Sumit Chakraborty - Publications

Affiliations: 
Weill Cornell Medical College, New York, NY, United States 
Area:
tuberculosis, enzyme catalysis

12 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2013 Chakraborty S, Gruber T, Barry CE, Boshoff HI, Rhee KY. Para-aminosalicylic acid acts as an alternative substrate of folate metabolism in Mycobacterium tuberculosis. Science (New York, N.Y.). 339: 88-91. PMID 23118010 DOI: 10.1126/Science.1228980  0.301
2012 Balakrishnan A, Nemeria NS, Chakraborty S, Kakalis L, Jordan F. Determination of pre-steady-state rate constants on the Escherichia coli pyruvate dehydrogenase complex reveals that loop movement controls the rate-limiting step. Journal of the American Chemical Society. 134: 18644-55. PMID 23088422 DOI: 10.1021/Ja3062375  0.339
2012 Balakrishnan A, Paramasivam S, Chakraborty S, Polenova T, Jordan F. Solid-state nuclear magnetic resonance studies delineate the role of the protein in activation of both aromatic rings of thiamin. Journal of the American Chemical Society. 134: 665-72. PMID 22092024 DOI: 10.1021/Ja209856X  0.321
2009 Li P, Chakraborty S, Stubbe J. Detection of covalent and noncovalent intermediates in the polymerization reaction catalyzed by a C149S class III polyhydroxybutyrate synthase. Biochemistry. 48: 9202-11. PMID 19711985 DOI: 10.1021/Bi901329B  0.302
2009 Nemeria NS, Chakraborty S, Balakrishnan A, Jordan F. Reaction mechanisms of thiamin diphosphate enzymes: defining states of ionization and tautomerization of the cofactor at individual steps. The Febs Journal. 276: 2432-46. PMID 19476485 DOI: 10.1111/J.1742-4658.2009.06964.X  0.313
2009 Brandt GS, Kneen MM, Chakraborty S, Baykal AT, Nemeria N, Yep A, Ruby DI, Petsko GA, Kenyon GL, McLeish MJ, Jordan F, Ringe D. Snapshot of a reaction intermediate: analysis of benzoylformate decarboxylase in complex with a benzoylphosphonate inhibitor. Biochemistry. 48: 3247-57. PMID 19320438 DOI: 10.1021/Bi801950K  0.343
2009 Chakraborty S, Nemeria NS, Balakrishnan A, Brandt GS, Kneen MM, Yep A, McLeish MJ, Kenyon GL, Petsko GA, Ringe D, Jordan F. Detection and time course of formation of major thiamin diphosphate-bound covalent intermediates derived from a chromophoric substrate analogue on benzoylformate decarboxylase. Biochemistry. 48: 981-94. PMID 19140682 DOI: 10.1021/Bi801810H  0.334
2008 Brandt GS, Nemeria N, Chakraborty S, McLeish MJ, Yep A, Kenyon GL, Petsko GA, Jordan F, Ringe D. Probing the active center of benzaldehyde lyase with substitutions and the pseudosubstrate analogue benzoylphosphonic acid methyl ester. Biochemistry. 47: 7734-43. PMID 18570438 DOI: 10.1021/Bi8004413  0.324
2008 Chakraborty S, Nemeria N, Yep A, McLeish MJ, Kenyon GL, Jordan F. Mechanism of benzaldehyde lyase studied via thiamin diphosphate-bound intermediates and kinetic isotope effects. Biochemistry. 47: 3800-9. PMID 18314961 DOI: 10.1021/Bi702302U  0.342
2007 Nemeria N, Chakraborty S, Baykal A, Korotchkina LG, Patel MS, Jordan F. The 1',4'-iminopyrimidine tautomer of thiamin diphosphate is poised for catalysis in asymmetric active centers on enzymes. Proceedings of the National Academy of Sciences of the United States of America. 104: 78-82. PMID 17182735 DOI: 10.1073/Pnas.0609973104  0.343
2006 Baykal A, Chakraborty S, Dodoo A, Jordan F. Synthesis with good enantiomeric excess of both enantiomers of alpha-ketols and acetolactates by two thiamin diphosphate-dependent decarboxylases. Bioorganic Chemistry. 34: 380-93. PMID 17083961 DOI: 10.1016/J.Bioorg.2006.09.006  0.342
2006 Nemeria NS, Korotchkina LG, Chakraborty S, Patel MS, Jordan F. Acetylphosphinate is the most potent mechanism-based substrate-like inhibitor of both the human and Escherichia coli pyruvate dehydrogenase components of the pyruvate dehydrogenase complex. Bioorganic Chemistry. 34: 362-79. PMID 17070897 DOI: 10.1016/J.Bioorg.2006.09.001  0.323
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