ArticleInternational journal of molecular sciences2020
Experimentally Determined Long Intrinsically Disordered Protein Regions Are Now Abundant in the Protein Data Bank.
Article in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- Intrinsic Disorder as a New Frontier in Antimicrobial Resistance and Bacterial Fitness.MicrobiologyOpen · 2026Review
- Intrinsically disordered regions in the NLRP family of receptors act as regulatory hubs for inflammasome condensation and activation.Frontiers in immunology · 2026Article
- Expose flexible conformations for intrinsically disordered protein.Current research in structural biology · 2025Article
- Targeting protein disorder: the next hurdle in drug discovery.Nature reviews. Drug discovery · 2025Review
- Regularly updated benchmark sets for statistically correct evaluations of AlphaFold applications.Briefings in bioinformatics · 2025Article
- Advanced computational approaches to understand protein aggregation.Biophysics reviews · 2024Review
- The structural landscape and diversity of Pyricularia oryzae MAX effectors revisited.PLoS pathogens · 2024Article
- The impact of genetically controlled splicing on exon inclusion and protein structure.PloS one · 2024Article
- Prediction of folding patterns for intrinsic disordered protein.Scientific reports · 2023Article
- The Origin of Discrepancies between Predictions and Annotations in Intrinsically Disordered Proteins.Biomolecules · 2023Article
- Computational Prediction of Protein Intrinsically Disordered Region Related Interactions and Functions.Genes · 2023Review
- Intrinsically Disordered Proteins: An Overview.International journal of molecular sciences · 2022Review
- Modeling the Dynamics of Protein-Protein Interfaces, How and Why?Molecules (Basel, Switzerland) · 2022Review
- Databases for intrinsically disordered proteins.Acta crystallographica. Section D, Structural biology · 2022Review
- Prediction of protein-protein interaction sites in intrinsically disordered proteins.Frontiers in molecular biosciences · 2022Review
- Intrinsically disordered signaling proteins: Essential hub players in the control of stress responses in Saccharomyces cerevisiae.PloS one · 2022Article
- Origin of Increased Solvent Accessibility of Peptide Bonds in Mutual Synergetic Folding Proteins.International journal of molecular sciences · 2021Article
- The protein disorder cycle.Biophysical reviews · 2021Review
- Bioinformatic Analysis of Lytic Polysaccharide Monooxygenases Reveals the Pan-Families Occurrence of Intrinsically Disordered C-Terminal Extensions.Biomolecules · 2021Article
- When Order Meets Disorder: Modeling and Function of the Protein Interface in Fuzzy Complexes.Biomolecules · 2021Review
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
Intrinsically disordered protein regions are commonly defined from missing electron density in X-ray structures. Experimental evidence for long disorder regions (LDRs) of at least 30 residues was so far limited to manually curated proteins. Here, we describe a comprehensive and large-scale analysis of experimental LDRs for 3133 unique proteins, demonstrating an increasing coverage of intrinsic disorder in the Protein Data Bank (PDB) in the last decade. The results suggest that long missing residue regions are a good quality source to annotate intrinsically disordered regions and perform functional analysis in large data sets. The consensus approach used to define LDRs allows to evaluate context dependent disorder and provide a common definition at the protein level.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.