| Year |
Citation |
Score |
| 2006 |
Rose I. Ubiquitin at Fox Chase: Nobel lecture Israel Journal of Chemistry. 46: 107-111. DOI: 10.1560/Etpm-W52U-1Qyc-Hmjv |
0.328 |
|
| 2005 |
Rose I. Ubiquitin at fox chase (Nobel Lecture) Angewandte Chemie - International Edition. 44: 5927-5931. PMID 16142821 DOI: 10.1002/Anie.200500995 |
0.328 |
|
| 2005 |
Rose I. Ubiquitin in Fox Chase (Nobel-Vortrag) Angewandte Chemie. 117: 6076-6081. DOI: 10.1002/Ange.200500995 |
0.339 |
|
| 2004 |
Rose IA, Weaver TM. The role of the allosteric B site in the fumarase reaction. Proceedings of the National Academy of Sciences of the United States of America. 101: 3393-7. PMID 14990798 DOI: 10.1073/Pnas.0307524101 |
0.386 |
|
| 2002 |
Rose IA, Nowick JS. Methylglyoxal synthetase, enol-pyruvaldehyde, glutathione and the glyoxalase system. Journal of the American Chemical Society. 124: 13047-52. PMID 12405831 DOI: 10.1021/Ja027065H |
0.309 |
|
| 1993 |
Rose IA, Warms JV, Yuan RG. Role of conformational change in the fumarase reaction cycle. Biochemistry. 32: 8504-11. PMID 8357797 DOI: 10.1021/bi00084a016 |
0.33 |
|
| 1993 |
Kuo DJ, Rose IA. Mechanism of proton abstraction in biotin-dependent carboxylation reactions Journal of the American Chemical Society. 115: 387-390. DOI: 10.1021/Ja00055A003 |
0.39 |
|
| 1992 |
Hadari T, Warms JV, Rose IA, Hershko A. A ubiquitin C-terminal isopeptidase that acts on polyubiquitin chains. Role in protein degradation. The Journal of Biological Chemistry. 267: 719-27. PMID 1309773 |
0.715 |
|
| 1991 |
Seeholzer SH, Jaworowski A, Rose IA. Enolpyruvate: chemical determination as a pyruvate kinase intermediate. Biochemistry. 30: 727-32. PMID 1988060 DOI: 10.1021/Bi00217A022 |
0.446 |
|
| 1987 |
Hershko A, Rose IA. Ubiquitin-aldehyde: a general inhibitor of ubiquitin-recycling processes. Proceedings of the National Academy of Sciences of the United States of America. 84: 1829-33. PMID 3031653 DOI: 10.1073/Pnas.84.7.1829 |
0.723 |
|
| 1987 |
Rose IA, Warms JV. A specific endpoint assay for ubiquitin. Proceedings of the National Academy of Sciences of the United States of America. 84: 1477-81. PMID 3031643 DOI: 10.1073/Pnas.84.6.1477 |
0.467 |
|
| 1987 |
Kuo DJ, Rose IA. Aconitase: its source of catalytic protons. Biochemistry. 26: 7589-96. PMID 2827757 DOI: 10.1021/Bi00398A009 |
0.319 |
|
| 1986 |
Pickart CM, Rose IA. Mechanism of ubiquitin carboxyl-terminal hydrolase. Borohydride and hydroxylamine inactivate in the presence of ubiquitin. The Journal of Biological Chemistry. 261: 10210-7. PMID 3015923 |
0.719 |
|
| 1985 |
Rose IA, Warms JV. Complexes of muscle aldolase in equilibrium with fructose 1,6-bisphosphate. Biochemistry. 24: 3952-7. PMID 4052378 DOI: 10.1021/Bi00336A023 |
0.456 |
|
| 1985 |
Kuo DJ, Rose IA. Chemical trapping of complexes of dihydroxyacetone phosphate with muscle fructose-1,6-bisphosphate aldolase. Biochemistry. 24: 3947-52. PMID 4052377 DOI: 10.1021/Bi00336A022 |
0.445 |
|
| 1985 |
Jaworowski A, Rose IA. Partition kinetics of ribulose-1,5-bisphosphate carboxylase from Rhodospirillum rubrum. The Journal of Biological Chemistry. 260: 944-8. PMID 3918036 |
0.303 |
|
| 1985 |
Pickart CM, Rose IA. Functional heterogeneity of ubiquitin carrier proteins. Progress in Clinical and Biological Research. 180: 215. PMID 2994086 |
0.649 |
|
| 1985 |
Pickart CM, Rose IA. Ubiquitin carboxyl-terminal hydrolase acts on ubiquitin carboxyl-terminal amides. The Journal of Biological Chemistry. 260: 7903-10. PMID 2989266 |
0.616 |
|
| 1985 |
Pickart CM, Rose IA. Functional heterogeneity of ubiquitin carrier proteins. The Journal of Biological Chemistry. 260: 1573-81. PMID 2981864 |
0.702 |
|
| 1984 |
Rose IA. Failure to confirm previous observations on triosephosphate isomerase intermediate and bound substrate complexes. Biochemistry. 23: 5893-4. PMID 6525338 DOI: 10.1021/Bi00319A032 |
0.306 |
|
| 1984 |
Jaworowski A, Hartman FC, Rose IA. Intermediates in the ribulose-1,5-bisphosphate carboxylase reaction. The Journal of Biological Chemistry. 259: 6783-9. PMID 6427222 |
0.323 |
|
| 1984 |
Hershko A, Heller H, Eytan E, Kaklij G, Rose IA. 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. 81: 7021-5. PMID 6095265 DOI: 10.1073/Pnas.81.22.7021 |
0.681 |
|
| 1983 |
Haas AL, Warms JV, Rose IA. Ubiquitin adenylate: structure and role in ubiquitin activation. Biochemistry. 22: 4388-94. PMID 6313038 DOI: 10.1021/Bi00288A007 |
0.694 |
|
| 1983 |
Rose IA, Warms JV. An enzyme with ubiquitin carboxy-terminal esterase activity from reticulocytes. Biochemistry. 22: 4234-7. PMID 6313036 DOI: 10.1021/Bi00287A012 |
0.471 |
|
| 1983 |
Iyengar R, Rose IA. Methylglyoxal synthase uses the trans isomer or triose-1,2-enediol 3-phosphate Journal of the American Chemical Society. 105: 3301-3303. DOI: 10.1021/Ja00348A057 |
0.304 |
|
| 1983 |
Rose IA, Iyengar R. The D2O effect on catalysis by triose phosphate isomerase requires isotope exchange on the enzyme Journal of the American Chemical Society. 105: 295-297. DOI: 10.1021/Ja00340A027 |
0.355 |
|
| 1982 |
Haas AL, Rose IA. The mechanism of ubiquitin activating enzyme. A kinetic and equilibrium analysis. The Journal of Biological Chemistry. 257: 10329-37. PMID 6286650 |
0.599 |
|
| 1982 |
Haas AL, Warms JV, Hershko A, Rose IA. Ubiquitin-activating enzyme. Mechanism and role in protein-ubiquitin conjugation. The Journal of Biological Chemistry. 257: 2543-8. PMID 6277905 |
0.776 |
|
| 1981 |
Iyengar R, Rose IA. Liberation of the triosephosphate isomerase reaction intermediate and its trapping by isomerase, yeast aldolase, and methylglyoxal synthase. Biochemistry. 20: 1229-35. PMID 7013791 DOI: 10.1021/Bi00508A027 |
0.45 |
|
| 1981 |
Iyengar R, Rose IA. Concentration of activated intermediates of the fructose-1,6-bisphosphate aldolase and triosephosphate isomerase reactions. Biochemistry. 20: 1223-9. PMID 7013790 DOI: 10.1021/Bi00508A026 |
0.447 |
|
| 1981 |
Haas AL, Rose IA. 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. 78: 6845-8. PMID 6273891 DOI: 10.1073/Pnas.78.11.6845 |
0.645 |
|
| 1981 |
Hershko A, Ciechanover A, Rose IA. Identification of the active amino acid residue of the polypeptide of ATP-dependent protein breakdown. The Journal of Biological Chemistry. 256: 1525-8. PMID 6257674 |
0.725 |
|
| 1980 |
Rose IA. The isotope trapping method: desorption rates of productive E.S complexes. Methods in Enzymology. 64: 47-59. PMID 7374457 DOI: 10.1016/S0076-6879(80)64004-X |
0.382 |
|
| 1980 |
Hershko A, Ciechanover A, Heller H, Haas AL, Rose IA. 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. 77: 1783-6. PMID 6990414 DOI: 10.1073/Pnas.77.4.1783 |
0.782 |
|
| 1979 |
Rose IA, Warms JV, Hershko A. A high molecular weight protease in liver cytosol. The Journal of Biological Chemistry. 254: 8135-8. PMID 468813 |
0.663 |
|
| 1979 |
Hershko A, Ciechanover A, Rose IA. 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. 76: 3107-10. PMID 290989 DOI: 10.1073/Pnas.76.7.3107 |
0.73 |
|
| 1978 |
Rose IA. Enzyme reactions of ATP studied by positional isotope exchange. Federation Proceedings. 37: 2775-82. PMID 31305 |
0.327 |
|
| 1977 |
O'Connell EL, Rose IA. Glycidol phosphates and 1,2-anhydrohexitol 6-phosphates. Methods in Enzymology. 46: 381-8. PMID 909428 DOI: 10.1016/S0076-6879(77)46045-2 |
0.301 |
|
| 1977 |
Summers MC, Rose IA. Proton transfer reactions of methylglyoxal synthase. Journal of the American Chemical Society. 99: 4475-8. PMID 325056 DOI: 10.1021/Ja00455A044 |
0.301 |
|
| 1977 |
Midelfort CF, Rose IA. Studies on the mechanism of Escherichia coli glucosamine-6-phosphate isomerase. Biochemistry. 16: 1590-6. PMID 322702 DOI: 10.1021/Bi00627A010 |
0.377 |
|
| 1976 |
Rose IA, O'Connell EL, Solomon F. Intermolecular tritium transfer in the transcarboxylase reaction. The Journal of Biological Chemistry. 251: 902-4. PMID 1249062 |
0.54 |
|
| 1976 |
Creighton DJ, Rose IA. Oxalacetate decarboxylase activity in muscle is due to pyruvate kinase. The Journal of Biological Chemistry. 251: 69-72. PMID 1244356 |
0.306 |
|
| 1976 |
Creighton DJ, Rose IA. Studies on the mechanism and stereochemical properties of the oxalacetate decarboxylase activity of pyruvate kinase. The Journal of Biological Chemistry. 251: 61-8. PMID 1244355 |
0.362 |
|
| 1976 |
Wong LJ, Rose IA. 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. 251: 5431-9. PMID 987038 |
0.305 |
|
| 1976 |
Midelfort CF, Gupta RK, Rose IA. Fructose 1,6-bisphosphate: isomeric composition, kinetics, and substrate specificity for the aldolases. Biochemistry. 15: 2178-85. PMID 776219 DOI: 10.1021/Bi00655A023 |
0.367 |
|
| 1976 |
Midelfort CF, Rose IA. A stereochemical method for detection of ATP terminal phosphate transfer in enzymatic reactions. Glutamine synthetase. The Journal of Biological Chemistry. 251: 5881-7. PMID 9406 |
0.348 |
|
| 1975 |
Hanson KR, Rose IA. Interpretations of enzyme reaction stereospecificity Accounts of Chemical Research. 8: 1-10. DOI: 10.1021/Ar50085A001 |
0.409 |
|
| 1973 |
Willard JM, Rose IA. Formation of enolpyruvate in the phosphoenolpyruvate carboxytransphosphorylase reaction. Biochemistry. 12: 5241-6. PMID 4357336 DOI: 10.1021/Bi00750A003 |
0.3 |
|
| 1972 |
Kosow DP, Rose IA. Origin of the delayed feedback control of glucose utilization in ascites tumor cells. Biochemical and Biophysical Research Communications. 48: 376-83. PMID 5065065 DOI: 10.1016/S0006-291X(72)80061-5 |
0.306 |
|
| 1971 |
Klinman JP, Rose IA. Stereochemistry of the interconversions of citrate and acetate catalyzed by citrate synthase, adenosine triphosphate citrate lyase, and citrate lyase. Biochemistry. 10: 2267-72. PMID 5165527 DOI: 10.1021/Bi00788A013 |
0.538 |
|
| 1971 |
Klinman JP, Rose IA. Mechanism of the aconitate isomerase reaction. Biochemistry. 10: 2259-66. PMID 5114988 DOI: 10.1021/Bi00788A012 |
0.467 |
|
| 1971 |
Klinman JP, Rose IA. Purification and kinetic properties of aconitate isomerase from Pseudomonas putida. Biochemistry. 10: 2253-9. PMID 5114987 DOI: 10.1021/Bi00788A011 |
0.462 |
|
| 1971 |
Solomon F, Rose IA. Significance of ADP-ATP exchange for the hexokinase reaction mechanism. Archives of Biochemistry and Biophysics. 147: 349-50. PMID 4255952 DOI: 10.1016/0003-9861(71)90344-4 |
0.608 |
|
| 1970 |
Rose IA. Stereochemistry of pyruvate kinase, pyruvate carboxylase, and malate enzyme reactions. The Journal of Biological Chemistry. 245: 6052-6. PMID 5484463 |
0.31 |
|
| 1964 |
Lienhard GE, Rose IA. The mechanism of action of 6-phosphogluconate dehydrogenase Biochemistry. 3: 190-195. PMID 14163940 DOI: 10.1021/bi00890a009 |
0.498 |
|
| 1964 |
Lienhard GE, Rose IA. The stereochemistry of decarboxylation of isocitrate by isocitric acid dehydrogenase Biochemistry. 3: 185-190. PMID 14163939 DOI: 10.1021/bi00890a008 |
0.514 |
|
| 1958 |
Rose IA. The absolute configuration of dihydroxyacetone phosphate tritiated by aldolase reaction Journal of the American Chemical Society. 80: 5835-5836. DOI: 10.1021/Ja01554A063 |
0.33 |
|
| 1956 |
ROSE IA, OCHOA S. Phosphorylation by particulate preparations of Azotobacter vinelandii. The Journal of Biological Chemistry. 220: 307-14. PMID 13319349 |
0.404 |
|
| 1954 |
ROSE IA, GRUNBERG-MANAGO M, KOREY SR, OCHOA S. Enzymatic phosphorylation of acetate. The Journal of Biological Chemistry. 211: 737-56. PMID 13221579 |
0.624 |
|
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