Evidence map›Paper›PMID 26922996›Full record

ReviewChemical reviews2016

Dynamic Protein Interaction Networks and New Structural Paradigms in Signaling.

Veronika Csizmok, Ariele Viacava Follis, Richard W Kriwacki, Julie D Forman-Kay

Abstract readReview
In one paragraph

Review in Chemical reviews, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 104 papers.

0numbers the graph read from it
0cells of the map it votes in
104citing 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

104 citing papers in PubMed.

  1. Review
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  19. The Role of Uridine in Health and Disease.Journal of inflammation research · 2025
    Review
  20. Article

44 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

4 authors.

Veronika CsizmokMolecular Structure & Function, The Hospital for Sick Children , Toronto, ON M5G 0A4, Canada.
Ariele Viacava FollisDepartment of Structural Biology, St. Jude Children's Research Hospital , Memphis, Tennessee 38105, United States.
Richard W KriwackiDepartment of Structural Biology, St. Jude Children's Research Hospital , Memphis, Tennessee 38105, United States.
Julie D Forman-KayMolecular Structure & Function, The Hospital for Sick Children , Toronto, ON M5G 0A4, Canada.

Funding

Viral Vector Technology (VVTSR)P30CA021765 · NCI · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI CHARLES ROBERTS · 1985 to 2026
$166.9M
Structural Determinants in Cell Growth Control by p21 and p27R01CA082491 · NCI · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI KRIWACKI, RICHARD W · 2001 to 2011
$2.7M
The Molecular Basis of Liquid-like Structure of the NucleolusR01GM115634 · NIGMS · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI KRIWACKI, RICHARD W · 2015 to 2018
$1.8M
Understanding the Structural Mechanism of Puma-induced ApoptosisR01GM083159 · NIGMS · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI KRIWACKI, RICHARD W · 2009 to 2012
$1.3M
NCI NIH HHS P30 CA021765NCI NIH HHS R01 CA082491NIGMS NIH HHS R01 GM083159NIGMS NIH HHS R01 GM115634
6 · The paper itself

Abstract

Understanding signaling and other complex biological processes requires elucidating the critical roles of intrinsically disordered proteins (IDPs) and regions (IDRs), which represent ∼30% of the proteome and enable unique regulatory mechanisms. In this review, we describe the structural heterogeneity of disordered proteins that underpins these mechanisms and the latest progress in obtaining structural descriptions of conformational ensembles of disordered proteins that are needed for linking structure and dynamics to function. We describe the diverse interactions of IDPs that can have unusual characteristics such as "ultrasensitivity" and "regulated folding and unfolding". We also summarize the mounting data showing that large-scale assembly and protein phase separation occurs within a variety of signaling complexes and cellular structures. In addition, we discuss efforts to therapeutically target disordered proteins with small molecules. Overall, we interpret the remodeling of disordered state ensembles due to binding and post-translational modifications within an expanded framework for allostery that provides significant insights into how disordered proteins transmit biological information.

Indexed as

Allosteric RegulationIntrinsically Disordered ProteinsProtein FoldingProtein Interaction Domains and MotifsProtein Processing, Post-TranslationalProtein Structure, TertiaryProtein UnfoldingSignal TransductionSmall Molecule LibrariesIntrinsically Disordered ProteinsSmall Molecule Libraries

Identifiers

PMID26922996
PMCPMC5342629

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.