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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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ALOG domains: provenance of plant homeotic and developmental regulators from the DNA-binding domain of a novel class of DIRS1-type retroposons

TL;DR: The evolutionary history of the ALOG domain represents a unique instance of a domain, otherwise exclusively found in retroelements, being recruited as a specific transcription factor in the streptophyte lineage of plants, adding to the growing evidence for derivation of DNA-binding domains of eukaryotic specific TFs from mobile and selfish elements.
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CYSTM, a novel cysteine-rich transmembrane module with a role in stress tolerance across eukaryotes

TL;DR: CYSTM proteins are likely to be part of a novel cellular protective mechanism that is widely active in eukaryotes, including humans, and may have critical role in responding to deleterious compounds at the plasma membrane via chelation or redox-based mechanisms.
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Antimicrobial Peptides, Polymorphic Toxins, and Self-Nonself Recognition Systems in Archaea: an Untapped Armory for Intermicrobial Conflicts.

TL;DR: This work confidently predicts that more than 1,600 archaeal proteins, currently annotated as “hypothetical” in public databases, are components of conflict and self-versus-nonself discrimination systems.
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Structure-function analysis of manganese exporter proteins across bacteria

TL;DR: The role of three structurally related proteins known or predicted to be involved in manganese transport in bacteria from the MntP, UPF0016, and TerC families are characterized and the first phenotypic and biochemical evidence for the role of Alx, a member of the TerC family, inManganese homeostasis is provided.
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TET methylcytosine oxidases: new insights from a decade of research

TL;DR: The puzzle of whether DNA methylation was reversible remained unclear for many decades until the discovery of the TET (Ten-Eleven Translocation) family of 5-methylcytosine oxidases, which use reduced iron, molecular oxygen and the tricarboxylic acid cycle metabolite 2-oxoglutarate to oxidise the methyl group of 5mC to 5-hydroxymethylcyTosine (5hmC) and beyond.