Year |
Citation |
Score |
2023 |
Vaidya K, Rodrigues G, Gupta S, Devarajan A, Yeolekar M, Madhusudhan MS, Kamat SS. Identification of sequence determinants for the ABHD14 enzymes. Proteins. PMID 37974539 DOI: 10.1002/prot.26632 |
0.3 |
|
2020 |
Shanbhag K, Mhetre A, Khandelwal N, Kamat SS. The Lysophosphatidylserines-An Emerging Class of Signalling Lysophospholipids. The Journal of Membrane Biology. PMID 32767057 DOI: 10.1007/S00232-020-00133-2 |
0.368 |
|
2020 |
Singh S, Joshi A, Kamat SS. Mapping the neuroanatomy of ABHD16A-ABHD12 & lysophosphatidylserines provides new insights into the pathophysiology of the human neurological disorder PHARC. Biochemistry. PMID 32462874 DOI: 10.1021/Acs.Biochem.0C00349 |
0.344 |
|
2020 |
Chattopadhyay T, Maniyadath B, Bagul HP, Chakraborty A, Shukla N, Budnar S, Rajendran A, Shukla A, Kamat SS, Kolthur-Seetharam U. Spatiotemporal gating of SIRT1 functions by O-GlcNAcylation is essential for liver metabolic switching and prevents hyperglycemia. Proceedings of the National Academy of Sciences of the United States of America. PMID 32152092 DOI: 10.1073/Pnas.1909943117 |
0.31 |
|
2019 |
Kumar M, Ojha S, Rai P, Joshi A, Kamat SS, Mallik R. Insulin activates intracellular transport of lipid droplets to release triglycerides from the liver. The Journal of Cell Biology. PMID 31604801 DOI: 10.1083/Jcb.201903102 |
0.321 |
|
2019 |
Rajendran A, Vaidya K, Mendoza J, Bridwell-Rabb J, Kamat SS. Functional annotation of ABHD14B, an orphan serine hydrolase enzyme. Biochemistry. PMID 31478652 DOI: 10.1021/Acs.Biochem.9B00703 |
0.411 |
|
2019 |
Ahmad Malik S, Acharya JD, Mehendale NK, Kamat SS, Ghaskadbi SS. Pterostilbene reverses palmitic acid mediated insulin resistance in HepG2 cells by reducing oxidative stress and triglyceride accumulation. Free Radical Research. 1-251. PMID 31223033 DOI: 10.1080/10715762.2019.1635252 |
0.347 |
|
2019 |
Kelkar DS, Ravikumar G, Mehendale N, Singh S, Joshi A, Sharma AK, Mhetre A, Rajendran A, Chakrapani H, Kamat SS. A chemical-genetic screen identifies ABHD12 as an oxidized-phosphatidylserine lipase. Nature Chemical Biology. PMID 30643283 DOI: 10.1038/S41589-018-0195-0 |
0.319 |
|
2018 |
Abhyankar V, Kaduskar B, Kamat SS, Deobagkar D, Ratnaparkhi GS. DNA/RNA methyltransferase contributes to robust host defense in ageing animals by regulating sphingolipid metabolism. The Journal of Experimental Biology. PMID 30254027 DOI: 10.1242/Jeb.187989 |
0.31 |
|
2018 |
Joshi A, Shaikh M, Singh S, Rajendran A, Mhetre A, Kamat SS. Biochemical characterization of the PHARC associated serine hydrolase ABHD12 reveals its preference for very long chain lipids. The Journal of Biological Chemistry. PMID 30237167 DOI: 10.1074/Jbc.Ra118.005640 |
0.399 |
|
2018 |
Pathak D, Mehendale N, Singh S, Mallik R, Kamat SS. Lipidomics suggests a new role for ceramide synthase in phagocytosis. Acs Chemical Biology. PMID 29963848 DOI: 10.1021/Acschembio.8B00438 |
0.402 |
|
2018 |
Ulrich EC, Kamat SS, Hove-Jensen B, Zechel DL. Methylphosphonic Acid Biosynthesis and Catabolism in Pelagic Archaea and Bacteria. Methods in Enzymology. 605: 351-426. PMID 29909833 DOI: 10.1016/Bs.Mie.2018.01.039 |
0.358 |
|
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 |
0.482 |
|
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 |
0.621 |
|
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 |
0.483 |
|
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 |
0.648 |
|
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 |
0.635 |
|
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 |
0.488 |
|
2015 |
Kamat SS, Raushel FM. PhnJ – A novel radical SAM enzyme from the C–P lyase complex Perspectives in Science. 4: 32-37. DOI: 10.1016/J.Pisc.2014.12.006 |
0.511 |
|
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 |
0.527 |
|
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 |
0.5 |
|
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 |
0.566 |
|
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 |
0.531 |
|
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 |
0.554 |
|
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 |
0.516 |
|
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 |
0.497 |
|
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 |
0.514 |
|
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