ReviewJournal of biosciences2020
Dynamic conformational flexibility and molecular interactions of intrinsically disordered proteins.
Review in Journal of biosciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- GeoPep: A Geometry-Aware Masked Language Model for Protein-Peptide Binding Site Prediction.Journal of chemical information and modeling · 2026Article
- Correlated Evolution Drives Structural Convergence of Interacting Proteins.Journal of molecular evolution · 2026Article
- Role of Charge Patterning and Hydrophobicity in Peptide-Based Complex Coacervates.Biomacromolecules · 2025Article
- Second-order allosteric control as a mechanism for compensatory mutations in B-cell translocation gene 2.Protein science : a publication of the Protein Society · 2025Article
- Uncovering protein conformational dynamics within two-component viral biomolecular condensates.Protein science : a publication of the Protein Society · 2025Article
- Integrating chemical artificial intelligence and cognitive computing for predictive analysis of biological pathways: a case for intrinsically disordered proteins.Biophysical reviews · 2025Review
- Conservation of OFD1 Protein Motifs: Implications for Discovery of Novel Interactors and the OFD1 Function.International journal of molecular sciences · 2025Article
- Genome-Wide Characterization of Wholly Disordered Proteins inInternational journal of molecular sciences · 2025Article
- Article
- Development of a Cell-Based AlphaLISA Assay for High-Throughput Screening for Small Molecule Proteasome Modulators.ACS omega · 2023Article
- The Role of Intrinsically Disordered Proteins in Liquid-Liquid Phase Separation during Calcium Carbonate Biomineralization.Biomolecules · 2022Review
- Evolving Experimental Techniques for Structure-Based Drug Design.The journal of physical chemistry. B · 2022Review
- Functions and Mechanisms of Pro-Lysyl Oxidase Processing in Cancers and Eye Pathologies with a Focus on Diabetic Retinopathy.International journal of molecular sciences · 2022Review
- Immunoinformatic analysis of the whole proteome for vaccine design: An application toFrontiers in immunology · 2022Article
- Molecular Mechanisms Regulating the DNA Repair Protein APE1: A Focus on Its Flexible N-Terminal Tail Domain.International journal of molecular sciences · 2021Review
- The Multifaceted Nature of Nucleobindin-2 in Carcinogenesis.International journal of molecular sciences · 2021Review
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Intrinsically disordered proteins (IDPs) are highly flexible and undergo disorder to order transition upon binding. They are highly abundant in human proteomes and play critical roles in cell signaling and regulatory processes. This review mainly focuses on the dynamics of disordered proteins including their conformational heterogeneity, protein-protein interactions, and the phase transition of biomolecular condensates that are central to various biological functions. Besides, the role of RNA-mediated chaperones in protein folding and stability of IDPs were also discussed. Finally, we explored the dynamic binding interface of IDPs as novel therapeutic targets and the effect of small molecules on their interactions.
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Registered trials
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.