Evidence map›Paper›PMID 29634920›Full record

ReviewJournal of molecular biology2018

Expanding the Paradigm: Intrinsically Disordered Proteins and Allosteric Regulation.

Rebecca B Berlow, H Jane Dyson, Peter E Wright

Abstract readReview
In one paragraph

Review in Journal of molecular biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.

0numbers the graph read from it
0cells of the map it votes in
77citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

77 citing papers in PubMed.

  1. Differential proteostasis imbalance and the molecular basis of distinct synucleinopathies and tauopathies.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026
    Review
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  15. Phosphorylation enables allosteric control of a viral condensate.bioRxiv : the preprint server for biology · 2025
    Article
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  17. Article
  18. Review
  19. Article
  20. Article

17 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors.

Rebecca B BerlowDepartment of Integrative Structural and Computational Biology and Skaggs Institute of Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
H Jane DysonDepartment of Integrative Structural and Computational Biology and Skaggs Institute of Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
Peter E WrightDepartment of Integrative Structural and Computational Biology and Skaggs Institute of Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA. Electronic address: wright@scripps.edu.

Funding

Structural basis for CBP/p300 transcriptional regulationR01CA096865 · NCI · SCRIPPS RESEARCH INSTITUTE, THE · PI WRIGHT, PETER EDWIN · 2002 to 2016
$6.2M
Molecular basis for regulation of CREB by cell stress and retroviral oncoproteinsR01CA214054 · NCI · SCRIPPS RESEARCH INSTITUTE, THE · PI DENIZ, ASHOK A, WRIGHT, PETER EDWIN · 2017 to 2021
$3.0M
Interactions between Hsp90, Co-chaperones and Client ProteinsR01GM113251 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI DYSON, HELEN JANE · 2015 to 2018
$1.5M
NCI NIH HHS R01 CA096865NCI NIH HHS R01 CA214054NIGMS NIH HHS R01 GM113251
6 · The paper itself

Abstract

Allosteric regulatory processes are implicated at all levels of biological function. Recent advances in our understanding of the diverse and functionally significant class of intrinsically disordered proteins have identified a multitude of ways in which disordered proteins function within the confines of the allosteric paradigm. Allostery within or mediated by intrinsically disordered proteins ensures robust and efficient signal integration through mechanisms that would be extremely unfavorable or even impossible for globular protein interaction partners. Here, we highlight recent examples that indicate the breadth of biological outcomes that can be achieved through allosteric regulation by intrinsically disordered proteins. Ongoing and future work in this rapidly evolving area of research will expand our appreciation of the central role of intrinsically disordered proteins in ensuring the fidelity and efficiency of cellular regulation.

Indexed as

Allosteric RegulationBinding SitesGene Expression RegulationHumansIntrinsically Disordered ProteinsModels, MolecularProtein ConformationProtein FoldingThermodynamicsIntrinsically Disordered Proteinsallosterypost-translational modificationprotein disorderprotein–protein interaction

Identifiers

PMID29634920
PMCPMC6045455

What OpenQuestion holds

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Registered trials

None linked

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.