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
SAP – a putative DNA-binding motif involved in chromosomal organization
L. Aravind,Eugene V. Koonin +1 more
Journal ArticleDOI
Comparative genomics and evolution of proteins involved in RNA metabolism
TL;DR: A comprehensive, genome-wide census of all enzymatic and non-enzymatic protein domains involved in RNA metabolism was conducted by using sequence profile analysis and structural comparisons, which reconstructed the principal features of LUCA's RNA metabolism system by parsimony-based evolutionary analysis of all relevant groups of orthologous proteins.
Journal ArticleDOI
Chromosome 2 Sequence of the Human Malaria Parasite Plasmodium falciparum
Malcolm J. Gardner,Herve Tettelin,Daniel J. Carucci,Leda M. Cummings,L. Aravind,Eugene V. Koonin,Shamira J. Shallom,Tanya Mason,Kelly Yu,Claire Fujii,James Pederson,Kun Shen,Junping Jing,Christopher Aston,Zhongwu Lai,David C. Schwartz,Mihaela Pertea,Steven L. Salzberg,Lixin Zhou,Granger G. Sutton,Rebecca A. Clayton,Owen White,Hamilton O. Smith,Claire M. Fraser,Mark D. Adams,J. Craig Venter,Stephen L. Hoffman +26 more
TL;DR: Chromosome 2 of Plasmodium falciparum was sequenced; this sequence contains 947,103 base pairs and encodes 210 predicted genes as discussed by the authors.
Journal ArticleDOI
The HD domain defines a new superfamily of metal-dependent phosphohydrolases
L. Aravind,Eugene V. Koonin +1 more
Journal ArticleDOI
Unification of Cas protein families and a simple scenario for the origin and evolution of CRISPR-Cas systems
TL;DR: Evidence is presented that large subunits contained in most of the CRISPR-Cas systems could be homologous to Cas10 proteins which contain a polymerase-like Palm domain and are predicted to be enzymatically active in Type III CRISpr-cas systems but inactivated in Type I systems.