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
Classification of the caspase-hemoglobinase fold: detection of new families and implications for the origin of the eukaryotic separins.
L. Aravind,Eugene V. Koonin +1 more
TL;DR: This analysis indicates that caspase–hemoglobinase‐fold proteases and their inactivated derivatives are widespread in diverse bacteria, particularly those with a complex development, such as Streptomyces, Anabaena, Mesorhizobium, and Myxococcus.
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Comparative genomic analyses reveal a vast, novel network of nucleotide-centric systems in biological conflicts, immunity and signaling
TL;DR: Using comparative genomics, sequence and structure analysis, a vast network of systems defined by conserved prokaryotic gene-neighborhoods, which encode enzymes generating such nucleotides or alternatively processing them to yield potential signaling molecules are uncovered, pointing to evolutionary and mechanistic links.
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A superfamily of archaeal, bacterial, and eukaryotic proteins homologous to animal transglutaminases
TL;DR: It is proposed that many, if not all, microbial homologs of the transglutaminases are proteases and that the eukaryotic transglUTaminases have evolved from an ancestral protease.
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The natural history of the WRKY–GCM1 zinc fingers and the relationship between transcription factors and transposons
TL;DR: It is shown that the lineage-specific expansion of WRKY–GCM1 domain proteins acquired functional diversity mainly through expression divergence rather than by protein sequence divergence, and used as an example to illustrate the importance of transposons in the emergence of new TFs in different lineages.
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Ancient conserved domains shared by animal soluble guanylyl cyclases and bacterial signaling proteins.
TL;DR: The HNOB domain is predicted to function as a heme-dependent sensor for gaseous ligands, and transduce diverse downstream signals, in both bacteria and animals.