Irvin Rose

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2004 Nobel Prize in chemistry

1971 Guggenheim fellowship award

1.    Chen Zhijian J; Rose Irwin A. Cecile M. Pickart (1954-2006). Molecular cell 2006;22(5):571-3.
2.    Rose I A. Mechanistic inferences from stereochemistry. The Journal of biological chemistry 2006;281(10):6117-9.
3.    Rose Irwin. Ubiquitin at Fox Chase (Nobel lecture). Angewandte Chemie (International ed. in English) 2005;44(37):5926-31.
4.    Rose I. Ubiquitin at Fox Chase. Cell death and differentiation 2005;12(9):1198-201.
5.    Rose Irwin. Early work on the ubiquitin proteasome system, an interview with Irwin Rose. Interview by CDD.Cell death and differentiation 2005;12(9):1162-6.
6.    Rose Irwin A. Ubiquitin at Fox Chase. Proceedings of the National Academy of Sciences of the United States of America 2005;102(33):11575-7.
7.    Rose Irwin A; Weaver Todd M. The role of the allosteric B site in the fumarase reaction.
Proceedings of the National Academy of Sciences of the United States of America 2004;101(10):3393-7.
8.    Rose Irwin A; Nowick James S. Methylglyoxal synthetase, enol-pyruvaldehyde, glutathione and the glyoxalase system. Journal of the American Chemical Society 2002;124(44):13047-52.
9.    Rose I A. How fumarase recycles after the malate –> fumarate reaction. Insights into the reaction mechanism. Biochemistry 1998;37(51):17651-8.
10.    Rose I A. Restructuring the active site of fumarase for the fumarate to malate reaction.
Biochemistry 1997;36(40):12346-54.
11.    Rose I A. Isotopic strategies for the study of enzymes. Protein science : a publication of the Protein Society 1995;4(7):1430-3.
12.    Rose I A. Partition analysis: detecting enzyme reaction cycle intermediates.
Methods in enzymology 1995;249():315-40.
13.    Rose I A; Warms J V; Yuan R G. Role of conformational change in the fumarase reaction cycle. Biochemistry 1993;32(33):8504-11.
14.    Rose I A; Warms J V; Kuo D J. Proton transfer in catalysis by fumarase.
Biochemistry 1992;31(41):9993-9.
15.    Rose I A; Kuo D J. Role of CO2 in proton activation by histidine decarboxylase (pyruvoyl). Biochemistry 1992;31(25):5887-92.
16.    Hadari T; Warms J V; Rose I A; Hershko A. A ubiquitin C-terminal isopeptidase that acts on polyubiquitin chains. Role in protein degradation. The Journal of biological chemistry 1992;267(2):719-27.
17.    Seeholzer S H; Jaworowski A; Rose I A. Enolpyruvate: chemical determination as a pyruvate kinase intermediate. Biochemistry 1991;30(3):727-32.
18.    Rose I A; Kuo D J; Warms J V. A rate-determining proton relay in the pyruvate kinase reaction. Biochemistry 1991;30(3):722-6.
19.    Rose I A; Fung W J; Warms J V. Proton diffusion in the active site of triosephosphate isomerase. Biochemistry 1990;29(18):4312-7.
20.    Rose I A; Kuo D J. The substrate proton of the pyruvate kinase reaction.
Biochemistry 1989;28(25):9579-85.
21.    Yip V; Pusateri M E; Carter J; Rose I A; Lowry O H. Distribution of the glucose-1,6-bisphosphate system in brain and retina. Journal of neurochemistry 1988;50(2):594-602.
22.    Kuo D J; Rose I A. Aconitase: its source of catalytic protons. Biochemistry 1987;26(24):7589-96.
23.    Hershko A; Rose I A. Ubiquitin-aldehyde: a general inhibitor of ubiquitin-recycling processes. Proceedings of the National Academy of Sciences of the United States of America 1987;84(7):1829-33.
24.     Rose I A; Warms J V. A specific endpoint assay for ubiquitin. Proceedings of the National Academy of Sciences of the United States of America 1987;84(6):1477-81.
25.    Rose I A; Warms J V; Kuo D J. Concentration and partitioning of intermediates in the fructose bisphosphate aldolase reaction. Comparison of the muscle and liver enzymes.
The Journal of biological chemistry 1987;262(2):692-701.
26.    Pickart C M; Rose I A. Mechanism of ubiquitin carboxyl-terminal hydrolase. Borohydride and hydroxylamine inactivate in the presence of ubiquitin. The Journal of biological chemistry 1986;261(22):10210-7.
27.    Rose I A; Warms J V. Complexes of muscle aldolase in equilibrium with fructose 1,6-bisphosphate. Biochemistry 1985;24(15):3952-7.
28.     Kuo D J; Rose I A. Chemical trapping of complexes of dihydroxyacetone phosphate with muscle fructose-1,6-bisphosphate aldolase. Biochemistry 1985;24(15):3947-52.
29.    Pickart C M; Rose I A. Ubiquitin carboxyl-terminal hydrolase acts on ubiquitin carboxyl-terminal amides. The Journal of biological chemistry 1985;260(13):7903-10.
30.    Pickart C M; Rose I A. Functional heterogeneity of ubiquitin carrier proteins.
The Journal of biological chemistry 1985;260(3):1573-81.  Jaworowski A; Rose I A.
Partition kinetics of ribulose-1,5-bisphosphate carboxylase from Rhodospirillum rubrum.
The Journal of biological chemistry 1985;260(2):944-8.
31.    Pickart C M; Rose I A. Functional heterogeneity of ubiquitin carrier proteins.
Progress in clinical and biological research 1985;180():215.
32.    Rose I A. Failure to confirm previous observations on triosephosphate isomerase intermediate and bound substrate complexes. Biochemistry 1984;23(24):5893-4.
33.     Hershko A; Heller H; Eytan E; Kaklij G; Rose I A. Role of the alpha-amino group of protein in ubiquitin-mediated protein breakdown. Proceedings of the National Academy of Sciences of the United States of America 1984;81(22):7021-5.
34.    Jaworowski A; Hartman F C; Rose I A. Intermediates in the ribulose-1,5-bisphosphate carboxylase reaction. The Journal of biological chemistry 1984;259(11):6783-9.
35.    Haas A L; Warms J V; Rose I A Ubiquitin adenylate: structure and role in ubiquitin activation. Biochemistry 1983;22(19):4388-94.
36.    Rose I A; Warms J V. An enzyme with ubiquitin carboxy-terminal esterase activity from reticulocytes. Biochemistry 1983;22(18):4234-7.
37.    Haas A L; Rose I A. The mechanism of ubiquitin activating enzyme. A kinetic and equilibrium analysis. The Journal of biological chemistry 1982;257(17):10329-37.
38.    Rose I A; Iyengar R. Partition of intermediates of triosephosphate isomerase: slow conformational changes precede enolization and follow product release. Biochemistry 1982;21(7):1591-7.
39.    Haas A L; Warms J V; Hershko A; Rose I A. Ubiquitin-activating enzyme. Mechanism and role in protein-ubiquitin conjugation. The Journal of biological chemistry 1982;257(5):2543-8.
40.    Rose I A; Warms J V. Stability of hexokinase II in vitro and in ascites tumor cells.
Archives of biochemistry and biophysics 1982;213(2):625-34.
41.     Rose I A. Enzymology of enol intermediates. Österreichische Zeitschrift für Stomatologie 1982;87():84-97.
42.    Haas A L; Rose I A. Hemin inhibits ATP-dependent ubiquitin-dependent proteolysis: role of hemin in regulating ubiquitin conjugate degradation. Proceedings of the National Academy of Sciences of the United States of America 1981;78(11):6845-8.
43.    Wilkinson K D; Rose I A. Study of crystalline hexokinase-glucose complexes by isotope trapping. The Journal of biological chemistry 1981;256(19):9890-4.
44.    Rose I A. Chemistry of proton abstraction by glycolytic enzymes (aldolase, isomerases and pyruvate kinase). Philosophical transactions of the Royal Society of London. Series B, Biological sciences 1981;293(1063):131-43.
45.     Iyengar R; Rose I A. Liberation of the triosephosphate isomerase reaction intermediate and its trapping by isomerase, yeast aldolase, and methylglyoxal synthase. Biochemistry 1981;20(5):1229-35.
46.    Iyengar R; Rose I A. Concentration of activated intermediates of the fructose-1,6-bisphosphate aldolase and triosephosphate isomerase reactions. Biochemistry 1981;20(5):1223-9.
47.     Hershko A; Ciechanover A; Rose I A. Identification of the active amino acid residue of the polypeptide of ATP-dependent protein breakdown. The Journal of biological chemistry 1981;256(4):1525-8.
48.    Wilkinson K D; Rose I A. Glucose exchange and catalysis by two crystalline hexokinase x glucose complexes. Evidence for an obligatory ATP-dependent conformational change in catalysis. The Journal of biological chemistry 1980;255(16):7569-74.
49.    Rose I A. Mechanism of phosphoryl transfer by hexokinase. Biochemical and biophysical research communications 1980;94(2):573-8.
50.    Rose I A; Hanson K R; Wilkinson K D; Wimmer M J. A suggestion for naming faces of ring compounds. Proceedings of the National Academy of Sciences of the United States of America 1980;77(5):2439-41.
51.     Hershko A; Ciechanover A; Heller H; Haas A L; Rose I A. Proposed role of ATP in protein breakdown: conjugation of protein with multiple chains of the polypeptide of ATP-dependent proteolysis. Proceedings of the National Academy of Sciences of the United States of America 1980;77(4):1783-6.
52.     Rose I A; Warms J V. Lithium on glucose uptake in brain; role of glucose-1,6-P2 as a regulator of hexokinase. Biochemical and biophysical research communications 1980;92(3):1030-6.
53.    Rose I A.
The isotope trapping method: desorption rates of productive E.S complexes.
Methods in enzymology 1980;64():47-59.
54.    Wilkinson K D; Rose I A. Isotope trapping studies of yeast hexokinase during steady state catalysis. A combined rapid quench and isotope trapping technique. The Journal of biological chemistry 1979;254(24):12567-72.
55.    Rose I A; Warms J V; Hershko A. A high molecular weight protease in liver cytosol.
The Journal of biological chemistry 1979;254(17):8135-8.

56.    Hershko A; Ciechanover A; Rose I A. Resolution of the ATP-dependent proteolytic system from reticulocytes: a component that interacts with ATP. Proceedings of the National Academy of Sciences of the United States of America 1979;76(7):3107-10.
57.     Wimmer M J; Rose I A; Powers S G; Meister A. Evidence that carboxyphosphate is a kinetically competent intermediate in the carbamyl phosphate synthetase reaction.
The Journal of biological chemistry 1979;254(6):1854-9.
58.     Wilkinson K D; Rose I A. Activation of yeast hexokinase PII. Changes in conformation and association. The Journal of biological chemistry 1979;254(6):2125-31.
59.     Rose I A. Positional isotope exchange studies of enzyme mechanisms. Advances in enzymology and related areas of molecular biology 1979;50():361-95.
60.    Rose I A. Enzyme reactions of ATP studied by positional isotope exchange.
Federation proceedings 1978;37(14):2775-82.
61.    Wimmer M J; Rose I A. Mechanisms of enzyme-catalyzed group transfer reactions.
Annual review of biochemistry 1978;47():1031-78.
62.    Wimmer M J; Rose I A. Mechanism for oxygen exchange in the chloroplast photophosphorylation system. The Journal of biological chemistry 1977;252(19):6769-75.
63.    Rose I A; Warms J V; Wong L J. Inhibitors of glucose-1,6-bisphosphate synthase.
The Journal of biological chemistry 1977;252(12):4262-8.
64.    Summers M C; Rose I A. Proton transfer reactions of methylglyoxal synthase.
Journal of the American Chemical Society 1977;99(13):4475-8.
65.    Midelfort C F; Rose I A. Studies on the mechanism of Escherichia coli glucosamine-6-phosphate isomerase. Biochemistry 1977;16(8):1590-6.
66.     Rose I A; O’Connell E L. Specificity of fructose-1, 6-P2 aldolase (muscle) and partition of the enzyme among catalytic intermediates in the steady state.
The Journal of biological chemistry 1977;252(2):479-82.
67.    O’Connell E L; Rose I A. Glycidol phosphates and 1,2-anhydrohexitol 6-phosphates.
Methods in enzymology 1977;46():381-8.
68.    Midelfort C F; Rose I A. A stereochemical method for detection of ATP terminal phosphate transfer in enzymatic reactions. Glutamine synthetase. The Journal of biological chemistry 1976;251(19):5881-7.
69.    Wong L J; Rose I A. Kinetic competence of a phosphoryl enzyme intermediate in the glucose-1,6-p2 synthase-catalyzed reaction. Purification, properties, and kinetic studies.
The Journal of biological chemistry 1976;251(18):5431-9.
70.    Midelfort C F; Gupta R K; Rose I A. Fructose 1,6-bisphosphate: isomeric composition, kinetics, and substrate specificity for the aldolases. Biochemistry 1976;15(10):2178-85.
71.    Rose I A; O’Connell E L; Solomon F. Intermolecular tritium transfer in the transcarboxylase reaction. The Journal of biological chemistry 1976;251(3):902-4.
72.    Creighton D J; Rose I A. Oxalacetate decarboxylase activity in muscle is due to pyruvate kinase. The Journal of biological chemistry 1976;251(1):69-72.
73.    Creighton D J; Rose I A. Studies on the mechanism and stereochemical properties of the oxalacetate decarboxylase activity of pyruvate kinase. The Journal of biological chemistry 1976;251(1):61-8.
74.    Rose I A; Warms J V. PH dependence of the alpha-glucose 1,6-diphosphate inhibition of hexokinase II. Archives of biochemistry and biophysics 1975;171(2):678-81.
75.    Rose I A; Warms J V; Kaklij G. A specific enzyme for glucose 1,6-bisphosphate synthesis. The Journal of biological chemistry 1975;250(9):3466-70.
76.    Rose I A. Mechanism of the aldose-ketose isomerase reactions. Advances in enzymology and related areas of molecular biology 1975;43():491-517.
77.    Rose I A. Preparation of phosphoenolpyruvate and pyruvate specifically labeled with deuterium and tritium. Methods in enzymology 1975;41():110-5.
78.    Murakami K; Rose I A. Inactivation and reactivation of hexokinase type II. Archives of biochemistry and biophysics 1974;165(2):519-23.
79.    Rose I A; Warms J V; Kosow D P. Specificity for the glucose-6-P inhibition site of hexokinase. Archives of biochemistry and biophysics 1974;164(2):729-35.
80.    Rose I A; O’Connell E L; Litwin S. Determination of the rate of hexokinase-glucose dissociation by the isotope-trapping method. The Journal of biological chemistry 1974;249(16):5163-8.
81.    Rose I A; Warms J V. Glucose- and mannose-1,6-P2 as activators of phosphofructokinase in red blood cells. Biochemical and biophysical research communications 1974;59(4):1333-40.
82.    Willard J M; Rose I A. Formation of enolpyruvate in the phosphoenolpyruvate carboxytransphosphorylase reaction. Biochemistry 1973;12(26):5241-6.
83.    Kosow D P; Oski F A; Warms J V; Rose I A. Regulation of mammalian hexokinase: regulatory differences between isoenzyme I and II. Archives of biochemistry and biophysics 1973;157(1):114-24.
84.     Schray K J; O’Connell E L; Rose I A. Inactivation of muscle triose phosphate isomerase by D- and L-glycidol phosphate. The Journal of biological chemistry 1973;248(6):2214-8.
85.    Rose I A; O’Connell E L; Schray K J. Mannose 6-phosphate: anomeric form used by phosphomannose isomerase and its 1-epimerization by phosphoglucose isomerase.
The Journal of biological chemistry 1973;248(6):2232-4.
86.    O’Connell E L; Rose I A. Affinity labeling of phosphoglucose isomerase by 1,2-anhydrohexitol-6-phosphates. The Journal of biological chemistry 1973;248(6):2225-31.
87.    Schray K J; Benkovic S J; Benkovic P A; Rose I A. Catalytic reactions of phosphoglucose isomerase with cyclic forms of glucose 6-phosphate and fructose 6-phosphate. The Journal of biological chemistry 1973;248(6):2219-24.
88.    Kosow D P; Rose I A. Origin of the delayed feedback control of glucose utilization in ascites tumor cells. Biochemical and biophysical research communications 1972;48(2):376-83.
89.    Robinson J L; Rose I A. The proton transfer reactions of muscle pyruvate kinase. The Journal of biological chemistry 1972;247(4):1096-105.
90.    Rose I A. Enzyme reaction stereospecificity: a critical review. CRC critical reviews in biochemistry 1972;1(1):33-57.
91.    McFadden B A; Rose I A; Williams J O. Production of pyruvate and succinate by action of isocitrate lyase on -methylisocitrate. Archives of biochemistry and biophysics 1972;148(1):84-8.
92.    Solomon F; Rose I A. Significance of ADP-ATP exchange for the hexokinase reaction mechanism. Archives of biochemistry and biophysics 1971;147(1):349-50.
93.    Klinman J P; Rose I A. Stereochemistry of the interconversions of citrate and acetate catalyzed by citrate synthase, adenosine triphosphate citrate lyase, and citrate lyase.
Biochemistry 1971;10(12):2267-72.
94.    Klinman J P; Rose I A. Mechanism of the aconitate isomerase reaction. Biochemistry 1971;10(12):2259-66.
95.    Klinman J P; Rose I A. Purification and kinetic properties of aconitate isomerase from Pseudomonas putida. Biochemistry 1971;10(12):2253-9.
96.     Rose I A. Regulation of human red cell glycolysis: a review. Experimental eye research 1971;11(3):264-72.
97.     Kosow D P; Rose I A. Activators of yeast hexokinase. The Journal of biological chemistry 1971;246(8):2618-25.
98.    Schray K J; Rose I A. Anomeric specificity and mechanism of two pentose isomerases.
Biochemistry 1971;10(6):1058-62.
99.     Rose I A. Stereochemistry of pyruvate kinase, pyruvate carboxylase, and malate enzyme reactions. The Journal of biological chemistry 1970;245(22):6052-6.
100.    Rose I A; Warms J V. Control of red cell glycolysis. The cause of triose phosphate accumulation. The Journal of biological chemistry 1970;245(16):4009-15.
101.    Waley S G; Miller J C; Rose I A; O’Connell E L. Identification of site in triose phosphate isomerase labelled by glycidol phosphate. Nature 1970;227(5254):181.
102.    Cohn M; Pearson J E; O’Connell E L; Rose I A. Nuclear magnetic resonance assignment of the vinyl hydrogens of phosphoenolpyruvate. Stereochemistry of the enolase reaction. Journal of the American Chemical Society 1970;92(13):4095-8.
103.    Kosow D P; Rose I A. Product inhibition of the hexokinases. The Journal of biological chemistry 1970;245(1):198-204.
104.     Rose I A; O’Connell E L. Inactivation and labeling of triose phosphate isomerase and enolase by glycidol phosphate. The Journal of biological chemistry 1969;244(23):6548-50.
105.    Rose I A; O’Connell E L; Noce P; Utter M F; Wood H G; Willard J M; Cooper T G; Benziman M. Stereochemistry of the enzymatic carboxylation of phosphoenolpyruvate. The Journal of biological chemistry 1969;244(22):6130-3.
106.     Biellmann J F; O’Connell E L; Rose I A. Secondary isotope effects in reactions catalyzed by yeast and muscle aldolase. Journal of the American Chemical Society 1969;91(23):6484-8.
107.    Rose I A; O’Connell E L; Mortlock R P. Stereochemical evidence for a cis-enediol intermediate in Mn-dependent aldose isomerases. Biochimica et biophysica acta 1969;178(2):376-9.
108.    Rose I A; Warms J V. Glycolysis-dependent exchange of diphosphopyridine nucleotide-3H in red blood cells and ascites cells. The Journal of biological chemistry 1969;244(5):1114-7.
109.    Rose I A; O’Connell E L. Studies on the interaction of aldolase with substrate analogues. The Journal of biological chemistry 1969;244(1):126-34.
110.    Rose I A. The state of magnesium in cells as estimated from the adenylate kinase equilibrium. Proceedings of the National Academy of Sciences of the United States of America 1968;61(3):1079-86.
111.    Rose I A; O’Connell E L; Langdon R. Lack of exchange of the 1-oxygen of glucose with water during glucose transport in human red blood cells. Archives of biochemistry and biophysics 1968;126(2):727-8.
112.    Kosow D P; Rose I A. Ascites tumor mitochondrial hexokinase II. Effect of binding on kinetic properties. The Journal of biological chemistry 1968;243(13):3623-30.
113.    Oski F A; Rose I A. The role of alpha–beta glucose-6-phosphate interconversion in erythrocyte carbohydrate metabolism. The Journal of laboratory and clinical medicine 1967;70(4):535-8.
114.     Fiedler F; Müllhofer G; Trebst A; Rose I A. Mechanism of ribulose-diphosphate carboxydismutase reaction. European journal of biochemistry / FEBS 1967;1(4):395-9.
115.    Rose I A; O’Connell E L. Mechanism of aconitase action. I. The hydrogen transfer reaction. The Journal of biological chemistry 1967;242(8):1870-9.
116.    Rose I A; Warms J V. Mitochondrial hexokinase. Release, rebinding, and location. The Journal of biological chemistry 1967;242(7):1635-45.
117.    Rose I A; O’Connell E L. Demonstration of the Schiff base mechanism in an aldolase reaction by oxygen exchange. Archives of biochemistry and biophysics 1967;118(3):758-9.
118.    Rose I A; Warms J V. Control of glycolysis in the human red blood cell.
The Journal of biological chemistry 1966;241(21):4848-54.
119.    Johnson C K, Gabe E J, Taylor M R, Rose I A. Determination by neutron and x-ray diffraction of the absolute configuration of an enzymatically formed alpha-mono deuterioglycolate. Journal of the American Chemical Society 1965;87():1802-4.
120.    Rose I A, O’Connell E L, Mehler A H. Mechanism of the aldolase reaction. The Journal of biological chemistry 1965;240():1758-65.
121.    Muellhofer G, Rose I A. The position of carbon-carbon bond cleavage in the ribulose diphosphate carboxydismutase reaction.  The Journal of biological chemistry 1965;240():1341-6.
122.    Kemp R G, Rose I A. Coupling of reduced pyridine nucleotide in leuconostoc mesenteroides. The Journal of biological chemistry 1964;239():2998-3006.
123.    Rose I A; Warms J V; O’Connell E L. Role of inorganic phosphate in stimulating the glucose utilization of human red blood cells. Biochemical and biophysical research communications 1964;15(1):33-7.
124.    LIENHARD G E; ROSE I A. THE MECHANISM OF ACTION OF 6-PHOSPHOGLUCONATE DEHYDROGENASE. Biochemistry 1964;3():190-5.
125.    Lienhard G E, Rose I A. The Stereochemistry of ecarboxylation of isocitrate by isocitric acid dehydrogenase.  Biochemistry 1964;3():185-90.
126.    Rose I A, O’Connell E L. The role of glucose 6-phosphate in the regulation of glucose metabolism in human erythrocytes.  The Journal of biological chemistry 1964;239():12-7.
127.    Hanson K R, Rose I A.  The absolute stereochemical course of citric acid biosynthesis. Proceedings of the National Academy of Sciences of the United States of America 1963;50():981-8.
128.    Rose I A. Mechanism of C-H bond cleavage in aldolase and isomerase reactions.
Brookhaven symposia in biology 1962;15():293-309.
129.    Rose I A. O’Connell E L. Intramolecular hydrogen transfer in the phosphoglucose isomerase reaction. The Journal of biological chemistry 1961;236():3086-92.
130.    Rose I A. The use of kinetic isotope effects in the study of metabolic control. I. Degradation of glucose-1-D by the hexosemonophosphate pathway.
The Journal of biological chemistry 1961;236():603-9.
131.    Rose I A. O’Connell E L. Stereospecificity of the sugarphosphate isomerase reactions; a uniformity. Biochimica et biophysica acta 1960;42():159-60.
132.    Rose I A. Studies on the enolization of pyruvate by pyruvate kinase.
The Journal of biological chemistry 1960;235():1170-7.
133.    Rieder S V, Rose I A.. The mechanism of the triosephosphate isomerase reaction. The Journal of biological chemistry 1959;234(5):1007-10.
134.    Vishniac W, Rose I A. Mechanism of chlorophyll action in photosynthesis.
Nature 1958;182(4642):1089-90.
135.     Rose I A. Rieder S V. Studies on the mechanism on the aldolase reaction; isotope exchange reactions of muscle and yeast aldolase. The Journal of biological chemistry 1958;231(1):315-29.
136.    Rose I A. The mechanism of action of aldolase and the asymmetric labeling of hexose. Proceedings of the National Academy of Sciences of the United States of America 1958;44(1):10-5.
137.    Rose I A. Mechanism of the action of glyoxalase I. Biochimica et biophysica acta 1957;25(1):214-5.
138.    Rose I A, Ochoa S.  Phosphorylation by particulate preparations of Azotobacter vinelandii. The Journal of biological chemistry 1956;220(1):307-14.
139.    Rose I A, Grunberg-Manago M, Korey S R, Ochoa S. Enzymatic phosphorylation of acetate. The Journal of biological chemistry 1954;211(2):737-56.
140.    Utter M F, Kurahashi K., Rose I A. Some properties of oxalacetic carboxylase. The Journal of biological chemistry 1954;207(2):803-19.
141.    Rose I A, Carter C E. Pyrimidine precursors for Lactobacillus bulgaricus 09.
The Journal of biological chemistry 1954;207(2):701-7.
142.    Rose I A, Schweigert B S. Incorporation of C14 totally labeled nucleosides into nucleic acids. The Journal of biological chemistry 1953;202(2):635-45.
143.    Downing M, Rose I A, Schweigert B S. Purine and pyrimidine requirements of Lactobacillus leichmannii in the presence of vitamin B12 or thymidine.
Journal of bacteriology 1952;64(1):141-3.
144.    Rose I A, Schweigert B S. Effect of vitamin B12 on nucleic acid metabolism of the rat. Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine (New York, N.Y.) 1952;79(3):541-4.