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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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Book ChapterDOI

Adhesion molecules and other secreted host-interaction determinants in Apicomplexa: insights from comparative genomics.

TL;DR: In this paper, a synthetic overview of the diversity and evolutionary history of cell membrane-associated, secreted, and exported proteins related to apicomplexan parasitism is presented.
Journal ArticleDOI

Comparative genomics uncovers novel structural and functional features of the heterotrimeric GTPase signaling system

TL;DR: In this paper, the authors utilized the wealth of sequence data from recently sequenced eukaryotic genomes to uncover robust G-protein signaling systems in several poorly studied eukarial lineages such as the parabasalids, heteroloboseans and stramenopiles.
Journal ArticleDOI

Evolutionary connections between bacterial and eukaryotic signaling systems: a genomic perspective.

TL;DR: Laterally transferred protein domains, originally of bacterial provenance, appear to have contributed to the evolution of sensory pathways related to light, redox and nitric oxide signaling, and developmental pathways, such as Notch, cytokine and cytokinin signaling in eukaryotes.
Journal ArticleDOI

Diversification of AID/APOBEC-like deaminases in metazoa: multiplicity of clades and widespread roles in immunity.

TL;DR: It is proposed that biological conflicts of AADs with viruses and genomic retroelements are drivers of rapid AAD evolution, suggesting a widespread presence of mutagenesis-based immune-defense systems.
Journal ArticleDOI

Filling out the structural map of the NTF2-like superfamily

TL;DR: The analysis of these three protein domains suggests a potential non-catalytic ligand-binding role that may regulate the activities of domains with which they are combined in the same polypeptide or via operonic linkages, such as signaling domains (e.g. serine/threonine protein kinase).