ArticleBioinformatics (Oxford, England)2017
MFIB: a repository of protein complexes with mutual folding induced by binding.
Article in Bioinformatics (Oxford, England), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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51 citing papers in PubMed.
- Predicting molecular recognition features in protein sequences with MoRFchibi 2.0.BMC bioinformatics · 2026Article
- Pathogenic variations illuminate functional constraints in intrinsically disordered proteins.iScience · 2026Article
- Modern resources for intrinsic disorder predictions: protein language models, deep learning, meta-servers, and databases.Cellular and molecular life sciences : CMLS · 2026Review
- A deep learning method for predicting interactions for intrinsically disordered regions of proteins.bioRxiv : the preprint server for biology · 2025Article
- Article
- StrIDR: a database of intrinsically disordered regions of proteins with experimentally resolved structures.bioRxiv : the preprint server for biology · 2024Article
- AIUPred: combining energy estimation with deep learning for the enhanced prediction of protein disorder.Nucleic acids research · 2024Article
- Protein embeddings predict binding residues in disordered regions.Scientific reports · 2024Article
- Advanced computational approaches to understand protein aggregation.Biophysics reviews · 2024Review
- Tutorial: a guide for the selection of fast and accurate computational tools for the prediction of intrinsic disorder in proteins.Nature protocols · 2023Review
- Systematic identification of conditionally folded intrinsically disordered regions by AlphaFold2.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Computational Prediction of Protein Intrinsically Disordered Region Related Interactions and Functions.Genes · 2023Review
- Molecular Dynamics Simulation as a Tool to Identify Mutual Synergistic Folding Proteins.International journal of molecular sciences · 2023Article
- MobiDB: 10 years of intrinsically disordered proteins.Nucleic acids research · 2023Article
- DisCanVis: Visualizing integrated structural and functional annotations to better understand the effect of cancer mutations located within disordered proteins.Protein science : a publication of the Protein Society · 2023Article
- IDPsBind: a repository of binding sites for intrinsically disordered proteins complexes with known 3D structures.BMC molecular and cell biology · 2022Article
- Genetic variation associated with condensate dysregulation in disease.Developmental cell · 2022Article
- Compositional Bias of Intrinsically Disordered Proteins and Regions and Their Predictions.Biomolecules · 2022Article
- Characterization of intrinsically disordered regions in proteins informed by human genetic diversity.PLoS computational biology · 2022Article
- Databases for intrinsically disordered proteins.Acta crystallographica. Section D, Structural biology · 2022Review
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4 authors.
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No grant is acknowledged in the PubMed record.
Abstract
motivationIt is commonplace that intrinsically disordered proteins (IDPs) are involved in crucial interactions in the living cell. However, the study of protein complexes formed exclusively by IDPs is hindered by the lack of data and such analyses remain sporadic. Systematic studies benefited other types of protein-protein interactions paving a way from basic science to therapeutics; yet these efforts require reliable datasets that are currently lacking for synergistically folding complexes of IDPs.
resultsHere we present the Mutual Folding Induced by Binding (MFIB) database, the first systematic collection of complexes formed exclusively by IDPs. MFIB contains an order of magnitude more data than any dataset used in corresponding studies and offers a wide coverage of known IDP complexes in terms of flexibility, oligomeric composition and protein function from all domains of life. The included complexes are grouped using a hierarchical classification and are complemented with structural and functional annotations. MFIB is backed by a firm development team and infrastructure, and together with possible future community collaboration it will provide the cornerstone for structural and functional studies of IDP complexes. AVAILABILITY AND IMPLEMENTATION: MFIB is freely accessible at http://mfib.enzim.ttk.mta.hu/. The MFIB application is hosted by Apache web server and was implemented in PHP. To enrich querying features and to enhance backend performance a MySQL database was also created. CONTACT: simon.istvan@ttk.mta.hu, meszaros.balint@ttk.mta.hu. SUPPLEMENTARY INFORMATION: Supplementary data are available at Bioinformatics online.
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