L
L. Aravind
Researcher at National Institutes of Health
Publications - 401
Citations - 88329
L. Aravind is an academic researcher from National Institutes of Health. The author has contributed to research in topics: Gene & Protein domain. The author has an hindex of 127, co-authored 388 publications receiving 81679 citations. Previous affiliations of L. Aravind include Texas A&M University & University of California, San Francisco.
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Journal ArticleDOI
O-GlcNAcylation destabilizes the active tetrameric PKM2 to promote the Warburg effect.
Yang Wang,Jia Liu,Xin Jin,Dapeng Zhang,Dongxue Li,Fengqi Hao,Yunpeng Feng,Shan Gu,Fanlin Meng,Miaomiao Tian,Yi Zheng,Ling Xin,Xinbo Zhang,Xue Han,L. Aravind,Min Wei +15 more
TL;DR: It is demonstrated that O-GlcNAcylation is a regulatory mechanism for PKM2 in cancer cells and serves as a bridge betweenPKM2 and metabolic reprogramming typical of the Warburg effect.
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Application of comparative genomics in the identification and analysis of novel families of membrane-associated receptors in bacteria.
Vivek Anantharaman,L. Aravind +1 more
TL;DR: The identification of novel receptor families in prokaryotes is likely to aid in the experimental analysis of signal transduction and environmental responses of several bacteria, including pathogens such as Leptospira, Treponema, Corynebacterium, Coxiella, Bacillus anthracis and Cytophaga.
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Ter-dependent stress response systems: novel pathways related to metal sensing, production of a nucleoside-like metabolite, and DNA-processing
TL;DR: It is shown that both the TerB and TelA domains have been linked to diverse lipid-interaction domains, such as two novel PH-like and the Coq4 domains, in different bacteria, and are likely to comprise membrane-associated sensory complexes that might additionally contain periplasmic binding-protein-II and OmpA domains.
Journal ArticleDOI
THUMP--a predicted RNA-binding domain shared by 4-thiouridine, pseudouridine synthases and RNA methylases.
L. Aravind,Eugene V. Koonin +1 more
TL;DR: It is predicted that this domain is an RNA-binding domain that adopts an alpha/beta fold similar to that found in the C-terminal domain of translation initiation factor 3 and ribosomal protein S8.
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BEN: a novel domain in chromatin factors and DNA viral proteins.
TL;DR: Contextual analysis suggests that the BEN domain mediates protein-DNA and protein-protein interactions during chromatin organization and transcription in viral DNA during replication or transcription.