ArticleCell2016
Structured States of Disordered Proteins from Genomic Sequences.
Article in Cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers, 1 of them a synthesis that pooled it.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
69 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Systematic review and meta-analysis of human transcriptomics reveals neuroinflammation, deficient energy metabolism, and proteostasis failure across neurodegeneration.Neurobiology of disease · 2021Pooled it
- Memorization bias impacts modeling of alternative conformational states of solute carrier membrane proteins with methods from deep learning.PLoS computational biology · 2025Article
- Prevalence of loss-of-function, gain-of-function and dominant-negative mechanisms across genetic disease phenotypes.Nature communications · 2025Article
- Memorization Bias Impacts Modeling of Alternative Conformational States of Symmetric Solute Carrier Membrane Proteins with Methods from Deep Learning.bioRxiv : the preprint server for biology · 2025Article
- AlphaFold2's training set powers its predictions of some fold-switched conformations.Protein science : a publication of the Protein Society · 2025Article
- Prediction of Disordered Linear Interacting Peptides with CLIP.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Simultaneous enhancement of multiple functional properties using evolution-informed protein design.Nature communications · 2024Article
- Map conformational landscapes of intrinsically disordered proteins with polymer physics quantities.Biophysical journal · 2024Article
- The molecular basis for cellular function of intrinsically disordered protein regions.Nature reviews. Molecular cell biology · 2024Review
- Machine-learning-based methods to generate conformational ensembles of disordered proteins.Biophysical journal · 2024Article
- Systematic identification of conditionally folded intrinsically disordered regions by AlphaFold2.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Co-evolution-based prediction of metal-binding sites in proteomes by machine learning.Nature chemical biology · 2023Article
- DeMAG predicts the effects of variants in clinically actionable genes by integrating structural and evolutionary epistatic features.Nature communications · 2023Article
- Compensatory relationship between low-complexity regions and gene paralogy in the evolution of prokaryotes.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Binding stoichiometry and structural model of the HIV-1 Rev/importin β complex.Life science alliance · 2022Article
- VIVID: A Web Application for Variant Interpretation and Visualization in Multi-dimensional Analyses.Molecular biology and evolution · 2022Article
- A combined evolutionary and structural approach to disclose the primary structural determinants essential for proneurotrophins biological functions.Computational and structural biotechnology journal · 2021Article
- Toward Characterising the Cellular 3D-Proteome.Frontiers in bioinformatics · 2021Article
- αβDCA method identifies unspecific binding but specific disruption of the group I intron by the StpA chaperone.RNA (New York, N.Y.) · 2020Article
- Article
9 more citing papers are in PubMed but not listed here.
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Authors and funding
7 authors.
Funding
Abstract
Protein flexibility ranges from simple hinge movements to functional disorder. Around half of all human proteins contain apparently disordered regions with little 3D or functional information, and many of these proteins are associated with disease. Building on the evolutionary couplings approach previously successful in predicting 3D states of ordered proteins and RNA, we developed a method to predict the potential for ordered states for all apparently disordered proteins with sufficiently rich evolutionary information. The approach is highly accurate (79%) for residue interactions as tested in more than 60 known disordered regions captured in a bound or specific condition. Assessing the potential for structure of more than 1,000 apparently disordered regions of human proteins reveals a continuum of structural order with at least 50% with clear propensity for three- or two-dimensional states. Co-evolutionary constraints reveal hitherto unseen structures of functional importance in apparently disordered proteins.
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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 OpenQuestion graph.