ArticleThe FEBS journal2017
The dock-and-coalesce mechanism for the association of a WASP disordered region with the Cdc42 GTPase.
Article in The FEBS journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
What it found
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Who cites it
14 citing papers in PubMed, 31 citations in OpenAlex.
- Hierarchical folding-upon-binding of an intrinsically disordered protein.Nature communications · 2025Article
- An electrostatic network with strong connectivity is a phospho-sensor for regulating affinity of Syk-receptor association.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Atomistic molecular dynamics simulations of intrinsically disordered proteins.Current opinion in structural biology · 2025Review
- 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
- Kinetic Methods of Deducing Binding Mechanisms Involving Intrinsically Disordered Proteins.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Sequence-Dependent Correlated Segments in the Intrinsically Disordered Region of ChiZ.Biomolecules · 2020Article
- Templated folding of intrinsically disordered proteins.The Journal of biological chemistry · 2020Review
- Brownian Dynamics Simulations of Biological Molecules.Trends in chemistry · 2019Article
- Features of molecular recognition of intrinsically disordered proteins via coupled folding and binding.Protein science : a publication of the Protein Society · 2019Review
- Designed Mutations Alter the Binding Pathways of an Intrinsically Disordered Protein.Scientific reports · 2019Article
- Bond swapping from a charge cloud allows flexible coordination of upstream signals through WASP: Multiple regulatory roles for the WASP basic region.The Journal of biological chemistry · 2018Article
- Unified understanding of folding and binding mechanisms of globular and intrinsically disordered proteins.Biophysical reviews · 2018Review
- Electrostatic Interactions in Protein Structure, Folding, Binding, and Condensation.Chemical reviews · 2018Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Intrinsically disordered proteins (IDPs) play key roles in signaling and regulation. Many IDPs undergo folding upon binding to their targets. We have proposed that coupled folding and binding of IDPs generally follow a dock-and-coalesce mechanism, whereby a segment of the IDP, through diffusion, docks to its cognate subsite and, subsequently, the remaining segments coalesce around their subsites. Here, by a combination of experiment and computation, we determined the precise form of dock-and-coalesce operating in the association between the intrinsically disordered GTPase-binding domain (GBD) of the Wiskott-Aldrich Syndrome protein and the Cdc42 GTPase. The association rate constants (k
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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.