O
Omita A. Trivedi
Researcher at University of Chicago
Publications - 4
Citations - 560
Omita A. Trivedi is an academic researcher from University of Chicago. The author has contributed to research in topics: Gene & Moiety. The author has an hindex of 4, co-authored 4 publications receiving 512 citations.
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Journal ArticleDOI
Enzymic activation and transfer of fatty acids as acyl-adenylates in mycobacteria
Omita A. Trivedi,Pooja Arora,Vijayalakshmi Sridharan,Rashmi Tickoo,Debasisa Mohanty,Rajesh S. Gokhale +5 more
TL;DR: It is shown that some of the 36 annotated fadD genes, located adjacent to the PKS genes in the Mycobacterium tuberculosis genome, constitute a new class of long-chain fatty acyl-AMP ligases (FAALs), which are contrary to the previously described universal mechanism involving the formation of acy-coenzyme A thioesters.
Journal ArticleDOI
Dissecting the mechanism and assembly of a complex virulence mycobacterial lipid.
Omita A. Trivedi,Pooja Arora,Archana Vats,Mohd. Zeeshan Ansari,Rashmi Tickoo,Vijayalakshmi Sridharan,Debasisa Mohanty,Rajesh S. Gokhale +7 more
TL;DR: The molecular logic underlying the biosynthesis of a virulence lipid phthiocerol dimycocerosate (PDIM) is dissected and an attractive approach to explore host-pathogen interactions by altering mycobacterial surface coat is presented.
Journal ArticleDOI
Mechanistic and functional insights into fatty acid activation in Mycobacterium tuberculosis
Pooja Arora,Aneesh Goyal,Vivek T. Natarajan,Eerappa Rajakumara,Priyanka Verma,Radhika Gupta,Malikmohamed Yousuf,Omita A. Trivedi,Debasisa Mohanty,Anil K. Tyagi,Rajan Sankaranarayanan,Rajesh S. Gokhale +11 more
TL;DR: It is demonstrated that an insertion motif dictates formation of acyl-adenylate in FAALs, which are crucial nodes in biosynthetic network of virulent lipids and inhibitors directed against these proteins provide a unique multi-pronged approach of simultaneously disrupting several pathways.
Journal ArticleDOI
Correction: Corrigendum: Enzymic activation and transfer of fatty acids and acyl-adenylates in mycobacteria
Omita A. Trivedi,Pooja Arora,Vijayalakshmi Sridharan,Rashmi Tickoo,Debasisa Mohanty,Rajesh S. Gokhale +5 more
TL;DR: This corrects the article to show that the Higgs boson bacterium is a prokaryotic substance, not a “spatially aggregating substance”, which is a type of “plasmas” found in the fossil record.