ArticleBioinformatics (Oxford, England)2015
DISOPRED3: precise disordered region predictions with annotated protein-binding activity.
Article in Bioinformatics (Oxford, England), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 518 papers, 2 of them syntheses that pooled it.
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Who cites it
518 citing papers in PubMed, 2 syntheses or guidelines pooled it.
- Mapping protein states and interactions across the tree of life with co-fractionation mass spectrometry.Nature communications · 2023Pooled it
- Shift of the insoluble content of the proteome in the aging mouse brain.Proceedings of the National Academy of Sciences of the United States of America · 2023Pooled it
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- Beyond the structure-function paradigm: A comprehensive review of intrinsically disordered proteins.Biochemistry and biophysics reports · 2026Review
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- Structure and molecular function of the BCL7 proteins.Biochemical Society transactions · 2026Review
- Predicting molecular recognition features in protein sequences with MoRFchibi 2.0.BMC bioinformatics · 2026Article
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- In Search of Shape in the Unshaped: Constructing Ensembles of Intrinsically Disordered Proteins.Biophysics reviews · 2026Article
- Regulation of the histone H3K36 methyltransferase Set2 by the histone chaperone Spt6.bioRxiv : the preprint server for biology · 2026Article
- FuzDrop: sequence-based prediction of the propensity of proteins for liquid-liquid phase separation and aggregation.Nature protocols · 2026Review
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- IDBSpred: An intrinsically disordered binding site predictor using machine learning and protein language model.bioRxiv : the preprint server for biology · 2026Article
- CBP-IDRs regulate acetylation and gene expression.Cell reports · 2026Article
458 more citing papers are in PubMed but not listed here.
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Authors and funding
2 authors.
Funding
Abstract
motivationA sizeable fraction of eukaryotic proteins contain intrinsically disordered regions (IDRs), which act in unfolded states or by undergoing transitions between structured and unstructured conformations. Over time, sequence-based classifiers of IDRs have become fairly accurate and currently a major challenge is linking IDRs to their biological roles from the molecular to the systems level.
resultsWe describe DISOPRED3, which extends its predecessor with new modules to predict IDRs and protein-binding sites within them. Based on recent CASP evaluation results, DISOPRED3 can be regarded as state of the art in the identification of IDRs, and our self-assessment shows that it significantly improves over DISOPRED2 because its predictions are more specific across the whole board and more sensitive to IDRs longer than 20 amino acids. Predicted IDRs are annotated as protein binding through a novel SVM based classifier, which uses profile data and additional sequence-derived features. Based on benchmarking experiments with full cross-validation, we show that this predictor generates precise assignments of disordered protein binding regions and that it compares well with other publicly available tools.
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