ReviewIntrinsically disordered proteins
Transient disorder: Calcineurin as an example.
Review in Intrinsically disordered proteins. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- New variants and genotype-phenotype correlation ofFrontiers in neuroscience · 2025Article
- DNA facilitates heterodimerization between human transcription factors FoxP1 and FoxP2 by increasing their conformational flexibility.iScience · 2023Article
- The protein disorder cycle.Biophysical reviews · 2021Review
- A functionally divergent intrinsically disordered region underlying the conservation of stochastic signaling.PLoS genetics · 2021Article
- Calcineurin.Cell communication and signaling : CCS · 2020Review
- Life in Phases: Intra- and Inter- Molecular Phase Transitions in Protein Solutions.Biomolecules · 2019Review
- Novel calcineurin A (PPP3CA) variant associated with epilepsy, constitutive enzyme activation and downregulation of protein expression.European journal of human genetics : EJHG · 2019Article
- Calcium-Binding Proteins with Disordered Structure and Their Role in Secretion, Storage, and Cellular Signaling.Biomolecules · 2018Review
- Calcineurin in a Crowded World.Biochemistry · 2016Article
- Dancing Protein Clouds: The Strange Biology and Chaotic Physics of Intrinsically Disordered Proteins.The Journal of biological chemistry · 2016Review
- Digested disorder: Quarterly intrinsic disorder digest (July-August-September, 2013).Intrinsically disordered proteins · 2014Review
- Disorder in the lifetime of a protein.Intrinsically disordered proteinsArticle
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Authors and funding
1 author.
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Abstract
How intrinsically disordered proteins and regions evade degradation by cellular machinery evolved to recognize unfolded and misfolded chains remains a vexing question. One potential means by which this can occur is the disorder is transient in nature. That is, the disorder exists just long enough for it to be bound by a partner biomolecule and fold. A review of 30 y of studies of calmodulin's activation of calcineurin suggests that the regulatory domain of this vital phosphatase is a transiently disordered region. During activation, the regulatory domain progresses from a folded state, to disordered, followed by folding upon being bound by calmodulin. The transient disordered state of this domain is part of a critical intermediate state that facilitates the rapid binding of calmodulin. Building upon "fly-casting" as a means of facilitating partner binding, the mechanism by which calcineurin undergoes activation and subsequent deactivation could be considered "catch and release."
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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.