Zobrazeno 1 - 10
of 25
pro vyhledávání: '"Jessica H. Fong"'
Autor:
Jessica H. Fong, Martin Strauss
Publikováno v:
Discrete Mathematics & Theoretical Computer Science, Vol 4, Iss 2 (2001)
Several recent papers have shown how to approximate the difference ∑ i |a i-b i | or ∑|a i-b i | 2 between two functions, when the function values a i and b i are given in a data stream, and their order is chosen by an adversary. These algorithms
Externí odkaz:
https://doaj.org/article/3f8d39d557894d72b878ec9c2d399220
Autor:
Jessica H. Fong, Martin Strauss
Publikováno v:
Discrete Mathematics & Theoretical Computer Science, Vol Vol. 4 no. 2 (2001)
Several recent papers have shown how to approximate the difference ∑ _i|a_i-b_i| or ∑ |a_i-b_i|^2 between two functions, when the function values a_i and b_i are given in a data stream, and their order is chosen by an adversary. These algorithms
Externí odkaz:
https://doaj.org/article/80cefe586df543a985f0db103c711921
Autor:
Jessica H Fong, Benjamin A Shoemaker, Sergiy O Garbuzynskiy, Michail Y Lobanov, Oxana V Galzitskaya, Anna R Panchenko
Publikováno v:
PLoS Computational Biology, Vol 5, Iss 3, p e1000316 (2009)
We perform a large-scale study of intrinsically disordered regions in proteins and protein complexes using a non-redundant set of hundreds of different protein complexes. In accordance with the conventional view that folding and binding are coupled,
Externí odkaz:
https://doaj.org/article/fae7624c2cf143aab5955ba489bf4a81
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::55c7b3856edd6e76b2dd8f1f3735eb83
https://doi.org/10.1093/nar/gkr997
https://doi.org/10.1093/nar/gkr997
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d29ecd5a142c81cda012cb91e5a433f2
http://europepmc.org/articles/PMC3245041
http://europepmc.org/articles/PMC3245041
Autor:
Ruth Nussinov, Anna R. Panchenko, Teresa M. Przytycka, Inbar Cohen-Gihon, Jessica H. Fong, Roded Sharan
Publikováno v:
Mol. BioSyst.. 7:784-792
Most eukaryotic proteins are composed of two or more domains. These assemble in a modular manner to create new proteins usually by the acquisition of one or more domains to an existing protein. Promiscuous domains which are found embedded in a variet
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f71f7da6208a02cde6c2477f5d62a10d
https://doi.org/10.1039/c0mb00182a
https://doi.org/10.1039/c0mb00182a
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4f2c026177984fae9f84c055b453ce27
http://europepmc.org/articles/PMC3013737
http://europepmc.org/articles/PMC3013737
Autor:
Thomas Madej, Manoj Tyagi, Benjamin A. Shoemaker, Aron Marchler-Bauer, Dachuan Zhang, Stephen H. Bryant, Ratna R. Thangudu, Anna R. Panchenko, Jessica H. Fong
Publikováno v:
Nucleic Acids Research
IBIS is the NCBI Inferred Biomolecular Interaction Server. This server organizes, analyzes and predicts interaction partners and locations of binding sites in proteins. IBIS provides annotations for different types of binding partners (protein, chemi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2e24c67164220ef5b49a7050610c9c8b
https://doi.org/10.1093/nar/gkp842
https://doi.org/10.1093/nar/gkp842
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::488d1e0beb16392149316a39dcaa839f
https://doi.org/10.1093/nar/gkn845
https://doi.org/10.1093/nar/gkn845
Publikováno v:
Journal of Molecular Biology. 366:307-315
Domains are basic evolutionary units of proteins and most proteins have more than one domain. Advances in domain modeling and collection are making it possible to annotate a large fraction of known protein sequences by a linear ordering of their doma
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::de4af29e7a19268e08c21354fa98a262
https://doi.org/10.1016/j.jmb.2006.11.017
https://doi.org/10.1016/j.jmb.2006.11.017