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ModBase, a database of annotated comparative protein structure models, and associated resources

ModBase (http://salilab.org/modbase) is a database of annotated comparative protein structure models. The models are calculated by ModPipe, an automated modeling pipeline that relies primarily on Modeller for fold assignment, sequence–structure alignment, model building and model assessment (http://...

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Autores principales: Pieper, Ursula, Webb, Benjamin M., Barkan, David T., Schneidman-Duhovny, Dina, Schlessinger, Avner, Braberg, Hannes, Yang, Zheng, Meng, Elaine C., Pettersen, Eric F., Huang, Conrad C., Datta, Ruchira S., Sampathkumar, Parthasarathy, Madhusudhan, Mallur S., Sjölander, Kimmen, Ferrin, Thomas E., Burley, Stephen K., Sali, Andrej
Formato: Texto
Lenguaje:English
Publicado: Oxford University Press 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3013688/
https://www.ncbi.nlm.nih.gov/pubmed/21097780
http://dx.doi.org/10.1093/nar/gkq1091
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author Pieper, Ursula
Webb, Benjamin M.
Barkan, David T.
Schneidman-Duhovny, Dina
Schlessinger, Avner
Braberg, Hannes
Yang, Zheng
Meng, Elaine C.
Pettersen, Eric F.
Huang, Conrad C.
Datta, Ruchira S.
Sampathkumar, Parthasarathy
Madhusudhan, Mallur S.
Sjölander, Kimmen
Ferrin, Thomas E.
Burley, Stephen K.
Sali, Andrej
author_facet Pieper, Ursula
Webb, Benjamin M.
Barkan, David T.
Schneidman-Duhovny, Dina
Schlessinger, Avner
Braberg, Hannes
Yang, Zheng
Meng, Elaine C.
Pettersen, Eric F.
Huang, Conrad C.
Datta, Ruchira S.
Sampathkumar, Parthasarathy
Madhusudhan, Mallur S.
Sjölander, Kimmen
Ferrin, Thomas E.
Burley, Stephen K.
Sali, Andrej
author_sort Pieper, Ursula
collection PubMed
description ModBase (http://salilab.org/modbase) is a database of annotated comparative protein structure models. The models are calculated by ModPipe, an automated modeling pipeline that relies primarily on Modeller for fold assignment, sequence–structure alignment, model building and model assessment (http://salilab.org/modeller/). ModBase currently contains 10 355 444 reliable models for domains in 2 421 920 unique protein sequences. ModBase allows users to update comparative models on demand, and request modeling of additional sequences through an interface to the ModWeb modeling server (http://salilab.org/modweb). ModBase models are available through the ModBase interface as well as the Protein Model Portal (http://www.proteinmodelportal.org/). Recently developed associated resources include the SALIGN server for multiple sequence and structure alignment (http://salilab.org/salign), the ModEval server for predicting the accuracy of protein structure models (http://salilab.org/modeval), the PCSS server for predicting which peptides bind to a given protein (http://salilab.org/pcss) and the FoXS server for calculating and fitting Small Angle X-ray Scattering profiles (http://salilab.org/foxs).
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spelling pubmed-30136882011-01-03 ModBase, a database of annotated comparative protein structure models, and associated resources Pieper, Ursula Webb, Benjamin M. Barkan, David T. Schneidman-Duhovny, Dina Schlessinger, Avner Braberg, Hannes Yang, Zheng Meng, Elaine C. Pettersen, Eric F. Huang, Conrad C. Datta, Ruchira S. Sampathkumar, Parthasarathy Madhusudhan, Mallur S. Sjölander, Kimmen Ferrin, Thomas E. Burley, Stephen K. Sali, Andrej Nucleic Acids Res Articles ModBase (http://salilab.org/modbase) is a database of annotated comparative protein structure models. The models are calculated by ModPipe, an automated modeling pipeline that relies primarily on Modeller for fold assignment, sequence–structure alignment, model building and model assessment (http://salilab.org/modeller/). ModBase currently contains 10 355 444 reliable models for domains in 2 421 920 unique protein sequences. ModBase allows users to update comparative models on demand, and request modeling of additional sequences through an interface to the ModWeb modeling server (http://salilab.org/modweb). ModBase models are available through the ModBase interface as well as the Protein Model Portal (http://www.proteinmodelportal.org/). Recently developed associated resources include the SALIGN server for multiple sequence and structure alignment (http://salilab.org/salign), the ModEval server for predicting the accuracy of protein structure models (http://salilab.org/modeval), the PCSS server for predicting which peptides bind to a given protein (http://salilab.org/pcss) and the FoXS server for calculating and fitting Small Angle X-ray Scattering profiles (http://salilab.org/foxs). Oxford University Press 2011-01 2010-11-19 /pmc/articles/PMC3013688/ /pubmed/21097780 http://dx.doi.org/10.1093/nar/gkq1091 Text en © The Author(s) 2010. Published by Oxford University Press. http://creativecommons.org/licenses/by-nc/2.5 This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.5), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Articles
Pieper, Ursula
Webb, Benjamin M.
Barkan, David T.
Schneidman-Duhovny, Dina
Schlessinger, Avner
Braberg, Hannes
Yang, Zheng
Meng, Elaine C.
Pettersen, Eric F.
Huang, Conrad C.
Datta, Ruchira S.
Sampathkumar, Parthasarathy
Madhusudhan, Mallur S.
Sjölander, Kimmen
Ferrin, Thomas E.
Burley, Stephen K.
Sali, Andrej
ModBase, a database of annotated comparative protein structure models, and associated resources
title ModBase, a database of annotated comparative protein structure models, and associated resources
title_full ModBase, a database of annotated comparative protein structure models, and associated resources
title_fullStr ModBase, a database of annotated comparative protein structure models, and associated resources
title_full_unstemmed ModBase, a database of annotated comparative protein structure models, and associated resources
title_short ModBase, a database of annotated comparative protein structure models, and associated resources
title_sort modbase, a database of annotated comparative protein structure models, and associated resources
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3013688/
https://www.ncbi.nlm.nih.gov/pubmed/21097780
http://dx.doi.org/10.1093/nar/gkq1091
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