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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The prokaryotic antecedents of the ubiquitin-signaling system and the early evolution of ubiquitin-like β-grasp domains
TL;DR: In this paper, the authors systematically analyzed prokaryotic Ub-related β-grasp fold proteins using sensitive sequence profile searches and structural analysis, and identified novel Ubrelated proteins beyond the characterized ThiS, MoaD, TGS, and YukD domains.
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Identification of the m6Am Methyltransferase PCIF1 Reveals the Location and Functions of m6Am in the Transcriptome.
Konstantinos Boulias,Konstantinos Boulias,Diana Toczydlowska-Socha,Diana Toczydlowska-Socha,Ben R Hawley,Noa Liberman,Noa Liberman,Ken Takashima,Ken Takashima,Sara Zaccara,Théo Guez,Jean-Jacques Vasseur,Françoise Debart,L. Aravind,Samie R. Jaffrey,Eric L. Greer,Eric L. Greer +16 more
TL;DR: It is found that PCIF1 binds and is dependent on the m7G cap, and the accurate mapping technique will facilitate future studies to characterize m6Am's function.
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A novel family of predicted phosphoesterases includes Drosophila prune protein and bacterial recJ exonuclease
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Emergence of diverse biochemical activities in evolutionarily conserved structural scaffolds of proteins
TL;DR: Comparative analysis of numerous protein structures that have become available in the past few years, combined with genome comparison, has yielded new insights into the evolution of enzymes and their functions, revealing biochemical plasticity of a fold seems to hinge on the presence of a generic, symmetrical substrate-binding pocket as opposed to highly specialized binding sites.
Journal Article
SPOUT: a class of methyltransferases that includes spoU and trmD RNA methylase superfamilies, and novel superfamilies of predicted prokaryotic RNA methylases.
TL;DR: It is shown that the SpoU superfamily encompasses a greater diversity of (predicted) methylases than previously appreciated and contains two previously undetected families that are specific to the archaea and thermophilic bacteria.