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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Conserved domains in DNA repair proteins and evolution of repair systems
TL;DR: Several additional general trends in the evolution of repair proteins were noticed; in particular, multiple, independent fusions of helicase and nuclease domains, and independent inactivation of enzymatic domains that apparently retain adaptor or regulatory functions.
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DNA Methylation on N6-Adenine in C. elegans
Eric L. Greer,Eric L. Greer,Mario Andres Blanco,Mario Andres Blanco,Lei Gu,Lei Gu,Erdem Sendinc,Erdem Sendinc,Jianzhao Liu,David Aristizábal-Corrales,David Aristizábal-Corrales,Chih-Hung Hsu,Chih-Hung Hsu,L. Aravind,Chuan He,Yang Shi,Yang Shi +16 more
TL;DR: The presence of adenine N(6)-methylation (6mA) in C. elegans DNA is demonstrated and the exciting possibility that 6mA may be a carrier of heritable epigenetic information in eukaryotes is raised.
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Evolutionary genomics of Nucleo-Cytoplasmic Large DNA Viruses
TL;DR: It is shown that subsequent evolution of the NCLDV genomes involved lineage-specific expansion of paralogous gene families and acquisition of numerous genes via horizontal gene transfer from the eukaryotic hosts, other viruses, and bacteria (primarily, endosymbionts and parasites).
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The DNA-repair protein AlkB, EGL-9, and leprecan define new families of 2-oxoglutarate- and iron-dependent dioxygenases.
L. Aravind,Eugene V. Koonin +1 more
TL;DR: Here, using sequence profile searches, it is shown that several previously undetected protein families contain 2OG-Fe(II) oxygenase fold, which allows us to predict the catalytic activity for a wide range of biologically important, but biochemically uncharacterized proteins from eukaryotes and bacteria.
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Common Origin of Four Diverse Families of Large Eukaryotic DNA Viruses
TL;DR: The conservation of the disulfide-oxidoreductase, a major capsid protein, and two virion membrane proteins indicates that the odd-shaped virions of poxviruses have evolved from the more common icosahedral virion seen in asfarviruses, iridoviruses, and phycodnaviruses.