ArticleBioinformatics (Oxford, England)2018
DIBS: a repository of disordered binding sites mediating interactions with ordered proteins.
Article in Bioinformatics (Oxford, England), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.
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Who cites it
61 citing papers in PubMed.
- Beyond the structure-function paradigm: A comprehensive review of intrinsically disordered proteins.Biochemistry and biophysics reports · 2026Review
- 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
- IDBSpred: An intrinsically disordered binding site predictor using machine learning and protein language model.bioRxiv : the preprint server for biology · 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
- Expanding the Landscape of Amyloid Sequences with CARs-DB: A Database of Polar Amyloidogenic Peptides from Disordered Proteins.Methods in molecular biology (Clifton, N.J.) · 2024Article
- 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
- Minimum information guidelines for experiments structurally characterizing intrinsically disordered protein regions.Nature methods · 2023Review
- Classification of proteins inducing liquid-liquid phase separation: sequential, structural and functional characterization.Journal of biochemistry · 2023Article
- Biophysical and Integrative Characterization of Protein Intrinsic Disorder as a Prime Target for Drug Discovery.Biomolecules · 2023Review
- Computational Prediction of Protein Intrinsically Disordered Region Related Interactions and Functions.Genes · 2023Review
- How AlphaFold2 Predicts Conditionally Folding Regions Annotated in an Intrinsically Disordered Protein Database, IDEAL.Biology · 2023Article
- Molecular Dynamics Simulation as a Tool to Identify Mutual Synergistic Folding Proteins.International journal of molecular sciences · 2023Article
1 more citing papers are in PubMed but not listed here.
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6 authors.
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Abstract
Motivation: Intrinsically Disordered Proteins (IDPs) mediate crucial protein-protein interactions, most notably in signaling and regulation. As their importance is increasingly recognized, the detailed analyses of specific IDP interactions opened up new opportunities for therapeutic targeting. Yet, large scale information about IDP-mediated interactions in structural and functional details are lacking, hindering the understanding of the mechanisms underlying this distinct binding mode. Results: Here, we present DIBS, the first comprehensive, curated collection of complexes between IDPs and ordered proteins. DIBS not only describes by far the highest number of cases, it also provides the dissociation constants of their interactions, as well as the description of potential post-translational modifications modulating the binding strength and linear motifs involved in the binding. Together with the wide range of structural and functional annotations, DIBS will provide the cornerstone for structural and functional studies of IDP complexes. Availability and implementation: DIBS is freely accessible at http://dibs.enzim.ttk.mta.hu/. The DIBS 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: dosztanyi@caesar.elte.hu or bmeszaros@caesar.elte.hu. Supplementary information: Supplementary data are available at Bioinformatics online.
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