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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A bipolar DNA helicase gene, herA, clusters with rad50, mre11 and nurA genes in thermophilic archaea
TL;DR: The results suggest that the archaeal Rad50-Mre11 complex might act in association with a 5' to 3' exonuclease (NurA) and a bipolar DNA helicase (HerA) indicating a probable involvement in the initiation step of homologous recombination.
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CRISPR Screens Uncover Genes that Regulate Target Cell Sensitivity to the Morphogen Sonic Hedgehog
Ganesh V. Pusapati,Jennifer H. Kong,Bhaven B. Patel,Arunkumar Krishnan,Andreas Sagner,Maia Kinnebrew,James Briscoe,L. Aravind,Rajat Rohatgi +8 more
TL;DR: Genes that modify the interpretation of morphogen signals by regulating protein-trafficking events in target cells are uncovered, confirming the central role for primary cilia in Hh signaling.
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The SWIRM domain: a conserved module found in chromosomal proteins points to novel chromatin-modifying activities.
TL;DR: It is predicted that the proteins in which the SWIRM domain is combined with an amino-oxidase domain define a novel class of chromatin-modifying enzymes, which are likely to oxidize either the amino group of basic residues in histones and other chromosomal proteins or the polyamines in chromatin, and thereby alter the charge distribution.
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Structure of a lamprey variable lymphocyte receptor in complex with a protein antigen.
C. Alejandro Velikovsky,Lu Deng,Satoshi Tasumi,Lakshminarayan M. Iyer,Melissa C. Kerzic,L. Aravind,Zeev Pancer,Roy A. Mariuzza +7 more
TL;DR: The structure of an anti–hen egg white lysozyme (HEL) VLR, isolated by yeast display, bound to HEL is determined and it is likely that the generalized antigen-binding site of VLRs is defined.
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Novel eukaryotic enzymes modifying cell-surface biopolymers
Vivek Anantharaman,L. Aravind +1 more
TL;DR: It is posited that the combined action of the acyltransferase and esterase domain plays an important role in controlling the acYLation levels of glycans and thereby regulates their physico-chemical properties such as hygroscopicity, resistance to enzymatic hydrolysis and physical strength.