Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Stephen H. Bryant"'
Publikováno v:
Bioinformatics. 33:1621-1629
Motivation Genetic variants in drug targets and metabolizing enzymes often have important functional implications, including altering the efficacy and toxicity of drugs. Identifying single nucleotide variants (SNVs) that contribute to differences in
Autor:
David I. Hurwitz, Christopher J. Lanczycki, Noreen R. Gonzales, Stephen H. Bryant, Farideh Chitsaz, James S. Song, Marc Gwadz, Gabriele H. Marchler, Narmada Thanki, Lewis Y. Geer, Dachuan Zhang, Renata C. Geer, Fu Lu, Chanjuan Zheng, Roxanne A. Yamashita, Myra K. Derbyshire, Aron Marchler-Bauer, Shennan Lu
Publikováno v:
Nucleic Acids Research
CDD, the Conserved Domain Database, is part of NCBI’s Entrez query and retrieval system and is also accessible via http://www.ncbi.nlm.nih.gov/Structure/cdd/cdd.shtml. CDD provides annotation of protein sequences with the location of conserved doma
Autor:
Ratna R. Thangudu, Aron Marchler-Bauer, Jessica H. Fong, Dachuan Zhang, Anna R. Panchenko, Manoj Tyagi, Benjamin A. Shoemaker, Thomas Madej, Stephen H. Bryant
Publikováno v:
Nucleic Acids Research
We have recently developed the Inferred Biomolecular Interaction Server (IBIS) and database, which reports, predicts and integrates different types of interaction partners and locations of binding sites in proteins based on the analysis of homologous
Autor:
Chunlei Liu, Renata C. Geer, Kenneth J. Addess, Anna R. Panchenko, Lewis Y. Geer, Thomas Madej, Stephen H. Bryant, Aron Marchler-Bauer, Christopher J. Lanczycki, Shennan Lu, Jie Chen, Jessica H. Fong, Dachuan Zhang, Yanli Wang, Paul A. Thiessen
Publikováno v:
Nucleic Acids Research
Close to 60% of protein sequences tracked in comprehensive databases can be mapped to a known three-dimensional (3D) structure by standard sequence similarity searches. Potentially, a great deal can be learned about proteins or protein families of in
Autor:
Fu-Ping Lu, Carol DeWeese-Scott, John B. Anderson, James S. Song, Christopher J. Lanczycki, Zhaoxi Ke, Farideh Chitsaz, John D. Jackson, Mikhail Mullokandov, Roxanne A. Yamashita, Aron Marchler-Bauer, Marina V. Omelchenko, Chanjuan Zheng, Naigong Zhang, Noreen R. Gonzales, Marc Gwadz, Cynthia L. Robertson, Stephen H. Bryant, Gabriele H. Marchler, Jessica H. Fong, David I. Hurwitz, Lewis Y. Geer, Narmada Thanki, Renata C. Geer, Dachuan Zhang, Myra K. Derbyshire, Shennan Lu
Publikováno v:
Nucleic Acids Research
NCBI's Conserved Domain Database (CDD) is a resource for the annotation of protein sequences with the location of conserved domain footprints, and functional sites inferred from these footprints. CDD includes manually curated domain models that make
Autor:
Stephen H. Bryant, Anna R. Panchenko
Publikováno v:
Protein Science. 11:361-370
Sequence comparison methods based on position-specific score matrices (PSSMs) have proven a useful tool for recognition of the divergent members of a protein family and for annotation of functional sites. Here we investigate one of the factors that a
Autor:
Farideh Chitsaz, Mikhail Mullokandov, Stephen H. Bryant, Siqian He, Jessica H. Fong, John B. Anderson, Fu-er Lu, Asba Tasneem, Myra K. Derbyshire, David I. Hurwitz, Renata C. Geer, Roxanne A. Yamashita, Carol DeWeese-Scott, James S. Song, Christopher J. Lanczycki, Zhaoxi Ke, Cynthia A. Liebert, Shennan Lu, Chunlei Liu, Dachuan Zhang, Noreen R. Gonzales, Naigong Zhang, Narmada Thanki, Lewis Y. Geer, John D. Jackson, Gabriele H. Marchler, Aron Marchler-Bauer, Marc Gwadz
Publikováno v:
Nucleic Acids Research
NCBI's Conserved Domain Database (CDD) is a collection of multiple sequence alignments and derived database search models, which represent protein domains conserved in molecular evolution. The collection can be accessed at http://www.ncbi.nlm.nih.gov
Publikováno v:
Nucleic Acids Research
The sequencing of complete genomes has created a pressing need for automated annotation of gene function. Because domains are the basic units of protein function and evolution, a gene can be annotated from a domain database by aligning domains to the
Autor:
James S. Song, Gabriele H. Marchler, Carol DeWeese-Scott, Jodie J. Yin, Dmitri M. Krylov, John B. Anderson, Myra K. Derbyshire, Narmada Thanki, Aron Marchler-Bauer, Christopher J. Lanczycki, Zhaoxi Ke, Mikhail Mullokandov, Roxanne A. Yamashita, Chunlei Liu, John D. Jackson, Cynthia A. Liebert, Siqian He, Noreen R. Gonzales, Shennan Lu, Marc Gwadz, Fu Lu, Stephen H. Bryant, Luning Hao, David I. Hurwitz, Dachuan Zhang
Publikováno v:
Nucleic Acids Research
The conserved domain database (CDD) is part of NCBI's Entrez database system and serves as a primary resource for the annotation of conserved domain footprints on protein sequences in Entrez. Entrez's global query interface can be accessed at http://
Autor:
Anna R. Panchenko, Saikat Chakrabarti, Christopher J. Lanczycki, Teresa M. Przytycka, Stephen H. Bryant, Paul A. Thiessen
Publikováno v:
Nucleic Acids Research
Accurate multiple sequence alignments of proteins are very important to several areas of computational biology and provide an understanding of phylogenetic history of domain families, their identification and classification. This article presents a n