Virendar K. Kaushik
Broad Institute
20 Papers
103 Citations
Virendar K. Kaushik is an academic researcher from Broad Institute. The author has contributed to research in topics: Biology & Small molecule. The author has an hindex of 10, co-authored 20 publications. Previous affiliations of Virendar K. Kaushik include Novartis.
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Papers
Genetic analysis in UK Biobank links insulin resistance and transendothelial migration pathways to coronary artery disease
Derek Klarin,Derek Klarin,Qiuyu Martin Zhu,Qiuyu Martin Zhu,Connor A. Emdin,Connor A. Emdin,Mark Chaffin,Mark Chaffin,Steven Horner,Brian J. McMillan,Alison Leed,Michael E. Weale,Chris C. A. Spencer,François Aguet,Ayellet V. Segrè,Kristin G. Ardlie,Amit Khera,Amit Khera,Virendar K. Kaushik,Pradeep Natarajan,Pradeep Natarajan,Sekar Kathiresan,Sekar Kathiresan +22 more
TL;DR: Phenome-wide association scanning showed that CCDC92 likely affects coronary artery disease through insulin resistance pathways, whereas experimental analysis suggests that ARHGEF26 influences the transendothelial migration of leukocytes.
Mass spectrometric techniques for label-free high-throughput screening in drug discovery.
Thomas P. Roddy,Christopher Horvath,Steven J. Stout,Kristin L. Kenney,Pei-I Ho,Ji-Hu Zhang,Chad Vickers,Virendar K. Kaushik,Brian K. Hubbard,Y. Karen Wang +9 more
TL;DR: Three techniques that have been adapted for large-scale compound library screening, including four-way parallel multiplexed electrospray liquid chromatography tandem mass spectrometry (MUX-LC/MS/MS), four- way parallel staggered gradient liquid Chromatography tandem Mass Spectrometry(MS/ MS), and eight-way staggered flow injection MS/MS following 384-well plate solid-phase extraction (SPE), are described.
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New hypotheses about the structure-function of proprotein convertase subtilisin/kexin type 9: analysis of the epidermal growth factor-like repeat A docking site using WaterMap.
Robert A. Pearlstein,Qi-Ying Hu,Jing Zhou,David Yowe,Julian Levell,Bethany A Dale,Virendar K. Kaushik,Douglas S. Daniels,Susan Hanrahan,Woody Sherman,Robert Abel +10 more
TL;DR: It is proposed that the fast kon and entropically driven thermodynamics observed for PCSK9‐EGF‐A binding stem from the functional replacement of water occupying stable PCSK 9 hydration sites, and that the relatively fast koff observed for EGF‐A unbinding stems from the limited displacement of solvent occupying unstable hydration Sites.
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Small-molecule inhibitors directly target CARD9 and mimic its protective variant in inflammatory bowel disease
Elizaveta S. Leshchiner,Elizaveta S. Leshchiner,Jason S. Rush,Michael A. Durney,Zhifang Cao,Zhifang Cao,Vlado Dančík,Benjamin Chittick,Huixian Wu,Adam Petrone,Joshua A. Bittker,Andrew J. Phillips,José Carlos Rodríguez Pérez,Alykhan F. Shamji,Virendar K. Kaushik,Mark J. Daly,Mark J. Daly,Daniel B. Graham,Daniel B. Graham,Stuart L. Schreiber,Stuart L. Schreiber,Ramnik J. Xavier,Ramnik J. Xavier +22 more
TL;DR: The feasibility of using small-molecule inhibitors to recapitulate the antiinflammatory function of CARD9 mutations associated with protection from IBD is demonstrated and biochemical insights into CARD9 variant proteins are used to create a blueprint for IBD therapeutics.
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Crystal structure of MICU2 and comparison with MICU1 reveal insights into the uniporter gating mechanism
Kimberli J. Kamer,Kimberli J. Kamer,Wei Jiang,Virendar K. Kaushik,Vamsi K. Mootha,Vamsi K. Mootha,Vamsi K. Mootha,Zenon Grabarek,Zenon Grabarek +8 more
TL;DR: The structure of MICU2 is solved and it is proposed that in the MICU1–MICU2 oligomeric complex the C-terminal helices of both proteins form a central semiautonomous assembly which contributes to the gating mechanism of the uniporter.
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