Zobrazeno 1 - 5
of 5
pro vyhledávání: '"John J. Salama"'
Autor:
R. Farrall, K. Zheng, S. Sgro, G. Pintilie, Ken Bantoft, C. D'Abreo, Christopher W. V. Hogue, Ivan Ng, R. Yao, Michelle White, D. Dorairajoo, J. Moniakis, S. Tao, Brenda Muskat, D. Skinner, Martha Bajec, Susan Moore, R. Stasiuk, K. Anthony, C. E. Andrade, Ian Donaldson, R. Pirone, Kelly Boutilier, M. R. Dumontier, S. Wong, Ruth Isserlin, R. Willis, J. P. Paraiso, Brigitte Tuekam, A. Wrong, S. Konopinsky, F. Jack, M. Magidin, T. Kon, L. Hurrell, San Ling, E. Burgess, A. Hrvojic, Cheryl Wolting, R. Gonzaga, T. Shan, Kevin A. Snyder, V. Grytsan, E. Haldorsen, Howard J. Feldman, E. Garderman, D. Strumpf, Tony Pawson, Neil Bahroos, V. Gu, Michel Dumontier, Doron Betel, John J. Salama, Z. Wang, C. Alfarano, Benjamin Ouellette, V. Earles, Belinda S. Parker, Robin Haw, Eunjung Lee, E. Gryz, V. Le, Y. Gong, K. Buzadzija, J. Siew, R. Cavero, S. Zhang, J. Montojo, B. Yates, Y. Shu, A. Halupa, F. Juma, C. Xin, Asim Khan, B. Bobechko
Publikováno v:
Nucleic Acids Research, 33, D418-D424. Oxford University Press
Nucleic Acids Research
Nucleic Acids Research
The Biomolecular Interaction Network Database (BIND) (http://bind.ca) archives biomolecular interaction, reaction, complex and pathway information. Our aim is to curate the details about molecular interactions that arise from published experimental r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1798e4750fe350843e3f196b0bc0dd94
https://doi.org/10.1093/nar/gki051
https://doi.org/10.1093/nar/gki051
Publikováno v:
Biopolymers. 61:111-120
Software to automate the process of extracting molecular interactions from three- dimensional (3D) structures has been developed that records these as Biomolecular Interaction Network Database (BIND) pairwise interaction records. Full annotation of B
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ae5e20f6d0fc541231d94c45986e606d
https://doi.org/10.1002/1097-0282(2001/2002)61:2<111::aid-bip10143>3.0.co
https://doi.org/10.1002/1097-0282(2001/2002)61:2<111::aid-bip10143>3.0.co
Autor:
John Armstrong, Susan Moore, Antony F. Quinn, John J. Salama, Jason Nerothin, Arnaud Ceol, Christopher W. V. Hogue, Ioannis Xenarios, Sandra Orchard, Nisha Vinod, Rolf Apweiler, Michael E. Cusick, Ethan Cerami, Marc Vidal, David James Sherman, Peter Woollard, Luisa Montecchi-Palazzi, Matthias Oesterheld, Andrew Chatr-aryamontri, Volker Stümpflen, Gianni Cesareni, Mike Tyers, Bruno Aranda, Samuel Kerrien, David Eisenberg, Michael K. Gilson, Henning Hermjakob, Jérôme Wojcik, Lukasz Salwinski, Gary D. Bader
Publikováno v:
BMC Biology
BMC Biol. 5:44 (2007)
BMC Biology, vol. 5, pp. 44
BMC Biology, Vol 5, Iss 1, p 44 (2007)
BMC Biol. 5:44 (2007)
BMC Biology, vol. 5, pp. 44
BMC Biology, Vol 5, Iss 1, p 44 (2007)
Background Molecular interaction Information is a key resource in modern biomedical research. Publicly available data have previously been provided in a broad array of diverse formats, making access to this very difficult. The publication and wide im
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::78285247762be556b150bccce43ccb4e
http://hdl.handle.net/2108/35427
http://hdl.handle.net/2108/35427
Autor:
Kevin A. Snyder, John J. Salama, Christopher W. V. Hogue, Howard J. Feldman, Michel Dumontier
Publikováno v:
BMC Bioinformatics, 7. BioMed Central Ltd
BMC Bioinformatics
BMC Bioinformatics, Vol 7, Iss 1, p 152 (2006)
BMC Bioinformatics
BMC Bioinformatics, Vol 7, Iss 1, p 152 (2006)
Background Accurate small molecule binding site information for a protein can facilitate studies in drug docking, drug discovery and function prediction, but small molecule binding site protein sequence annotation is sparse. The Small Molecule Intera
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f2e8035b4d4f5a9842a157100860c2f8
https://cris.maastrichtuniversity.nl/en/publications/6b15453a-798a-48e3-9b56-88a08b391f4c
https://cris.maastrichtuniversity.nl/en/publications/6b15453a-798a-48e3-9b56-88a08b391f4c
Publikováno v:
Bioinformatics (Oxford, England). 17(9)
Summary: VISTRAJ is an application which allows 3D visualization, manipulation and editing of protein conformational space using probabilistic maps of this space called ‘trajectory distributions’. Trajectory distributions serve as input to FOLDTR
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5967f49beafbb70efcc644b0fed94ebc
https://pubmed.ncbi.nlm.nih.gov/11590106
https://pubmed.ncbi.nlm.nih.gov/11590106