Jonathan J. Burbaum - Publications
Affiliations: | Harvard University, Cambridge, MA, United States |
Area:
Chemistry; EnzymologyYear | Citation | Score | |||
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2004 | Adam GC, Burbaum J, Kozarich JW, Patricelli MP, Cravatt BF. Mapping enzyme active sites in complex proteomes. Journal of the American Chemical Society. 126: 1363-8. PMID 14759193 DOI: 10.1021/Ja038441G | 0.447 | |||
1992 | Burbaum JJ, Schimmel P. Amino acid binding by the Class I aminoacyl‐tRNA synthetases: Role for a conserved proline in the signature sequence Protein Science. 1: 575-581. PMID 1304356 DOI: 10.1002/Pro.5560010503 | 0.571 | |||
1991 | Burbaum JJ, Schimmel P. Assembly of a class I tRNA synthetase from products of an artificially split gene. Biochemistry. 30: 319-324. PMID 1988033 DOI: 10.1021/Bi00216A002 | 0.549 | |||
1991 | Schimmel P, Burbaum JJ. [25] Transfer RNA with double identity for in Vitro kinetic modeling of transfer RNA identity in Vivo Methods in Enzymology. 203: 485-500. PMID 1762569 DOI: 10.1016/0076-6879(91)03027-E | 0.555 | |||
1990 | Burbaum JJ, Starzyk RM, Schimmel P. Understanding structural relationships proteins of unsolved three‐dimensional structure Proteins. 7: 99-111. PMID 2183216 DOI: 10.1002/Prot.340070202 | 0.501 | |||
1989 | Starzyk RM, Burbaum JJ, Schimmel P. Insertion of new sequences into the catalytic domain of an enzyme. Biochemistry. 28: 8479-8484. PMID 2690943 DOI: 10.1021/Bi00447A031 | 0.604 | |||
1989 | Burbaum JJ, Knowles JR. Internal thermodynamics of enzymes determined by equilibrium quench: values of Kint for enolase and creatine kinase. Biochemistry. 28: 9306-17. PMID 2611231 DOI: 10.1021/Bi00450A010 | 0.572 | |||
1989 | Burbaum JJ, Raines RT, Albery WJ, Knowles JR. Evolutionary optimization of the catalytic effectiveness of an enzyme. Biochemistry. 28: 9293-305. PMID 2611230 DOI: 10.1021/Bi00450A009 | 0.583 | |||
1989 | Burbaum JJ, Knowles JR. The nature of pyruvate bound to pyruvate kinase as determined by 13C NMR spectroscopy Bioorganic Chemistry. 17: 359-371. DOI: 10.1016/0045-2068(89)90037-0 | 0.553 | |||
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