V
Vamsi K. Mootha
Researcher at Broad Institute
Publications - 243
Citations - 90559
Vamsi K. Mootha is an academic researcher from Broad Institute. The author has contributed to research in topics: Mitochondrion & Mitochondrial DNA. The author has an hindex of 85, co-authored 227 publications receiving 73860 citations. Previous affiliations of Vamsi K. Mootha include Harvard University & Beth Israel Deaconess Medical Center.
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Journal ArticleDOI
Effects of sodium benzoate, a widely used food preservative, on glucose homeostasis and metabolic profiles in humans
Belinda Lennerz,Scott Bradley Vafai,Scott Bradley Vafai,Nigel F. Delaney,Clary B. Clish,Amy Deik,Kerry A. Pierce,David S. Ludwig,Vamsi K. Mootha,Vamsi K. Mootha +9 more
TL;DR: This study evaluated whether acute exposure to GRAS levels of sodium benzoate alters insulin and glucose homeostasis through a randomized, controlled, cross-over study of 14 overweight subjects, and found no statistically significant effect of an acute oral exposure to sodium Benzoate on glucoseHomeostasis.
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Functional Genomic Analysis of Human Mitochondrial RNA Processing
TL;DR: It is demonstrated that one such factor, FASTKD4, modulates the half-lives of a subset of mt-mRNAs and associates with mtRNAs in vivo, and may be useful for diagnosing and deciphering the pathogenesis of mtDNA disorders.
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FOXRED1, encoding an FAD-dependent oxidoreductase complex-I-specific molecular chaperone, is mutated in infantile-onset mitochondrial encephalopathy
Elisa Fassone,Andrew J. Duncan,Jan-Willem Taanman,Alistair T. Pagnamenta,Michael I. Sadowski,Tatjana Holand,Waseem Qasim,Paul Rutland,Sarah E. Calvo,Vamsi K. Mootha,Maria Bitner-Glindzicz,Shamima Rahman,Shamima Rahman +12 more
TL;DR: A combined homozygosity mapping and bioinformatics approach in a consanguineous Iranian-Jewish pedigree led to the identification of a homozygous mutation in FOXRED1 in a child who presented with infantile-onset encephalomyopathy, and this FAD-dependent oxidoreductase, which has never previously been associated with human disease, is now shown to be a complex I-specific molecular chaperone.
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Spectroscopic determination of cytochrome c oxidase content in tissues containing myoglobin or hemoglobin.
TL;DR: A simple spectroscopic method for determining the cytochrome c oxidase, cy tochrome a, a3, content in tissue and mitochondria samples independent of myoglobin or blood contamination is described.
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SARS-CoV-2 hijacks folate and one-carbon metabolism for viral replication.
Yuchen Zhang,Rui Guo,Rui Guo,Rui Guo,Sharon H. Kim,Sharon H. Kim,Hardik Shah,Hardik Shah,Shuting Zhang,Jin Hua Liang,Jin Hua Liang,Jin Hua Liang,Ying Fang,Matteo Gentili,Colin N O' Leary,Steven J Elledge,Deborah T Hung,Vamsi K. Mootha,Vamsi K. Mootha,Benjamin E. Gewurz,Benjamin E. Gewurz,Benjamin E. Gewurz +21 more
TL;DR: In this paper, the authors show that SARS-CoV-2 remodels host folate and one-carbon metabolism at the post-transcriptional level to support de novo purine synthesis, bypassing viral shutoff of host translation.