Evidence map›Paper›PMID 26851278›Full record

ReviewThe Journal of biological chemistry2016

Role of Intrinsic Protein Disorder in the Function and Interactions of the Transcriptional Coactivators CREB-binding Protein (CBP) and p300.

H Jane Dyson, Peter E Wright

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 201 papers.

0numbers the graph read from it
0cells of the map it votes in
201citing papers in PubMed
14.5field-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

201 citing papers in PubMed, 346 citations in OpenAlex.

  1. Article
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  6. Review
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  11. Enhancer Dynamics for Gene Regulation in the Cardiovascular System.Arteriosclerosis, thrombosis, and vascular biology · 2026
    Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Single-base mJournal of virology · 2025
    Article
  19. Article
  20. Article

141 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 1 institution in 1 country.

H Jane DysonFrom the Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, California 92037-1000 dyson@scripps.edu.ORCID http://orcid.org/0000-0001-6855-3398
Peter E WrightFrom the Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, California 92037-1000 wright@scripps.edu.ORCID http://orcid.org/0000-0002-1368-0223
Scripps Research Institute · US

Funding

Structural basis for CBP/p300 transcriptional regulationR01CA096865 · NCI · SCRIPPS RESEARCH INSTITUTE, THE · PI WRIGHT, PETER EDWIN · 2002 to 2016
$6.2M
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 CA096865NCI NIH HHS R01 CA096865NIGMS NIH HHS GM113251NIGMS NIH HHS R01 GM113251
6 · The paper itself

Abstract

The transcriptional coactivators CREB-binding protein (CBP) and p300 undergo a particularly rich set of interactions with disordered and partly ordered partners, as a part of their ubiquitous role in facilitating transcription of genes. CBP and p300 contain a number of small structured domains that provide scaffolds for the interaction of disordered transactivation domains from a wide variety of partners, including p53, hypoxia-inducible factor 1α (HIF-1α), NF-κB, and STAT proteins, and are the targets for the interactions of disordered viral proteins that compete with cellular factors to disrupt signaling and subvert the cell cycle. The functional diversity of the CBP/p300 interactome provides an excellent example of the power of intrinsic disorder to facilitate the complexity of living systems.

Indexed as

CREB-Binding ProteinE1A-Associated p300 ProteinHumansHypoxia-Inducible Factor 1, alpha SubunitIntrinsically Disordered ProteinsModels, MolecularNF-kappa BProtein BindingProtein FoldingProtein Interaction Domains and MotifsProtein Structure, SecondarySTAT Transcription FactorsTranscription, GeneticTumor Suppressor Protein p53Viral ProteinsCREB-Binding ProteinCREBBP protein, humanE1A-Associated p300 ProteinEP300 protein, humanHIF1A protein, humanHypoxia-Inducible Factor 1, alpha SubunitIntrinsically Disordered ProteinsNF-kappa BSTAT Transcription FactorsTumor Suppressor Protein p53Viral ProteinscAMP response element-binding protein (CREB)coupled folding and bindinghypoxia-inducible factor (HIF)IDPIDRintrinsically disordered proteinintrinsically disordered regionprotein-protein interactionSTAT transcription factorstructure-functiontranscriptional activationtranscriptional coactivatorviral oncoprotein

Identifiers

PMID26851278
PMCPMC4807259
OpenAlexW2294967868

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.