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Cited by 322

The DOI matches its Crossref record; 102 of the 102 references it cites were found in a registry or an index.

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

Open access
Pieper, Ursula, Webb, Benjamin M., Dong, Guang Qiang, Schneidman-Duhovny, Dina, Fan, Hao, Kim, Seung Joong, Khuri, Natalia, Spill, Yannick G., Weinkam, Patrick, Hammel, Michal, Tainer, John A., Nilges, Michael, Sali, Andrej·2014·Nucleic Acids Research

Abstract

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 almost 30 million reliable models for domains in 4.7 million unique protein sequences. ModBase allows users to compute or update comparative models on demand, through an interface to the ModWeb modeling server (http://salilab.org/modweb). ModBase models are also available through the Protein Model Portal (http://www.proteinmodelportal.org/). Recently developed associated resources include the AllosMod server for modeling ligand-induced protein dynamics (http://salilab.org/allosmod), the AllosMod-FoXS server for predicting a structural ensemble that fits an SAXS profile (http://salilab.org/allosmod-foxs), the FoXSDock server for protein–protein docking filtered by an SAXS profile (http://salilab.org/foxsdock), the SAXS Merge server for automatic merging of SAXS profiles (http://salilab.org/saxsmerge) and the Pose & Rank server for scoring protein–ligand complexes (http://salilab.org/poseandrank). In this update, we also highlight two applications of ModBase: a PSI:Biology initiative to maximize the structural coverage of the human alpha-helical transmembrane proteome and a determination of structural determinants of human immunodeficiency virus-1 protease specificity.

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Crossref · 10.1093/nar/gkt1144

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Metadata

Authors
Pieper, U., Webb, B. M., Dong, G. Q., Schneidman-Duhovny, D., Fan, H., Kim, S. J., Khuri, N., Spill, Y. G., Weinkam, P., Hammel, M., Tainer, J. A., Nilges, M., & Sali, A.
Venue
Nucleic Acids Research
Published
2013-11-23
Volume
42
Issue
D1
Pages
D336-D346
ISSN
  • 0305-1048 (ISSN-L)
  • 1362-4962
OpenAlex
W4295888250
Cited by
322
References
102
FWCI
8.88
Type
journal article
Language
en
Open access
gold

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CoChat. (2026). Citation check: ModBase, a database of annotated comparative protein structure models and associated resources. https://app.cochat.ai/papers/10.1093/nar/gkt1144
The paper
Pieper, U., Webb, B. M., Dong, G. Q., Schneidman-Duhovny, D., Fan, H., Kim, S. J., Khuri, N., Spill, Y. G., Weinkam, P., Hammel, M., Tainer, J. A., Nilges, M., & Sali, A. (2014). ModBase, a database of annotated comparative protein structure models and associated resources. Nucleic Acids Research. https://doi.org/10.1093/nar/gkt1144

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.