Evidence map›Paper›PMID 26851279›Full record

ReviewThe Journal of biological chemistry2016

Modulation of Intrinsically Disordered Protein Function by Post-translational Modifications.

Alaji Bah, Julie D Forman-Kay

Open access · hybridAbstract readReview
In one paragraph

Review in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 288 papers.

0numbers the graph read from it
0cells of the map it votes in
288citing papers in PubMed
23.8field-weighted citation impact, top 1% of its field
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

288 citing papers in PubMed, 563 citations in OpenAlex.

  1. Article
  2. CDK8 phosphorylation of DELLA limits Mediator recruitment in gibberellin signaling.Proceedings of the National Academy of Sciences of the United States of America · 2026
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228 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

2 authors at 2 institutions in 1 country.

Alaji BahFrom the Program in Molecular Structure & Function, The Hospital for Sick Children, Toronto, Ontario M5G 0A4 and the Department of Biochemistry, University of Toronto, Toronto, Ontario M5S 1A8, Canada alaji.bah@sickkids.ca.
Julie D Forman-KayFrom the Program in Molecular Structure & Function, The Hospital for Sick Children, Toronto, Ontario M5G 0A4 and the Department of Biochemistry, University of Toronto, Toronto, Ontario M5S 1A8, Canada forman@sickkids.ca.
Hospital for Sick Children · CAUniversity of Toronto · CA

Funding

Canadian Institutes of Health Research
6 · The paper itself

Abstract

Post-translational modifications (PTMs) produce significant changes in the structural properties of intrinsically disordered proteins (IDPs) by affecting their energy landscapes. PTMs can induce a range of effects, from local stabilization or destabilization of transient secondary structure to global disorder-to-order transitions, potentially driving complete state changes between intrinsically disordered and folded states or dispersed monomeric and phase-separated states. Here, we discuss diverse biological processes that are dependent on PTM regulation of IDPs. We also present recent tools for generating homogenously modified IDPs for studies of PTM-mediated IDP regulatory mechanisms.

Indexed as

Protein Processing, Post-TranslationalAmino AcidsChromatinEukaryotic Initiation FactorsFactor IXHistonesHumansHydrophobic and Hydrophilic InteractionsIntrinsically Disordered ProteinsPhosphorylationProtein BindingProtein FoldingProtein Interaction Domains and MotifsProtein Structure, SecondaryStatic ElectricityThermodynamicsAmino AcidsChromatinEIF4EBP2 protein, humanEukaryotic Initiation FactorsFactor IXHistonesIntrinsically Disordered Proteinsintrinsically disordered proteinpost-translational modification (PTM)protein conformationprotein-DNA interactionprotein-protein interactionregulation

Identifiers

PMID26851279
PMCPMC4807257
OpenAlexW2300545781

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.