Siddhesh S. Kamat - Publications

Affiliations: 
2016- Biology & Chemistry Indian Inst. of Science Education and Research (IISER) Pune 
Area:
Chemical Biology, Biochemistry

14 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
2016 Kory N, Grond S, Kamat SS, Li Z, Krahmer N, Chitraju C, Zhou P, Fröhlich F, Semova I, Ejsing C, Zechner R, Cravatt BF, Farese RV, Walther TC. Mice Lacking Lipid Droplet-Associated Hydrolase, a Gene Linked to Human Prostate Cancer, Have Normal Cholesterol Ester Metabolism. Journal of Lipid Research. PMID 27836991 DOI: 10.1194/jlr.M072538  0.4
2016 Kolar MJ, Kamat SS, Parsons WH, Homan EA, Maher T, Peroni OD, Syed I, Fjeld K, Molven A, Kahn BB, Cravatt BF, Saghatelian A. Branched Fatty Acid Esters of Hydroxy Fatty Acids Are Preferred Substrates of the MODY8 Protein Carboxyl Ester Lipase. Biochemistry. PMID 27509211 DOI: 10.1021/acs.biochem.6b00565  1
2016 Ogura Y, Parsons WH, Kamat SS, Cravatt BF. A calcium-dependent acyltransferase that produces N-acyl phosphatidylethanolamines. Nature Chemical Biology. PMID 27399000 DOI: 10.1038/nchembio.2127  1
2016 Parsons WH, Kolar MJ, Kamat SS, Iii AB, Hulce JJ, Saez E, Kahn BB, Saghatelian A, Cravatt BF. AIG1 and ADTRP are atypical integral membrane hydrolases that degrade bioactive FAHFAs. Nature Chemical Biology. PMID 27018888 DOI: 10.1038/nchembio.2051  1
2015 Kamat SS, Camara K, Parsons WH, Chen DH, Dix MM, Bird TD, Howell AR, Cravatt BF. Immunomodulatory lysophosphatidylserines are regulated by ABHD16A and ABHD12 interplay. Nature Chemical Biology. 11: 164-71. PMID 25580854 DOI: 10.1038/nchembio.1721  1
2015 Camara K, Kamat SS, Lasota CC, Cravatt BF, Howell AR. Combining cross-metathesis and activity-based protein profiling: new β-lactone motifs for targeting serine hydrolases. Bioorganic & Medicinal Chemistry Letters. 25: 317-21. PMID 25541002 DOI: 10.1016/j.bmcl.2014.11.038  1
2014 Korczynska M, Xiang DF, Zhang Z, Xu C, Narindoshvili T, Kamat SS, Williams HJ, Chang SS, Kolb P, Hillerich B, Sauder JM, Burley SK, Almo SC, Swaminathan S, Shoichet BK, et al. Functional annotation and structural characterization of a novel lactonase hydrolyzing D-xylono-1,4-lactone-5-phosphate and L-arabino-1,4-lactone-5-phosphate. Biochemistry. 53: 4727-38. PMID 24955762 DOI: 10.1021/bi500595c  1
2013 Kamat SS, Burgos ES, Raushel FM. Potent inhibition of the C-P lyase nucleosidase PhnI by Immucillin-A triphosphate. Biochemistry. 52: 7366-8. PMID 24111876 DOI: 10.1021/bi4013287  1
2013 Kamat SS, Raushel FM. The enzymatic conversion of phosphonates to phosphate by bacteria. Current Opinion in Chemical Biology. 17: 589-96. PMID 23830682 DOI: 10.1016/j.cbpa.2013.06.006  1
2013 Kamat SS, Williams HJ, Dangott LJ, Chakrabarti M, Raushel FM. The catalytic mechanism for aerobic formation of methane by bacteria. Nature. 497: 132-6. PMID 23615610 DOI: 10.1038/nature12061  1
2011 Kamat SS, Williams HJ, Raushel FM. Intermediates in the transformation of phosphonates to phosphate by bacteria. Nature. 480: 570-3. PMID 22089136 DOI: 10.1038/nature10622  1
2011 Kamat SS, Holmes-Hampton GP, Bagaria A, Kumaran D, Tichy SE, Gheyi T, Zheng X, Bain K, Groshong C, Emtage S, Sauder JM, Burley SK, Swaminathan S, Lindahl PA, Raushel FM. The catalase activity of diiron adenine deaminase. Protein Science : a Publication of the Protein Society. 20: 2080-94. PMID 21998098 DOI: 10.1002/pro.748  1
2011 Kamat SS, Fan H, Sauder JM, Burley SK, Shoichet BK, Sali A, Raushel FM. Enzymatic deamination of the epigenetic base N-6-methyladenine. Journal of the American Chemical Society. 133: 2080-3. PMID 21275375 DOI: 10.1021/ja110157u  1
2011 Kamat SS, Bagaria A, Kumaran D, Holmes-Hampton GP, Fan H, Sali A, Sauder JM, Burley SK, Lindahl PA, Swaminathan S, Raushel FM. Catalytic mechanism and three-dimensional structure of adenine deaminase. Biochemistry. 50: 1917-27. PMID 21247091 DOI: 10.1021/bi101788n  1
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