ArticleScientific reports2019
Designed Mutations Alter the Binding Pathways of an Intrinsically Disordered Protein.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Alternative Splicing of a Structured Partner Alters the Folding-Upon-Binding Trajectory of an Intrinsically Disordered Protein.Journal of the American Chemical Society · 2026Article
- Electrical Forces Improve Memory in Old Age.Reviews of physiology, biochemistry and pharmacology · 2025Review
- The Chlamydia pneumoniae effector SemD exploits its host's endocytic machinery by structural and functional mimicry.Nature communications · 2024Article
- Why Does Synergistic Activation of WASP, but Not N-WASP, by Cdc42 and PIPJournal of molecular biology · 2023Article
- N-WASP is competent for downstream signaling before full release from autoinhibition.The Journal of chemical physics · 2023Article
- Sequence-Dependent Backbone Dynamics of Intrinsically Disordered Proteins.Journal of chemical theory and computation · 2022Article
- The dynamic properties of a nuclear coactivator binding domain are evolutionarily conserved.Communications biology · 2022Article
- Introducing intrinsic disorder reduces electrostatic steering in protein-protein interactions.Biophysical journal · 2021Article
- Molecular Details of a Coupled Binding and Folding Reaction between the Amyloid Precursor Protein and a Folded Domain.ACS chemical biology · 2021Article
- Mapping the transition state for a binding reaction between ancient intrinsically disordered proteins.The Journal of biological chemistry · 2020Article
- Revealing the Hidden Sensitivity of Intrinsically Disordered Proteins to their Chemical Environment.The journal of physical chemistry letters · 2020Article
- Disordered proteins follow diverse transition paths as they fold and bind to a partner.Science (New York, N.Y.) · 2020Article
- Measuring the affinity of protein-protein interactions on a single-molecule level by mass photometry.Analytical biochemistry · 2020Article
- Features of molecular recognition of intrinsically disordered proteins via coupled folding and binding.Protein science : a publication of the Protein Society · 2019Review
- Intrinsically Disordered Transactivation Domains Bind to TAZ1 Domain of CBP via Diverse Mechanisms.Biophysical journal · 2019Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Many cellular functions, including signaling and regulation, are carried out by intrinsically disordered proteins (IDPs) binding to their targets. Experimental and computational studies have now significantly advanced our understanding of these binding processes. In particular, IDPs that become structured upon binding typically follow a dock-and-coalesce mechanism, whereby the docking of one IDP segment initiates the process, followed by on-target coalescence of remaining IDP segments. Multiple dock-and-coalesce pathways may exist, but one may dominate, by relying on electrostatic attraction and molecular flexibility for fast docking and fast coalescing, respectively. Here we critically test this mechanistic understanding by designing mutations that alter the dominant pathway. This achievement marks an important step toward precisely manipulating IDP functions.
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