Ries, A. and Kühn, K. (1990). ”Crystals of the NC1 domain of human type IV collagen.” J. Mol. Biol. 211, 683-684.
877. Duerring, M., Huber, R., Bode, W., Ruembeli, R. and Zuber, H. (1990). ”Refined three-dimensional structure of phycoerythrocyanin from the cyanobacterium Mastigocladus laminosus at 2.7 Å.” J. Mol. Biol. 211, 633-644.
878. Messerschmidt, A. and Huber, R. (1990). ”The blue oxidases, ascorbate oxidase, laccase and ceruloplasmin. Modelling and structural relationships.” Eur. J. Biochem. 187, 341-352.
879. Huber, R. (1990). ”A structural basis of light energy and electron transfer in biology. (E. Antonini Plenary Lecture).” Eur. J. Biochem. 187, 283-305.
880. Huber, R. (1989). ”A structural basis of light energy and electron transfer in biology.(Nobel Lecture).” Bioscience Reports 9, 635-673.
881. Karshikov, A., Engh, R., Bode, W. and Atanasov, B. P. (1989). ”Electrostatic interactions in proteins: calculations of the electrostatic term of free energy and the electrostatic potential field.” Eur. Biophys. J. 17, 287-297.
882. D’ Andrea, G., Maccarone, M., Oratore, A., Avigliano, L. and Messerschmidt, A. (1989). ”Kinetic features of ascorbic acid oxidase after partial deglycation.” Biochem. J. 264, 601-604.
883. Huber, R. and Carrell, R. W. (1989). ”Implications of the three-dimensional structure of a1-antitrypsin for structure and function of serpins.” Biochemistry 28, 8951-8966.
884. Holak, T. A., Gondol, D., Otlewski, J. and Wilusz, T. (1989). ”Determination of the complete three-dimensional structure of the trypsin inhibitor from squash seeds in aqueous solution by nuclear magnetic resonance and a combination of distance geometry and dynamical simulated annealing.” J. Mol. Biol. 210, 635-648.
885. Holak, T. A., Bode, W., Huber, R., Otlewski, J. and Wilusz, T. (1989). ”Nuclear magnetic resonance solution and X-ray structure of squash trypsin inhibitor exhibit the same conformation of the proteinase binding loop.” J. Mol. Biol. 210, 649-654.
886. Messerschmidt, A., Rossi, A., Ladenstein, R., Huber, R., Bolognesi, M., Marchesini, A., Petruzelli, R. and Finazzi-Agro, A. (1988). Preliminary X-ray crystal structure and partial cDNA-sequence of ascorbate oxidase from zucchini. Oxidases and related redox systems. T. E. King, H. S. Mason and M. Morrison. New York, Alan R. Liss, Inc. 274: 285-288.
887. Bode, W. (1988). X-ray crystal structures of components of the kallikrein-kinin system originally Discovered by Frey, Kraut and Werle. The Kallikrein-Kinin System in Health and Disease. International Symposium, Munich.
888. Roth, M., Lewit-Bentley, A., Michel, H., Deisenhofer, J., Huber, R. and Oesterhelt, D. (1989). ”Detergent structure in crystals of a bacterial photosynthetic reaction centre.” Nature 340, 659-662.
889. Huber, R. (1989). ”A structural basis of light energy and electron transfer in biology. (Nobel Lecture).” Chemica Scripta 29, 103-122.
890. Bode, W., Mayr, I., Baumann, U., Huber, R., Stone, S. R. and Hofsteenge, J. (1989). ”The refined 1.9 Å crystal structure of human a-thrombin: interaction with D-Ph-Pro-Arg chloromethylketone and significance of the Tyr-Pro-Pro-Trp insertion segment.” EMBO J. 8, 3467-3475.
891. Huber, R. (1989). ”Flexibility and rigidity in proteins and protein pigment complexes.” Nova acta Leopoldina NF 61, 31-33.
892. Bode, W., Musil, D., Engh, R., Huber, R., Brzin, J., Kos, J. and Turk, V. (1989). The 2.0 Å X-ray crystal structure of chicken egg white cystatin and its probable interaction with papain. 7th ICOP Meeting, Shimoda, Japan, Japan Scientific Societies Press,Tokyo.
893. Deisenhofer, J., Huber, R. and Michel, H. (1989). The structure of the photochemical reaction center of Rhodopseudomonas viridis and its implications for function. PREDICTION OF PROTEIN STRUCTURE AND THE PRINCIPLES OF PROTEIN CONFORMATION. G. D. Fasman, Plenum Publishing Corporation: 99-116.
894. Karshikov, A. and Ladenstein, R. (1989). ”Electrostatic effects in a large enzyme complex: subunit interactions and electrostatic potential field of the icosahedral b60, capsid of heavy riboflavin synthase.” Proteins 5, 248-257.
895. Huber, R. (1989). ”A structural basis of light energy and electron transfer in biology. (Nobel Lecture).” EMBO J. 8, 2125-2147.
896. Huber, R. (1989). ”A structural basis of light energy and electron transfer in biology.(Nobel Lecture).” Angew. Chemie 28, 848-869.
897. Huber, R. (1989). ”Eine strukturelle Grundlage für die Übertragung von Lichtenergie und Elektronen in der Biologie.” Angew. Chemie 101, 849-871.
898. Laber, B., Krieglstein, K., Henschen, A., Kos, J., Turk, V., Huber, R. and Bode, W. (1989). ”The cysteine proteinase inhibitor chicken cystatin is a phosphoprotein.” FEBS Lett. 248, 162-168.
899. Billeter, M., Kline, A. D., Braun, W., Huber, R. and Wüthrich, K. (1989). ”Comparison of the high resolution structures of the a-amylase inhibitor tendamistat determined by nuclear magnetic resonance in solution and by X-ray diffraction in single crystals.” J. Mol. Biol. 206, 677-687.
900. Braun, W., Epp, O., Wüthrich, K. and Huber, R. (1989). ”Solution of the phase problem in the X-ray diffraction method for proteins with the nuclear magnetic resonance solution structures as initial model. patterson search and refinement for the a-amylase inhibitor tendamistat.” J. Mol. Biol. 206, 669-676.
901. Bode, W., Meyer, E. and Powers, J. C. (1989). ”Human leukocyte and porcine pancreatic elastase: X-ray crystal structures, mechanism, substrate specificity, and mechanism-based inhibitors.” Biochem. 28, 1951-1963.
902. Messerschmidt, A., Rossi, A., Ladenstein, R., Huber, R., Bolognesi, M., Gatti, G., Marchesini, A., Petruzzelli, R. and Finazzi-Agrò, A. (1989). ”X-ray crystal structure of the blue oxidase ascorbate oxidase from zucchini.” J. Mol. Biol. 206, 513-529.
903. Engh, R., Löbermann, H., Schneider, M., Wiegand, G., Huber, R. and Bertil Laurell, C. (1989). ”The S variant of human a1-antitrypsin, structure and implications for function and metabolism.” Protein Eng. 2, 407-415.
904. Hinrichsen, A., Böckl, H. J. and Schramm, H. J. (1989). ”Electron microscopical examination of different aggregation and decomposition states of phosphorylase kinase.” Biol. Chem. Hoppe-Seyler 370, 125-133.
905. Machleidt, W., Thiele, U., Laber, B., Assfalg-Machleidt, I., Esterl, A., Wiegand, G., Kos, J., Turk, V. and Bode, W. (1989). ”Mechanism of inhibition of papain by chicken egg white cystatin. inhibition constants of N-terminally truncated forms and cyanogen bromide fragments of the inhibitor.” FEBS Lett. 243, 234-238.
906. Auerswald, E. A., Genenger, G., Assfalg-Machleidt, I., Kos, J. and Bode, W. (1989). ”Synthesis of a (desSer1 Ile29 Leu89) chicken cystatin gene, expression in E. coli as fusion protein and its isolation.” FEBS Lett. 243, 186-192.
907. Huber, R. (1988). Flexibility and rigidity of proteins and protein-pigment complexes. Protein structure function relationship. Z. H. Zaidi, Elsevier Science Publishers B.V. (Biomedical Division): 115-137.
908. Bode, W. (1988). The specific interaction of human leucocyte elastase with various protein inhibitors. 39. Colloquium Mosbach, Springer-Verlag, Berlin.
909. Bode, W., Greyling, H. J., Huber, R., Otlewski, J. and Wilusz, T. (1989). ”The refined 2.0 Å X-ray crystal structure of the complex formed between bovine b-trypsin and CMTI-I, a trypsin inhibitor from squash seeds (Cucurbita maxima). Topological similarity of the squash seed inhibitors with the carbopeptidase A inhibitor from potaoes.” FEBS Lett. 242, 285-292.
910. Hoeffken, H. W., Knof, S. H., Bartlett, P. A., Huber, R., Moellering, H. and Schumacher, G. (1988). ”Crystal structure determination, refinement and molecular model of creatine aminohydrolase from Pseudomonas putida.” J. Mol. Biol. 204, 417-433.
911. Schramm, H. and Witke, W. (1988). ”Electron microscopical localization of the a2-macroglobulin thiol ester sites.” Biol. Chem. Hoppe-Seyler 369, 1151-1156.
912. Schäffer, J., Gallay, O. and Ladenstein, R. (1988). ”Glutathione transferase from bovine placenta. Preparation, biochemical characterization, crystallization and preliminary crystallographic analysis of a neutral class p enzyme.” J. Biol. Chem. 263, 17405-17411.
913. Ladenstein, R., Schneider, M., Huber, R., Bartunik, H. D., Wilson, K., Schott, K. and Bacher, A. (1988). ”Heavy riboflavin synthase from Bacillus subtilis. Crystal structure analysis of the Icosahedral b60 capsid at 3.3 Å resolution.” J. Mol. Biol. 203, 1045-1070.
914. Fabry, S., Lehmacher, A., Bode, W. and Hensel, R. (1988). ”Expression of the glyceraldehyde-3-phosphate dehydrogenase gene from the extremely thermophilic archaebacterium Methanothermus fervidus in E. coli. Enzyme purification, crystallization and preliminary crystal data.” FEBS Lett. 237, 213-217.
915. Messerschmidt, A., Rossi, A., Ladenstein, R., Huber, R., Bolognesi, M., Marchesini, A., Petruzelli, R. and Finazzi, A. (1988). Preliminary X-ray crystal structure and partial cDNA-sequence of ascorbate oxidase from yzcchini. Oxidases and related redox systems, Alan R. Liss. Inc.: 285-288.
916. Ladenstein, R., Schneider, M., Huber, R., Schott, K. and Bacher, A. (1988). ”The structure of the icosahedral b60 capsid of heavy riboflavin synthase from Bacillus subtilis.” Zeitschrift für Kristallographie 185, 122-124.
917. Duerring, M., Huber, R. and Bode, W. (1988). ”The structure of g-N-methylasparagine in C-phycocyanin from Mastigocladus laminosus and Agmenellum quadruplicatum.” FEBS Lett. 236, 167-170.
918. Bode, W., Engh, R., Musil, D., Thiele, U., Huber, R., Karshikov, A., Brzin, J., Kos, J. and Turk, V. (1988). ”The 2.0 Å X-ray crystal structure of chicken egg white cystatin and its possible mode of interaction with cysteine proteinases.” EMBO J. 7, 2593-2599.
919. Wei, A., Mayr, I. and Bode, W. (1988). ”The refined 2.3 Å crystal structure of human leukocyte elastase in a complex with a valine chloromethyl ketone inhibitor.” FEBS Lett. 234, 367-373.
920. Declerc, J. P., Tinant, B., Parello, J., Etienne, G. and Huber, R. (1988). ”Crystal structure determination and refinement of pike 4.10 parvalbumin (minor component from Esox lucius).” J. Mol. Biol. 202, 349-353.
921. Schneider, S., Scharnagl, C., Duerring, M., Schirmer, T. and Bode, W. (1988). Effect of protein environment and excitonic coupling on the excited-state properties of the bilinchromophores in C-phycocyanin. Photosynthetic light-harvesting systems. Scheer and Schneider. Berlin, Walter de Gruyter and Co: 483-490.
922. Meyer, E., Cole, G., Rhadakrishnan, R. and Epp, O. (1988). ”Structure of native porcine pancreatic elastase at 1.65 Å resolution.” Acta Crystallographica B44, 26-38.
923. Turk, V., Brzin, J., Lenarcic, B., Locnikar, P., Popovic, T., Ritonja, A., Rabnik, J., Bode, W. and Machleidt, W. (1985). ”Structure and function of lysosomal cysteine proteinases and their protein inhibitors.” Intracellular Protein Catabolism91-103.
924. Grütter, M. G., Fendrich, G., Huber, R. and Bode, W. (1988). ”The 2.5 Å X-ray crystal structure of the acid-stable proteinase inhibitor from human mucous secretions analysed in its complex with bovine a-chymotrypsin.” EMBO J. 7, 345-351.
925. Ladenstein, R., Huber, R., Schott, K., Schneider, M., König, A. and Bacher, A. (1987). The icosahedral b60 capsid of heavy riboflavin synthase (6.7-dimethyl-8-ribityllumazine synthase/riboflavin synthase). Flavins and Flavoproteins. D.E. Edmundson and D.B. McCormick. Berlin, Walter de Gruyter and Co: 441-444.
926. Huber, R. (1987). ”Flexibility and rigidity, requirements for the function of proteins and protein pigment complexes.” Biochem. Soc. Trans. 15, 1009-1020.
927. Michel-Beyerle, M. E., Plato, M., Deisenhofer, J., Michel, H., Bixon, M. and Jortner, J. (1988). ”Undirectionality of charge separation in reaction centers photosynthetic bacteria.” Biochimica et Biophysica Acta 932, 52-70.
928. Michel, H. and Deisenhofer, J. (1988). ”Relevance of the photosynthetic reaction center from purple bacteria to the structure of photosystem II.” Biochem. 27, 1-7.
929. Huber, R. (1988). ”Flexibility and rigidity of proteins and protein-pigment complexes.” Angew. Chem. Int. E. Engl. 27, 79-88.
930. Huber, R. (1988). ”Beweglichkeit und Starrheit in Proteinen und Protein-Pigment-Komplexen.” Angew. Chemie. 100, 79-89. Huber, R., Schneider, M., Mayr, I., Müller, R., Deutzmann, R., Suter, F., Zuber, H., Falk, H. and Kayser, H. (1987). ”Molecular structure of the bilin binding protein (BBP) from Pieris brassicae after refinement at 2.0 Å resolution.” J. Mol. Biol. 198, 499-513.
931. Schirmer, T. and Vincent, M. G. (1987). ”Polarized absorption and fluorescence spectra of single crystals of C-phycocyanin.” Biochem. et Biophys. Acta 893, 379-385.
932. Tschesche, H., Kolkenbock, H. and Bode, W. (1987). ”The covalent structure of the elastase inhibitor from Anemonia sulcata – a ”Non-Classical” Kazal-type protein.” Biol. Chem. Hoppe-Seyler 368, 1297-1304.
933. Brünger, A. T., Huber, R. and Karplus, M. (1987). ”Trypsinogen-trypsin transition: a molecular dynamics study of induced conformational change in the activation domain.” Biochem. 26, 5153-5162.
934. Messerschmidt, A. and Pflugrath, J. W. (1987). ”Crystal orientation and XY-ray pattern prediction routines for area detector diffractometer systems in macromolecular crystallography.” J. Appl. Cryst. 20, 306-315.
935. Schmidt, G., Siebzehnrübl, S., Fischer, R., Rüdiger, W., Scheer, H., Schirmer, T., Bode, W. and Huber, R. (1987). ”ZZE-configuration of chromophore b-153* in C-phycocyanin from Mastigocladus laminosus.” Z. Naturforsch. 42c, 845-848.
936. Schirmer, T., Bode, W. and Huber, R. (1987). ”Refined three-dimensional structures of two cyanobacterial C-phycocyanins at 2.1 and 2.5 Å resolution.” J. Mol. Biol. 196, 677-695.
937. Bode, W., Papamokos, E. and Musil, D. (1987). ”The high-resolution X-ray crystal structure of the complex formed between subtilisin Carlsberg and eglin c, an elastase inhibitor from the leech Hirudo medicinalis.” Eur. J. Biochem. 166, 673-692.
938. Huber, R. (1987). The structural basis of photosynthetic light reactions in bacteria. Biological Organization: macromolecular interactions at high resolution. R. M. Burnett and H. J. Vogel. Orlando, Academic Press Inc.: 283-286.
939. Michel, H. and Deisenhofer, J. (1987). The structural organization of photosynthetic reaction centers. Progress in photosynthesis research. J. Biggins, Martinus Nijhoff Publishers: 353-362.
940. Deisenhofer, J. and Michel, H. (1987). The structure of the photosynthetic reaction center from Rhodopseudomonas viridis. Photobiochemistry and Photobiophysics, Elsevier: Suppl.133-140.
941. Ladenstein, R. and Epp, O. (1987). Catalysis by seleno glutathione peroxidase. Biological Macromolecules and Assemblies – Active Sites of Enzymes. F. A. Jurnak and A. Mc.Pherson, John Wiley and Sons, Inc. 3: 524-558.
942. Ludwig, H. C., Lottspeich, F., Henschen, A., Ladenstein, R. and Bacher, A. (1987). ”Heavy riboflavin synthase of Bacillus subtilis.” J. Biol. Chem. 262, 1016-1021.
943. Ladenstein, R., Bacher, A. and Huber, R. (1987). ”Some observations of a correlation between the symmetry of large heavy-atom complexes and their binding sites on proteins.” J. Mol. Biol. 195, 751-753.
944. Bode, W., Schirmer, T., Huber, R., Sidler, W. and Zuber, H. (1987). X-ray structure of the light-harvesting biliprotein C-phycocyanin from M. laminosus. Crystallography molecular biology. D. Moras, J. Drenth, D. Strandberg and K. Wilson, NATO ASI Series, Series A: Life Sciences. 126.
945. Huber, R., Schneider, M., Epp, O., Mayr, I., Messerschmidt, A., J., P. and Kayser, H. (1987). ”Crystallization, crystal structure analysis and preliminary molecular model of the bilin binding protein from the insect Pieris brassicae.” J. Mol. Biol. 195, 423-434.
946. Sinha, S., Watorek, W., Karr, S., Giles, J., Bode, W. and Travis, J. (1987). ”Primary structure of human neutrophil elastase.” Proc. Natl. Acad. Sci. USA, 84, 2228-2232.
947. Meyer, E. F. and Bode, W. (1987). The study and design of specific inhibitors to elastase. QSAR in drug and toxocology. D. Hadzi and B. Jerman-Blazic. Amsterdam, Elsevier Science Publ. B.V.: 247-254.
948. Huber, R. and Bennett, W. S. (1987). ”Antibody-antigen flexibility.” Nature 326, 334-335.
949. Deisenhofer, J., Remington, S. J. and Steigemann, W. (1985). Experience with various techniques for the refinement of protein structures. Methods in enzymology, diffraction methods for biological macromolecules, part B. H.W. Wyckoff, C.H.W. Hirs and S.N. Timasheff, Academic Press, Inc. 115: 303-324.
950. Hackenjos, W. A. and Schramm, H. J. (1987). ”Electron microscopical structure analysis of yeast fatty-acid synthase at low resolution.” Biol. Chem. Hoppe-Seyler 368, 19-36.
951. Wlodawer, A., Deisenhofer, J. and Huber, R. (1987). ”Comparison of two highly refined structures of bovine pancreatic trypsin inhibitor.” J. Mol. Biol. 193, 145-156.
952. Fink, E., Rehm, H., Gippner, C., Bode, W., Eulitz, M., Machleidt, W. and Fritz, H. (1986). ”The primary structure of bdellin B-3 from the leech Hirudo medicinalis.” Biol. Chem. Hoppe-Seyler 367, 1235-1242.
953. Allen, J. P., Feher, G., Yeates, T. O., Rees, D. C., Deisenhofer, J., Michel, H. and Huber, R. (1986). ”Structural homology of reaction centers from Rhodopseudomonas sphaeroides and Rhodopseudomonas viridis as determined by X-ray diffraction.” Proc. Natl. Acad. Sci. USA 83, 8589-8593.
954. Huber, R. (1986). ”The structural basis of photosynthetic light reactions in bacteria.” Chemical Scripta 26B, 257-258.
955. Ladenstein, R., Bartunik, H. D., Schneider, M., Huber, R., Schott, K. and Bacher, A. (1986). Structure of the riboflavin synthase/lumazine synthase complex. Arrangement and chain folding of b-Subunits in the icosahedral capsid. Chemistry and Biology of Pteridines. B. A. Cooper and V. M. Whitehead. Berlin, Walter de Gruyter and Co: 103-106.
956. Michel, H., Epp, O. and Deisenhofer, J. (1986). ”Pigment-protein interactions in the photosynthetic reaction center from Rhodopseudomonas viridis.” EMBO J. 5, 2445-2451.
957. Bode, W., Wei, A., Huber, R., Meyer, E., Travis, J. and Neumann, S. (1986). ”X-ray crystal structure of the complex of human leucocyte elastase (PMN elastase) and the third domain of the turkey ovomucoid.” EMBO J. 5, 2453-2458.
958. Huber, R. and Bennett, W. S. J. (1983). Functional significance of flexibility in proteins. XVIIIth Solvay Conference on Chemistry, Nov.-Dec. 1983, Springer-Verlag, Berlin.
959. Huber, R. (1986). ”Structural basis for antigen-antibody recognition.” Science 233, 702-703.
960. Clark Bock, S., Skriver, K., Nielsen, E., Throgersen, H. C., Wiman, B., Donaldson, V. H., Eddy, R. L., Marinan, J., Radziejewska, E., Huber, R., Shows, T. B. and Magnusson, S. (1986). ”Human C1 inhibitor: primary structure, cDNA cloning and chromosomal localization.” Biochemistry 25, 4292-4301.
961. Scott, A. I., Mackenzie, N. E., Malthouse, J. P. G., Primrose, W. U., Fagerness, P. E., Brisson, A., Le Zong Qi, Bode, W., Carter, C. M. and Yi Jin, J. (1986). ”Inhibition of trypsin by carbobenzyloxylysyl chloromethyl ketone: 13C NMR and X-ray diffraction analyses of the enzyme-inhibitor complex.” Tetrahedron 42, 3269-3276.
962. Michel, H., Deisenhofer, J., Miki, K., Epp, O., Lottspeich, F. and Weyer, K. A. (1986). ”High resolution structure of a membrane protein complex: the photosynthetic reaction centre from Rhodopseudomonas viridis.” Biochem. Proc. B89, 57-59.
963. Michel, H. and Deisenhofer, J. (1986). X-ray diffraction studies on a crystalline bacterial photosynthetic reaction center: a progress report and conclusions on the structure of photosystem II reaction centers. Encyclopedia of plant physiology New Series, photosynthesis III. L.A. Stachelin and C. J. Arntzen. Berlin, Springer-Verlag. 19: 371-381.
964. Wiegand, G. and Remington, S. J. (1986). ”Citrate synthase: structure, control and mechanism.” Ann. Rev. Biophys. Chem. 15, 97-117.
965. Pflugrath, J. W., Wiegand, G., Huber, R. and Vertesy, L. (1986). ”Crystal structure determination, refinement and the molecular model of the a-amylase inhibitor Hoe-467A.” J. Mol. Biol. 189, 383-386.
966. Timpl, R., Oberbäumer, I., von der Mark, H., Bode, W., Wick, G., Weber, S. and Engel, J. (1985). Structure and biology of the globular domain of basement membrane type IV collagen. Biology, chemistry and pathology of collagen. P. Fleischmajer, B.R. Olsen and K. Kühn, Annals of the New York Academy of Sciences. 460: 58-72.
967. Schirmer, T., Huber, R., Schneider, M., Bode, W., Miller, M. and Hackert, M. L. (1986). ”Crystal structure analysis and refinement at 2.5 Å of hexameric C-phycocyanin from the cyanobacterium Agmenellum quadruplicatum. The molecular model and its implications for light-harvesting.” J. Mol. Biol. 188, 651-676.
968. Deisenhofer, J., Huber, R. and Michel, H. (1986). ”Die strukturelle Grundlage der Licht-Reaktionen in Bakterien.” Nachr. Chem. Tech. Lab. 34, 417-422.
969. Allen, J. P., Feher, G., Yeats, T. O., Rees, D. C., Eisenberg, D. C., Deisenhofer, J., Michel, H. and Huber, R. (1986). ”Preliminary electron density mapping of the reaction centers from R. Sphaeroides using the molecular replacement method.” Biophys. J. 49, 583a.
970. Knapp, E. W., Fischer, S. F., Zinth, W., Sander, M., Kaiser, W., Deisenhofer, J. and Michel, H. (1985). ”Analysis of optical spectra from single crystals of Rhodopseudomonas viridis reaction centers.” Proc. Natl. Acad. Sci. USA, 82, 8463-8467.
971. Bode, W., Papamokos, E., Musil, D., Seemueller, U. and Fritz, H. (1986). ”Refined 1.2 Å crystal structure of the complex formed between subtilisin Carlsberg and the inhibitor eglin c. Molecular structure of eglin and its detailed interaction with subtilisin.” EMBO J. 5, 813-818.
972. Bode, W. and Huber, R. (1986). Crystal structures of pancreatic serine endopeptidases. Molecular and cellular basis of digestion. P. Desnuelle, H.Sjöström and O. Norèn. Amsterdam, Elsevier Science Publishers B.V. (Biomedical Division): 213-234.
973. Huber, R. (1984). Structural and functional significance of domain association in proteins. UNESCO Workshop on structure and function of proteins, Budapest, September 13-15, Budapest.
974. Scheibe, E., Huber, R. and Epp, O. ”Über Gm-Epitope von menschlichem IgG1*.”
975. Gollwitzer, R. and Bode, W. (1986). ”X-ray crystallographic and biochemical characterization of single crystals formed by proteolytically modified human fibrinogen.” Eur. J. Biochem. 154, 437-443.
976. Deisenhofer, J., Epp, O., Miki, K., Huber, R. and Michel, H. (1985). ”Structure of the protein subunits in the photosynthetic reaction centre of Rhodopseudomonas viridis at 3 Å resolution.” Nature 318, 618-624.
977. Ladenstein, R., Meyer, B., Huber, R., Labischinski, H., Bartels, K., Bartunik, H. D., Bachmann, L., Ludwig, H. C. and Bacher, A. (1986). ”Heavy riboflavin synthase from Bacillus subtilis. particle dimensions, crystal packing and molecular symmetry.” J. Mol. Biol. 187, 87-100.
978. Rümbeli, R., Schirmer, T., Bode, W., Sidler, W. and Zuber, H. (1985). ”Crystallization of phycoerythrocyanin from the cyanobacterium Mastigocladus laminosus and preliminary characterization of two crystal forms.” J. Mol. Biol. 186, 197-199.
979. Huber, R. (1985). Experience with the application of Patterson search techniques. Daresbury Study Weekend, 15-16 February 1985, Science and Eng. Research Council, Daresbury Laboratory.
980. Zinth, W., Knapp, E. W., Fischer, S. F., Kaiser, W., Deisenhofer, J. and Michel, H. (1985). ”Correlation of structural and spectroscopic properties of a photosynthetic reaction center.” Chem. Phys. Lett. 119, 1-4.
981. Wang, D., Bode, W. and Huber, R. (1985). ”Bovine chymotrypsinogen A X-ray crystal structure analysis and refinement of a new crystal form at 1.8 Å resolution.” J. Mol. Biol. 185, 595-624.
982. Schirmer, T., Bode, W., Huber, R., Sidler, W. and Zuber, H. (1985). ”X-ray crystallographic structure of the light-harvesting biliprotein C-phycocyanin from thermophilic cyanobacterium Mastigocladus laminosus and its resemblance to globin structures.” J. Mol. Biol. 184, 257-277.
983. Huber, R. and Schneider, M. (1985). ”A group refinement procedure in protein crystallography using fourier transforms.” J. Appl. Cryst. 18, 165-169.
984. Deisenhofer, J., Michel, H. and Huber, R. (1985). ”The structural basis of photosynthetic light reactions in bacteria.” Trends Biochem. Sci. 10, 243-248.
985. Schramm, H. J. and Jennissen, H. P. (1985). ”Two dimensional electron microscopic analysis of the chalice form of phosphorylase kinase.” J. Mol. Biol. 181, 503-516.
986. Southan, C., Lane, D. A., Bode, W. and Henschen, A. (1985). ”Thrombin-induced fibrinopeptide release from a fibrinogen variant (fibrinogen Sydney I) with an Aa Arg-16 His substitution.” Eur. J. Biochem. 147, 593-600.
987. Bode, W. and Schirmer, T. (1985). ”Determination of the protein content of crystals formed by Mastigocladus laminosus C-phycocyanin, Chroomonas spec.,phycocyanin-645 and modified human fibrinogen using an improved ficoll density gradient method.” Biol. Chem. Hoppe-Seyler 366, 287-295.
988. Bode, W., Brzin, J. and Turk, V. (1985). ”Crystallizationof chicken egg white cystatin, a low molecular weight protein inhibitor of cysteine proteinases, and preliminary X-ray diffraction data.” J. Mol. Biol. 181, 331-332.
989. Schirmer, T., Bode, W., Huber, R., Sidler, W. and Zuber, H. (1985). The crystal and molecular structure of C-phycocyanin from Mastigocladus laminosus and its implications for function and evolution. Optical properties and structure of tetrapyrroles. G. Blauer and H. Sund. Berlin, Walter de Gruyter and Co.: 445-449.
990. Bode, W., Epp, O., Huber, R., Laskowski, Jr., M and Ardelt, W. (1985). ”The crystal and molecular structure of the third domain of silver pheasant ovomucoid (OMSVP3).” Eur. J. Biochem. 147, 387-395.
991. Ladenstein, R., Meyer, B., Huber, R., Labischinski, H., Bartels, K., Bartunik, H. D., Bachmann, L., Ludwig, H. C. and Bacher, A. (1984). Electron microscopy and X-ray diffraction studies on heavy riboflavin synthase from Bacillus subtilis. Flavins and flavoproteins. R. C. Bray, P. C. Engel and S. G. Mayhew. Berlin, Walter de Gruyter and Co: 375-378.
992. Ludwig, H. C., Lottspeich, F., Henschen, A., Ladenstein, R. and Bacher, A. (1984). Heavy riboflavin synthase from Bacillus subtilis. Primary structure and reaggregation of the b-subunits. Flavins and flavoproteins. R.C. Bray, P.C. Engel and S.G. Mayhew. Berlin, Walter de Gruyter and Co: 379-382.
993. Morisset, W., Wehrmeyer, W., Schirmer, T. and Bode, W. (1984). ”Crystallization and preliminary X-ray diffraction data of the cryptomonad biliprotein phycocyanin-645 from a Chroomonas spec.” Arch. Microbiol. 140, 202-205.
994. Wlodawer, A., Walter, J., Huber, R. and Sjölin, L. (1984). ”Structure of bovine pancreatic trypsin inhibitor. Results of joint neutron and X-ray refinement of crystal form II.” J. Mol. Biol. 180, 301-320.
995. Deisenhofer, J., Epp, O., Miki, K., Huber, R. and Michel, H. (1984). ”X-ray structure analysis of a membrane protein complex. Electron density map at 3 Å resolution and a model of the chromophores of the photosynthetic reaction center from Rhodopseudomonas viridis.” J. Mol. Biol. 180, 385-398.
996. Ladenstein, R. (1984). ”Molecular enzymology of seleno-glutathione peroxidase.” Peptide and Protein Reviews 4, 173-214.
997. Huber, R. (1984). ”Three-dimensional structure of antibodies.” Behring Institute Mitteilungen 76, 1-14.
998. Bode, W., Walter, J., Huber, R., Wenzel, H. R. and Tschesche, H. (1984). ”The refined 2.2 Å (0.22-nm) X-ray crystal structure of the ternary complex formed by bovine trypsinogen, valine-valine and the Arg15 analogue of bovine pancreatic trypsin inhibitor.” Eur. J. Biochem. 144, 185-190.
999. Ladenstein, R. and Epp, O. (1984). Hydroperoxide reduction by seleno glutathione peroxidase:a structural approach. Oxidative damage and related enzymes. G. Rotilio and J.V. Bannister. London-New York, Harwood Acad. Publ.: 363-368.
1000. Löbermann, H., Tokuoka, R., Deisenhofer, J. and Huber, R. (1984). ”Human a1-proteinase inhibitor. Crystal structure analysis of two crystal modifications, molecular model and preliminary analysis of the implications for function.” J. Mol. Biol. 177, 531-556.
1001. Deisenhofer, J. and Huber, R. (1983). The contribution of X-ray crystallography to our understanding of immunoglobulin function. Progress in Immunology V. Y. Yamamura and T. Tada, Academic Press Japan, Inc: 47-59.
1002. Bennett, W. S. and Huber, R. (1984). ”Structural and functional aspects of domain motions in proteins.” CRC Crit. Rev. Biochem. 15, 291-384.
1003. Gollwitzer, R., W., B., Schramm, H. J., Typke, D. and Guckenberger, R. (1982). Paracrystalline structure of native human fibrinogen. Fibrinogen – recent biochemical and medical aspects. A. Henschen, H. Graeff and F. Lottspeich. Berlin, Walter de Gruyter and Co.: 1-10.
1004. Gollwitzer, R., Bode, W. and Karges, H. E. (1983). ”On the aggregation of fibrinogen molecules.” Thrombosis Research 5, 41-53.
1005. Wiegand, G., Remington, S., Deisenhofer, J. and Huber, R. (1984). ”Crystal structure analysis and molecular model of a complex of citrate synthase with oxaloacetate and S-acetonyl-coenzyme A.” J. Mol. Biol., 174, 205-219.
1006. Nishikawa, K. (1983). ”Assessment of secondary-structure prediction of proteins comparison of computerized Chou-Fasman method with others.” Biochimica et Biophysica Acta 748, 285-299.
1007. Butz, T., Lerf, A. and Huber, R. (1983). ”Hyperfine interaction investigations of the internal dynamics of biomolecules.” Hyperfine interactions 15/16, 869-880.
1008. Ladenstein, R., Ludwig, H. C. and Bacher, A. (1983). ”Crystallization and preliminary X-ray diffraction study of heavy riboflavin synthase from Bacillus subtilis.” J. Biol. Chem. 258, 11981-11983.
1009. Michel, H., Deisenhofer, J., Miki, K., Weyer, K. and Lottspeich, F. (1983). Crystallization of membrane proteins and actual state of structure analysis of photosynthetic reaction centre crystals. Structure and function of membrane proteins. E. Quagliariello and F. Palmieri, Elsevier Science Publishers B.V.: 191-197.
1010. Arutjunjan, E. G., Deisenhofer, J., Tepljakov, A. V., Kuranova, I. P., Oblomova, G. B. and Vainstein, B. K. (1983). ”Strukturnye parametry Svajazyvanija ligandov Leggemoglobinom Llupina pri razresenii 2.0 Å.” Doklady Akademii Nauk SSSR, 270, no.3.
1011. Gollwitzer, R., Bode, W., Schramm, H. J., Typke, D. and Guckenberger, R. (1983). Laser diffraction of oriented fibrinogen molecule. Molecular biology of fibrinogen and fibrin. M.W. Mosesson and R.F. Doolottle, Annals of the New York Academy of Sciences. 408: 214-225.
1012. Walter, J. and Bode, W. (1983). ”the X-ray crystal structure analysis of the refined complex formed by bovine trypsin and p-amidinophenylpyruvate at 1.4 Å resolution.” Hoppe Seyler`s Z. Physiol. Chem. 364, 949-959.
1013. Marquart, M., Walter, J., Deisenhofer, J., Bode, W. and Huber, R. (1983). ”The geometry of the reactive site and of the peptide groups in trypsin, trypsinogen and its complexes with inhibitors.” Acta Cryst. B39, 480-490.
1014. Walter, J. and Huber, R. (1983). ”Pancreatic trypsin inhibitor.” J. Mol. Biol. 167, 911-917.
1015. Epp, O., Ladenstein, R. and Wendel, A. (1983). ”The refined structure of the selenoenzyme glutathione peroxidase at 0.2-nm resolution.” Eur. J. Biochem. 133, 51-69.
1016. Bode, W. and Kress, L. F. (1983). ”Crystallization and preliminary X-ray diffraction data of proteinase II from Crotalus adamanteus (Eastern Diamond Rattlesnake).” FEBS Lett. 154, 274-276.
1017. Bode, W. and Chen, Z. (1983). The X-ray structures of porcine pancreatic kallikrein and of its complex with bovine pancreatic trypsin inhibitor. Kinins III, part A. H. Fritz, N. Back, G. Dietze and G.L. Haberland. New York, Plenum Press: 289-308.
1018. Huber, R. (1983). E. Werle’s kallikrein inactivator, a model in biochemistry and biophysics. Kinins III, part A. H. Fritz, N. Back, G. Dietze and G.L. Haberland. New York, Plenum Press: 29-36.
1019. Michel, H. (1983). ”Crystallization of membrane proteins.” Trends Biochem. Sci., 8, 56-59.
1020. Michel, H. (1982). ”Characterization and crystal packing of three-dimensional bacteriorhodopsin crystals.” EMBO J., 1, 1267-1271.
1021. Huber, R. and Bennett, W. S. J. (1983). Functional significance of flexibility in proteins. Mobility and recognition in cell biology. Sund and Veeger. Berlin, Walter de Gruyter and Co.: 21-48.
1022. Huber, R. and Bennett, W. S. J. (1983). ”Functional significance of flexibility in proteins.” Biopolymers, 22, 261-279.
1023. Chen, Z. and Bode, W. (1983). ”Refined 2.5 Å X-ray crystal structure of the complex formed by porcine kallikrein A and the bovine pancreatic trypsin inhibitor, crystallization, Patterson search, structure determination, refinement, structure and comparison with its components and with the bovine trypsin-pancreatic trypsin inhibitor complex.” J. Mol. Biol. 164, 283-311.
1024. Bode, W., Chen, Z., Bartels, K., Kutzbach, C., Schmidt-Kastner, G. and Bartunik, H. (1983). ”Refined 2 Å X-ray crystal structure of porcine pancreatic kallikrein A, a specific trypsin-like serine proteinase. crystallization, structure determination, crystallographic refinement structure and its comparison with bo trypsin J.Mol.Biol. 164, 237-282.
1025. Steigemann, W. and Weber, E. (1982). Structure of deoxy- and oxy-erythrocruorin and related ligand states at 1,4 Å resolution. Hemoglobin and oxygen binding. C. Ho, Elsevier North Holland: 19-24.
1026. Bode, W. (1982). ”Struktur und Funktion von Serinproteinasen.” ILU Forum 5, 21.
1027. Henschen, A., Southan, C., Kehl, M. and Bode, W. (1982). ”On the specificity of thrombin: evidence for the selective cleavage of a histidyl bond.” Hoppe Seyler`s Z. f. Biochemie, 363, 982.
1028. Bolognesi, M., Gatti, G., Menegatti, E., Guarneri, M., Marquart, M., Papamokos, E. and Huber, R. (1982). ”Three-dimensional structure of the complex between pancreatic secretory trypsin inhibitor (Kazal Type) and trypsinogen at 1.8 Å resolution. structure solution, crystallographic refinement and preliminary structural interpretation.” J. Mol. Biol., 162, 839-868.
1029. Huber, R. and Bennett, W. S. J. (1982). ”Functional significance of flexibility inproteins.” Pure and Appl. Chem. 54, 2489-2500.
1030. Huber, R. (1982). ”Spatial structure of the immunoglobulin molecule.” EUROPEAN SURGICAL RESEARCH 14, 447-463.
1031. Löbermann, H., Lottspeich, F., Bode, W. and Huber, R. (1982). [ ”Interaction of human a1-proteinase inhibitor with Chymotrypsinogen A and crystallization of a proteolytically Modified a1-proteinase inhibitor.” Hoppe Seyler`s Z. physiol. Chem. 363, 1377-1388.
1032. Remington, S. J., Wiegand, G. and Huber, R. (1981). Molecular structure of citrate synthase. 11th Workshop Conference Hoechst, Schloß Reisensburg, 11.-15. Oktober, 1981, Schloß Reisensburg.
1033. Butz, T., Lerf, A. and Huber, R. (1982). ”Intramolecular reorientational motion in trypsinogen studied by perturbed angular correlation of 199mHg labels.” Physical Rev. Lett. 48, 890-893.
1034. Papamokos, E., Weber, E., Bode, W., Huber, R., Empie, M. W., Kato, I. and Laskowski, M. J. (1982). ”Crystallographic refinement of Japanese quail ovomucoid, a Kazal-type inhibitor, and model building studies of complexes with serine proteases.” J. Mol. Biol., 158, 515-537.
1035. Remington, S., Wiegand, G. and Huber, R. (1982). ”Crystallographic refinement and atomic models of Two Different forms of citrate synthase at 2.7 and 1.7 Å resolution.” J. Mol. Biol. 158, 111-152.
1036. Marquart, M. and Deisenhofer, J. (1982). ”The three-dimensional structure of antibodies.” Immunmology Today, 3, 160-166.
1037. Huber, R. (1982). ”Structural and functional aspects of flexible domains in proteins (immunoglobulins, trypsinogen, citrate synthase).” Chimia 36, 196-197.
1038. Walter, J., Steigemann, W., Singh, T. P., Bartunik, H., Bode, W. and Huber, R. (1982). ”On the disordered activation domain in trypsinogen: chemical labelling and low temperature crystallography.” Acta Cryst. B38, 1462-1472.
1039. Huber, R. and Benett, W. S. (1983). Enzyme als Biokatalysatoren. Biophysik. H. W., W. Lohmann, H. Markt and H. Ziegler. Berlin, Springer Verlag.
1040. Huber, R. (1981). IDIOTYPES: Antigens on the inside. Workshop at the Basel Institute for immunology – November 19-20. Organizers: Claudia Berek, Howard Etlinger and Michael Julius, Basel, ROCHE Editiones ”ROCHE”, Basel, Switzerland.
1041. Laskowski, M. J., Empie, M. W., Kato, I., Kohr, W. J., Ardelt, W., Bogard, W. C. J., Weber, E., Papamokos, E., Bode, W. and Huber, R. (1981). Correlation of amino acid sequence with inhibitor activity and specificity of protein inhibitors of serine proteinases. 32. Colloquium – Mosbach, Springer-Verlag Berlin.
1042. Ladenstein, R., Epp, O. and Wendel, A. (1981). The structure of the selenoenzyme GSH peroxidase. 32. Colloquium – Mosbach, Springer-Verlag Berlin.
1043. Marquart, M., Deisenhofer, J., Huber, R. and Palm, W. (1981). The structures of the intact immunoglobulin KOL, its Fab fragment, a human Fc fragment and Fc-protein A complex after crystallographic refinement at 3.0, 1.9, 2.9 and 2.8 Å resolution. Structural aspects of recognition and assembly in biological macromolecules. M. Balaban, J.L. Sussman, W. Traub and A. Yonath. Rehovot, Balaban ISS: 253-261.
1044. Bode, W. and Huber, R. (1981). Segmental flexibility and its functional significance in trypsinogen-trypsin. Structural aspects of recognition and assembly in biological macromolecules. M. Balaban, J. L. Sussman, W. Traub and A. Yonath. Rehovot, Balaban ISS: 19.
1045. Huber, R. (1981). ”Segmental flexibility in some protein molecules.” Periodicum Biologorum 83, 9-11.
1046. Eklund, H., Samama, J. P., Wallen, L., Bränden, C. I., Akeson, A. and Jones, T. A. (1981). ”Structure of a triclinic ternary complex of horse liver alcohol dehydrogenase at 2.9 Å resolution.” J. Mol. Biol. 146, 561-587.
1047. Weber, E., Papamokos, E., Bode, W., Huber, R., Kato, I. and Laskowski, M. (1981). ”Crystallization, crystal structure analysis and molecular model of the third domain of Japanese quail ovomucoid, a Kazal type inhibitor.” J. Mol. Biol. 149, 109-123.
1048. Harutyunyan, E. H., Kuranova, I. P., Vainshtein, B. K. and Steigemann, W. (1981). ”X-ray investigation of leghemoglobin. XI. The structure of acetate ferric-leghemoglobin at 2.0 Å resolution.” Kristallographia 25, 81-103.
1049. Deisenhofer, J. (1981). ”Crystallographic refinement and atomic models of a human Fc-fragment and its complex with fragment B of protein A from Staphylococcus aureus at 2.9 and 2.8 Å resolution.” Biochemistry 20, 2361-2370.
1050. Steigemann, W. (1980). ”Refinement experiences using chain constraints in real space and energy restraints in reciprocal space.” Daresbury Laboratory Report
1051. Ladenstein, R., Epp, O., Huber, R. and Wendel, A. (1979). Molecular model of the selenoenzyme glutathione peroxidase. Third international Symposium on Organic selenium and Tellurium compounds, Metz.
1052. Marquart, M., Deisenhofer, J., Huber, R. and Palm, W. (1981). ”The structures of the intact immunoglobulin Kol, its Fab fragment, a human Fc-fragment and Fc-protein A complex after crystallographic refinement at 0.3, 0.19, 0.29 and 0.28 nm resolution. I. Intact Kol and Kol Fab fragment.” Hoppe Seyler`s Z. physiol. Chem. 362, 17-32.
1053. Huber, R. (1980). ”Spatial structure of immunoglobulin molecules.” Klin. Wochenschr. 58, 1217-1231.
1054. Gollwitzer, R. and Bode, W. (1980). ”Correlation between structure and enzymatic digestion in fibrinogen.” Haematologica 65, 528-534.
1055. Gollwitzer, R., Bode, W., Schramm, H. J., Typke, D. and Guckenberger, R. (1980). Paracrystalline structure of native human fibrinogen. Proteins and related subjects. H. Peeters, Pergamon Press. 28: 307-310.
1056. Huber, R., Scholze, H., Pâques, E. P. and Deisenhofer, J. (1980). ”Crystal structure analysis and molecular model of human C3a anaphylatoxin.” Hoppe Seyler`s Z. physiol. Chem. 361, 1389-1399.
1057. Marquart, M., Deisenhofer, J., Huber, R. and Palm, W. (1980). ”Crystallographic refinement and atomic models of the intactimmunoglobulin molecule Kol and its antigen-binding fragment at 3.0 Å and 1.9 Å resolution.” J. Mol. Biol. 141, 369-391.
1058. Lill, U., Pirzer, P., Kukla, D., Huber, R. and Eggerer, H. (1980). ”Nicotinic acid metabolism.” Hoppe-Seyler`s Z. physiol. Chemie 361, 875-884.
1059. Pâques, E. P., Scholze, H. and Huber, R. (1980). ”Purification and crystallization of human anaphylatoxin, C3a.” Hoppe-Seyler`s Z. physiol. Chemie 361, 977-980.
1060. Singh, T. P., Bode, W. and Huber, R. (1980). ”Low-temperature protein crystallography. effect on flexibility, temperature factor, mosaic spread, extinction and diffuse scattering in two examples: bovine trypsinogen and Fc fragment.” Acta Cryst. B36, 621-627.
1061. Paques, E. P. (1989). ”Purification and partial characterization of the third component of the complement system from porcine Serum (C3) and of a crystallizable Degradation product of the fourth component of the complement system from human Serum (C4). Study of the tryptic digestion products of human and porcine C3 and of human C4.” Hoppe-Seyler`s Z. physiol. Chem., 361, 445-456.
1062. Deisenhofer, J. and Huber, R. (1980). Conformational flexibility and its functional significance in some protein molecules. Protein folding. R. Jaenicke, Elsevier/North Holland, Biomedical Press: 565-582.
1063. Huber, R. (1979). Conformational flexibility and its functional significance in some protein molecules. 30. Colloquium Mosbach, Springer-Verlag Berlin.
1064. Ladenstein, R., Epp, O., Bartels, K., Jones, A., Huber, R. and Wendel, A. (1979). ”Structure analysis and molecular model of the selenoenzyme glutathione peroxidase at 2.8 Å-resolution.” J. Mol. Biol. 134, 199-218.
1065. Ladenstein, R., Marchesini, A. and Palmieri, S. (1979). ”Preliminary crystallographic study of ascorbic acid oxidase from green zucchini squash.” FEBS Lett. 107, 407.
1066. Huber, R. (1979). ”Conformational flexibility and its functional significance in some protein molecules.” Trends in Biochemical Sciences 4, 271-276.
1067. Deisenhofer, J. and Huber, R. (1979). ”Conformational flexibility and its functional relevance in some protein molecules.” Hoppe-Seyler’s Z. physiol. Chem. 360, 1001-1016.
1068. Appelt, K., Dijk, J. and Epp, O. (1979). ”The crystallization of protein BL17 from the 50 S ribosomal subunit of Bacillus Stearothermophilus.” FEBS Lett., 103, 66-70.
1069. Huber, R. (1979). Antibody structure. Molecular mechanisms of biological recognition. . M. Balaban, Elsevier/North-Holland Biomedical Press: 255-269.
1070. Huber, R. (1979). ”Conformational flexibility in protein molecules.” Nature 280, 538-539.
1071. Bode, W. (1979). ”Aktivierung, Aktivität und Inhibierung des Rindertrypsins.” Naturwissenschaften 66, 251-258.
1072. Deisenhofer, J., Matsushima, M., Colman, P. M., Marquart, M., Huber, R. and Palm, W. (1978). Three-dimensional structure of an antibody molecule and several fragments. Immunology. Gergely, Medgyesi and Hollàn: 255-256.
1073. Bode, W. (1979). ”The transition of bovine trypsinogen to a trypsin-like state upon strong ligand binding.II. The binding of the pancreatic trypsin inhibitor and of isoleucine-valine and of sequentially related peptides to trypsinogen and to p-guanidinobenzoate-trypsinogen.” J. Mol. Biol. 127, 357-374.
1074. Paques, P. E., Huber, R., Priess, H. and Wright, J. K. (1979). ”Isolation of the globular region of the subcomponent q of the C1 component of complement.” Hoppe-Seyler’s Z. physiol. Chem. 360, 177-183.
1075. ”Structure of erythrocruorin in different ligand states refined at 1.4 Å resolution.” J. Mol. Biol. 127, 309-338.
1076. Wiegand, G., Kukla, D., Scholze, H., Jones, T. A. and Huber, R. (1979). ”Crystal structure analysis of the tetragonal crystal form and preliminary molecular model of pig-heart citrate synthase.” Eur. J. Biochem. 93, 41-50.
1077. Deisenhofer, J., Matsushima, M., Colman, P. M. and Marquart, M. (1978). Three-dimensional structure of an antibody molecule and several fragments. Versatility of Proteins. C. H. Li. New York, Academic Press: 293-294.
1078. Bode, W. (1978). Activation, action and inhibition of trypsinogen-trypsin. Round-Table Conference, Leuven, Belgium, Biomedical Press Elsevier/North – Holland.
1079. Jones, T. A. (1978). ”A graphics model building and refinement system for macromolecules.” J. Appl. Cryst. 11, 268-272.
1080. Deisenhofer, J., Jones, T. A., Huber, R., Sjödahl, J. and Sjöquist, J. (1978). ”Crystallization, and crystal structure analysis and atomic model of the complex formed by a human Fc fragment and fragment B of protein A from Staphylococcus aureus.” Hoppe-Seyler’s Z. physiol. Chem. 359, 975-985.
1081. Matsushima, M., Marquart, M., Jones, T. A., Colman, P., Bartels, K., Huber, R. and Palm, W. (1978). ”Crystal structure of the human Fab fragment Kol and its comparison with the intact Kol molecule.” J. Mol. Biol. 121, 441-459.
1082. Bode, W. and Huber, R. (1978). ”Crystal structure analysis and refinement of two variants of trigonal trypsinogen, trigonal trypsin and PEG (polyethylene glycol) trypsinogen and their comparison with orthorhombic trypsin and trigonal trypsinogen.” FEBS Lett. 90, 265-269.
1083. Huber, R. and Bode, W. (1978). ”Structural basis of the activation and action of trypsin.” Acc. Chemi. Res. 11, 114-122.
1084. Weber, E., Steigemann, W., Jones, T. A. and Huber, R. (1978). ”The structure of oxy-erythrocruorin at 1.4 Å resolution.” J. Mol. Biol. 120, 327-336.
1085. Huber, R. and Bode, W. (1977). Activation, action and inhibition of trypsin as deduced from the threedimensional structures of trypsinogen, trypsin and their complexes with the basic pancreatic trypsin inhibitor. 11th FEBS Meeting Copenhagen1977, Copenhagen, Pergamon Press, Oxford.
1086. Bode, W., Schwager, P. and Huber, R. (1978). ”The transition of bovine trypsinogen to a trypsin-like state upon strong ligand binding. The refined crystal structures of the bovine trypsinogen-pancreatic trypsin inhibitor complex and of its ternary complex with Ile-Val at 1.9 Å resolution.” J. Mol. Biol. 118, 99-112.
1087. Deisenhofer, J. (1977). ”Dreidimensionale Struktur der Antikörper.” Die Gelben Hefte XVII, 106-115.
1088. Huber, R. and Bode, W. (1977). Structural basis of the activation and action of trypsin. NMR in Biology. R. A. Dwek, I. D. Campbell, R. E. Richards and J. R. P. Williams. New York, Academic Press: 1-31.
1089. Fehlhammer, H., Bode, W. and Huber, R. (1977). ”Crystal structure of bovine trypsinogen at 1.8 Å resolution. II. Crystallographic refinement, refined crystal structure and comparison with bovine trypsin.” J. Mol. Biol. 111, 415-438.
1090. Bartels, K. (1977). Absorption corrections. The Rotation Method in Crystallography. U. W. Arndt and A. J. Wonacott. Amsterdam, North Holland Publ. Co.: 153-275.
1091. Jones, A., Bartels, K. and Schwager, P. (1977). Refinement of crystal orientation parameters. The Rotation Method in Crystallography. U. W. Arndt and A. J. Wonacott. Amsterdam, North Holland Publ. Co.: 105-275.
1092. Huber, R. (1977). Enzyme als Biokatalysatoren.
1093. Biophysik. W. Hoppe, W. Lohmann, H. Markl and H. Ziegler. Berlin, Springer-Verlag. Huber, R., Deisenhofer, J., Colman, P. M., Matsushima, M. and Palm, W. (1976). ”Crystallographic structure studies of an IgG molecule and an Fc fragment.” Nature 264, 415-420.
1094. Huber, R., Deisenhofer, J., Colman, P. M., Matsushima, M. and Palm, W. (1976). X-ray diffraction analysis of immunoglobulin structure. 27. Colloquium Mosbach: The Immune System, Springer-Verlag Berlin. Bode, W. and Huber, R. (1976). ”Induction of the bovine trypsinogen-trypsin transition by peptides sequentially similar to the N-terminus of trypsin.” FEBS Lett. 68, 231-236.
1095. Deisenhofer, J., Colman, P. M., Epp, O. and Huber, R. (1976). ”Crystallographic structural studies of a human Fc fragment. II. A complete model based on a Fourier map at 3.5 Å resolution.” Hoppe-Seyler’s Z. physiol. Chem. 357, 1421-1434.
1096. Bode, W., Fehlhammer, H. and Huber, R. (1976). ”Crystal structure of bovine trypsinogen at 1.8 Å resolution. I. Data collection, application of Patterson search techniques and preliminary structural interpretation.” J. Mol. Biol. 106, 325-335.
1097. Colman, P. M., Fehlhammer, H. and Huber, R. (1975). Patterson search methods in protein structure determination: b-trypsin and immunoglobulin fragments. Crystallographic computing techniques. F. R. Ahmed, K. Huml and B. Sedlácek. Copenhagen, Munksgaard Verlag: 248-258.
1098. Steigemann, W., Deisenhofer, J. and Huber, R. (1975). Constrained crystallographic refinement of three protein structures. Crystallographic computing techniques. F. R. Ahmed, K. Huml and B. Sedlácek. Copenhagen, Munksgaard Verlag: 302-306.
1099. Hetzel, R., Wüthrich, K., Deisenhofer, J. and Huber, R. (1976). ”Dynamics of the aromatic amino acid residues in the globular conformation of the basic pancreatic trypsin inhibitor (BPTI). II. Semi-empirical energy calculations.” Biophys. Struct. Mech. 2, 159-180.
1100. Bode, W., Schwager, P. and Huber, R. (1976). Structural studies on the pancreatic trypsin inhibitor-trypsin complex and its free components: structure and function relationship in serine protease inhibition and catalysis. Proteolysis and physiological regulation. Miami Winter Symposia. New York, Academic Press. 11: 43-76.
1101. Ladenstein, R. and Wendel, A. (1976). ”Crystallographic data of the selenoenzyme glutathione peroxidase.” J. Mol. Biol. 104, 877-882.
1102. Huber, R. (1976). ”Antibody structure.” Trends Biochem. Sci. 1, 174-178.
1103. Wiegand, G. and Kaleja, R. (1976). ”Fluorescent guanosine-nucleotide analogs suitable for photoaffinity-labeling experiments.” Eur. J. Biochem. 65, 473-479.
1104. Bartels, K. and Colman, P. M. (1976). ”Subunit symmetry of tetrameric phosphorylase.” Biophys. Struct. Mech. 2, 43-59.
1105. Wiegand, G. (1976). ”Crystallization and preliminary X-ray data of well-ordered crystals from pig heart citrate synthase.” FEBS Lett. 62, 281-283.
1106. Deisenhofer, J., Colman, P. M., Huber, R., Haupt, H. and Schwick, G. (1976). ”Crystallographic structural studies of a human Fc-fragment. I. An electron density map at 4 Å resolution and a partial model.” Hoppe-Seyler’s Z. Physiol. Chem. 357, 435-445.
1107. Colman, P. M., Deisenhofer, J., Huber, R. and Palm, W. (1976). ”Structure of the human antibody molecule Kol (immunoglobulin GI). An electron density map at 5 Å resolution.” J. Mol. Biol. 100, 257-282.
1108. Epp, O., Lattman, E. E., Schiffer, M., Huber, R. and Palm, W. (1975). ”The molecular structure of a dimer composed of the variable portions of the Bence-Jones protein REI refined at 2.0 Å resolution.” Biochemistry 14, 4943-4952.
1109. Bode, W., Schwager, P. and Huber, R. (1975). Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor. IV. Strong, specific protein interaction and catalysis. Tenth FEBS Meeting.
1110. Bode, W. and Schwager, P. (1975). ”The refined crystal structure of bovine b-trypsin at 1.8 Å resolution. II. Crystallographic refinement, calcium binding site, benzamidine binding site and active site at pH 7.0.” J. Mol. Biol. 98, 693-717.
1111. Fehlhammer, H. and Bode, W. (1975). ”The refined crystal structure of bovine b-trypsin at 1.8 Å resolution. I. Crystallization, data collection and application of Patterson search techniques.” J. Mol. Biol. 98, 683-692.
1112. Schalch, W. and Bode, W. (1975). ”Involvement of tyrosine residues in the protemer-protemer interaction of Proteus Mirabilis flagella as studied by spectroscopic methods, chemical modification and aggregation experiments.” Biochimica et Biophysica Acta 405, 292-305.
1113. Bode, W. and Schwager, P. (1975). ”The single calcium-binding site of crystalline bovine b-trypsin.” FEBS Lett. 56, 139-143.
1114. Huber, R., Bode, W., Kukla, D., Kohl, U. and Ryan, C. A. (1975). ”The structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor. III. Structure of the anhydro-trypsin-inhibitor complex.” Biophys. Struct. Mech. 1, 189-201.
1115. Schwager, P., Bartles, K. and Jones, A. (1975). ”Refinement of setting angles in screenless film methods.” J. Appl. Cryst. 8, 275-280.
1116. Colman, P. M. (1974). ”Noncrystallographic symmetry and the sampling theorem.” Zeitschrift für Kristallographie 140, 344-349.
1117. Fehlhammer, H., Schiffer, M., Epp, O., Colman, P. M., Lattman, E. E., Schwager, P., Steigemann, W. and Schramm, H. J. (1975). ”The structure determination of the variable portion of the Bence-Jones protein AU.” Biophys. Struct. Mech. 1, 139-146.
1118. Deisenhofer, J. and Steigemann, W. (1975). ”Crystallographic Refinement of the structure of bovine pancreatic trypsin inhibitor at 1.5 Å resolution.” Acta Cryst. B31, 238-250.
1119. Huber, R. and Steigemann, W. (1974). ”Two cis-prolines in the Bence-Jones protein REI and the cis-Pro-bend.” FEBS Lett. 48, 235-237.
1120. Huber, R., Kukla, D., Bode, W., Schwager, P., Bartels, K., Deisenhofer, J. and Steigemann, W. (1974). ”Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor. II. Crystallographic refinement at 1.9 Å resolution.” J. Mol. Biol. 89, 73-101.
1121. Huber, R., Kukla, D., Steigemann, W., Deisenhofer, J. and Jones, T. A. (1974). Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor. Refinement of the crystal structure analysis. 2nd International Research Conference on Proteinase Inhibitors (Bayer Symposium V), Springer-Verlag, Berlin. Deisenhofer, J. and Steigemann, W. (1974). The model of the basic pancreatic trypsin inhibitor refined at 1.5 Å resolution. 2nd International Research Conference on Proteinase Inhibitors (Bayer Symposium V), Springer-Verlag, Berlin.
1122. Colman, P. M., Epp, O., Fehlhammer, H., Bode, W., Palm, W., Schiffer, M., Lattmann, E. E. and Jones, T. A. (1974). ”X-ray studies on antibody fragments.” FEBS Lett. 44, 194-199.
1123. Steigemann, W. (1973). The Faltmolekül method and other Patterson search techniques in structure analysis. Modern Methods of Steroid Analysis. E. Heftmann. New York, Academic Press Inc.
1124. Epp, O., Colman, P., Fehlhammer, H., Bode, W., Palm, W., Schiffer, M. and Huber, R. (1974). ”Crystal and molecular structure of a dimer composed of the variable portions of the Bence-Jones protein REI.” Eur. J. Biochem. 45, 513-524.
1125. Palm, W. and Colman, P. M. (1974). ”Preliminary X-ray data from well-ordered crystals of a human immunoglobulin G molecule.” J. Mol. Biol. 82, 587-588.
1126. Huber, R. (1973). ”Entwicklungslinien der Strukturanalyse von Proteinmolekülen.” Mitteilungen aus der Max-Planck-Gesellschaft 3, 172-189.
1127. Rühlmann, A., Kukla, D., Schwager, P., Bartels, K. and Huber, R. (1973). ”Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor, crystal structure determination and stereochemistry of the contact region.” J. Mol. Biol. 77, 417-436. Huber, R. (1973).
1128. The structure of the pancreatic trypsin inhibitor (kallikrein inactivator). The Jerusalem Symposia on Quantum Chemistry and Biochemistry V, Jerusalem. Schwager, P., Bartels, K. and Huber, R. (1973).
1129. ”A simple empirical absorption-correction method for X-ray intensity data films.” Acta Cryst. A29, 291-295. Huber, R. (1972).
1130. Interaction between chymotrypsin (trypsin) and the pancreatic trypsin inhibitor (kallikrein inactivator). 23. Colloquium der Ges. für Biologische Chemie, Mosbach/Baden, Springer-Verlag Berlin. Amiconi, G., Antonini, E., Brunori, M., Formanek, H. and Huber, R. (1972). ”Functional properties of native and reconstituted haemoglobins from Chironomus thummi thummi.” Eur. J. Biochem. 31, 52-58.
1131. Kopfmann, G. (1972). ”A statistical evaluation of absorption by C. Katayama, N. Sakabe, and K. Sakabe.” Acta Cryst. A28, 661.
1132. Blow, D. M., Wright, C. S., Kukla, D., Rühlmann, A., Steigemann, W. and Huber, R. (1972). ”A model for the association of bovine pancreatic trypsin inhibitor with chymotrypsin and trypsin.” J. Mol. Biol. 69, 137-144.
1133. Epp, O., Palm, W., Fehlhammer, H., Rühlmann, A., Steigemann, W., Schwager, P. and Huber, R. (1972). ”Crystallographic evidence for structurally similar domains in the human k-type Bence-Jones protein REI.” J. Mol. Biol. 69, 315-318.
1134. Huber, R. (1972). Structure of the haemoglobin molecule. Synthese, Struktur und Funktion des Hämoglobins (Molecular Biology and Clinical Aspects). H. Martin and L. Nowicki. München, J.F. Lehmanns Verlag: 175.
1135. Fasold, H., Ortanderl, F., Huber, R., Bartels, K. and Schwager, P. (1972). ”Crystallization and crystallographic data of rabbit muscle phosphorylase a and b.” FEBS Lett. 21, 229-232.
1136. Wüthrich, K., Keller, R. M., Brunori, M., Giacometti, G., Huber, R. and Formanek, H. (1972). ”Similarities of the heme environment in vertebrate oxygene-binding hemoproteins.” FEBS Lett. 21, 63-66.
1137. Rühlmann, A., Schramm, H. J., Kukla, D. and Huber, R. (1971). ”Pancratic trypsin inhibitor (Kunitz). Part II: complexes with proteinases.” Cold Spring Harbor Symposia on Quantitative Biology, XXXVI, 148-150.
1138. Huber, R., Kukla, D., Rühlmann, A. and Steigemann, W. (1971). ”Pancratic trypsin inhibitor (Kunitz). Part I: Structure and function.” Cold Spring Harbor Symposia on Quantitative Biology, XXXVI, 141-148.
1139. Huber, R. (1971). ”Struktur eines Proteinase-Inhibitors.” Umschau in Wissenschaft und Technik 71, 534-535.
1140. Huber, R., Kukla, D., Rühlmann, A. and Steigemann, W. (1970). The atomic structure of the basic trypsin inhibitor of bovine organs (kallikrein inactivator). International Research Conference on Proteinase Inhibitors, Munich, Walter de Gruyter, Berlin.
1141. Epp, O., Steigemann, W., Formanek, H. and Huber, R. (1971). ”Crystallographic evidence for the tetrameric subunit structure of L-asparaginase from Escherichia coli.” Eur. J. Biochem. 20, 432-437.
1142. Huber, R., Epp, O. and Formanek, H. (1971). ”pH-induced structural change in erythrocruorin.” J. Mol. Biol. 57, 377-379.
1143. Huber, R., Epp, O., Formanek, H. and Steigemann, W. (1971). ”The atomic structure of erythrocruorin in the light of the chemical sequence and its comparison with myoglobin.” Eur. J. Biochem. 19, 42-50.
1144. Huber, R., Epp, O. and Formanek, H. (1970). ”The structures of deoxy- and carbonmonoxy-erythrocruorin.” J.Mol. Biol., 52, 349-354.
1145. Huber, R., Kukla, D., Rühlmann, A., Epp, O. and Formanek, H. (1970). ”The basic trypsin inhibitor of bovine pancreas. I. Structure analysis and conformation of the polypeptide chain.” Naturwiss. 57, 389. Programmed ”Faltmolekül” method. International Summer School on Crystallographic computing, Munksgaard Copenhagen.
1146. Huber, R., Epp, O. and Formanek, H. (1969). ”The 2.8 Å resolution Fourier synthesis of the insect hemoglobin erythrocruorin.” Acta Cryst. A25, 15-28.
1147. Huber, R., Epp, O. and Formanek, H. (1969). ”Aufklärung der Molekülstruktur des Insektenhämoglobins.” Naturwiss. 56, 362.
1148. Huber, R., Epp, O. and Formanek, H. (1969). ”The environment of the haem group in erythrocruorin (Chironomus thummi).” J. Mol. Biol. 42, 591.
1149. Amit, A., Huber, R. and Hoppe, W. (1968). ”Die Röntgenstrukturanalyse des Bullvalens.” Acta Cryst. B24, 865.
1150. Huber, R. and Kopfmann, G. (1969). ”Experimental absorption correction: results.” Acta Cryst. A25, 143-152.
1151. Huber, R. (1968). Proteinkristallstrukturanalyse. 10. Diskussionstagung der Sektion für Kristallkunde in der Deutschen Mineralogischen Gesellschaft, Bern.
1152. Qasba, R., Brandl, F., Hoppe, W. and Huber, R. (1969). ”Kristallstrukturanalyse der monoklinen Modifikationen des 3,5,8,10-Tetramethylcycloheptazulens.” Acta Cryst. B25, 1198-1200.
1153. Huber, R. and Formanek, H. (1966). ”Heavy-atom derivatives of erythrocruorin of Chironomus thummi.” Acta Cryst. 21, 10-18.
1154. Huber, R., Formanek, H. and Epp.O (1968). ”Die Kristallstrukturanalyse des Met-Erythrocruorins (Chironomus thummi) bei 5.5 Å Auflösung.” Naturwiss. 55, 75.
1155. Huber, R., Formanek, H. and Epp.O (1967). Die 5 Å Kristallstrukturanalyse von Erythrocruorin (Chironomus thummi). 9. Diskussionstagung der Sektion für Kristallkunde in der Deutschen Mineralogischen Gesellschaft, Bonn, Jülich.
1156. Amit, A., Brandl, F., Hoppe, W., Gieren, A., Hädicke, E., Brodherr, N., Röhrl, M. and Huber, R. (1967). Schweratom- und Faltmolekülstrukturanalysen von organischen Verbindungen. 9. Diskussionstagung der Sektion für Kristallkunde in der Deutschen Mineralogischen Gesellschaft, Bonn, Jülich.
1157. Huber, R. and Kopfmann, G. (1967). Eine Methode zur Absorptionskorrektur durch Intensitätsmessungen. 9. Diskussionstagung der Sektion für Kristallkunde in der Deutschen Mineralogischen Gesellschaft, Bonn, Jülich.
1158. Paulus, E., Hoppe, W. and Huber, R. (1965). Röntgenstrukturanalyse von homologen Kobalt- und Rhodium-Cyclooctatetraen-Komplexen. 8. Diskussionstagung der Sektion für Kristallkunde in der Deutschen Mineralogischen Gesellschaft, Marburg.
1159. Huber, R., Formanek, H. and Epp, O. (1965). Isomorphe Substitutionen am Erythrocruorin von Chironomus thummi. 8. Diskussionstagung der Sektion für Kristallkunde in der Deutschen Mineralogischen Gesellschaft, Marburg.
1160. Hoppe, W. and Huber, R. (1965). Die Anwendung der Faltmolekülmethode bei der Strukturanalyse von Ecdyson. 8. Diskussionstagung der Sektion für Kristallkunde in der Deutschen Mineralogischen Gesellschaft, Marburg.
1161. Kopfmann, G. and Huber, R. (1968). ”A method of absorption correction by X-ray-intensity measurements.” Acta Cryst. A24, 348.
1162. Paulus, E., Hoppe, W. and Huber, R. (1967). ”Struktur von Cyclooctatetraen-di-metall-cyclopentadienyl-Komplexen.” Naturwiss. 54, 67.
1163. Huber, R. and Hoppe, W. (1965). ”Zur Chemie des Ecdysons VII. Die Kristall- und Molekülstrukturanalyse des Insektenverpuppungshormons Ecdyson mit der automatisierten Faltmolekülmethode.” Chem. Ber. 98, 2403-2424.
1164. Hoppe, W. and Huber, R. (1965). ”Zur Chemie des Ecdysons II. Bestimmung des Sterinskeletts und seiner Orientierung mit diffuser Röntgenstreuung in Kristallen von Ecdyson.” Chem. Ber. 98, 2353-2360.
1165. Huber, R. (1966). ”Die automatisierte Faltmolekülmethode.” Fortschritte Miner. 42, 226.
1166. Huber, R. (1965). ”Die automatisierte Faltmolekülmethode.” Acta Cryst. 19, 353-356.
1167. Huber, R., Langer, R. and Hoppe, W. (1965). ”Kristall- und Molekülstruktur des syn-Methyldiazotat-Kaliums CH3N2OK.” Acta Cryst. 18, 467.
1168. Huber, R., Formanek, H., Braun, V., Braunitzer, G. and Hoppe, W. (1964). ”Chemische und röntgenographische Untersuchungen am Erythrocruorin.” Ber. Bunsenges. Phys. Chem. 68, 818.
1169. Karlson, P., Hoffmeister, H., Hoppe, W. and Huber, R. (1963). ”Zur Chemie des Ecdysons.” Liebigs Ann. Chem. 662, 1.
1170. Hoppe, W., Anzenhofer, R. and Huber, R. (1963). Experience with two new methods for structure determination. Crystallography and crystal perfection. Symposium held in Madras, Academic Press, London.
1171. Müller, E., Hoppe, W., Hagenmeier, H., Haiss, H., Huber, R., Rundel, W. and Suhr, H. (1963). ”Struktur isomerer Diazotate: das Hantzschsche Methyldiazotat.” Chem. Ber. 96, 1712-1719.
1172. Huber, R. (1964). ”Bericht über den 6. Internationalen Kongreß der Internationalen Union für Kristallographie, Rom.” Angew. Chem. 76, 189.
1173. Huber, R. and Hoppe, W. (1963). ”Die Röntgenstrukturanalyse des syn-Kaliummethyldiazotates.” Acta Cryst. A16, 63.
1174. Hoppe, W., Huber, R. and Gaßmann, J. (1963). ”Die ”Phasenverfeinerung” – ein neues Konzept in der Kristallstrukturanalyse.” Acta Cryst. A16, 4.
1175. Anzenhofer, K. and Huber, R. (1963). ”Ein Programm zur automatischen Auswertung von den Intensitäten bis zur Zeichnung von Fourier-Synthesen.” Acta Cryst. A16, 173.
1176. Huber, R. and Hoppe, W. (1962). ”Lineare Gleichungen zwischen Strukturfaktorprodukten zur Bestimmung von zusätzlichen Vorzeichen in der Schweratomtechnik.” Phys. Verh. Mosbach 13, 117.
1177. Huber, R. (1962). ”Die Röntgenstrukturanalyse des syn-Kaliumethyldiazotates.” Dissertation, Technische Hochschule München.
1178. Huber, R. (1960). ”Chemische und röntgenographische Untersuchungen zur Formel und Molekülform des Ecdysons.” Diplomarbeit, Technische Hochschule München.
Photos of Robert Huber
