Evidence map›Paper›PMID 26934307›Full record

ArticleTranscription2016

The essential role of acetyllysine binding by the YEATS domain in transcriptional regulation.

Forest H Andrews, Erin K Shanle, Brian D Strahl, Tatiana G Kutateladze

Abstract read
In one paragraph

Article in Transcription, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing 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

25 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Epigenetics-targeted drugs: current paradigms and future challenges.Signal transduction and targeted therapy · 2024
    Review
  7. Article
  8. Review
  9. GAS41 promotes H2A.Z deposition through recognition of the N terminus of histone H3 by the YEATS domain.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  10. Differences and similarities in recognition of co-factors by Taf14.Biochimica et biophysica acta. Gene regulatory mechanisms · 2023
    Article
  11. Review
  12. Article
  13. Taf2 mediates DNA binding of Taf14.Nature communications · 2022
    Article
  14. Review
  15. Fragment-Based Discovery of AF9 YEATS Domain Inhibitors.International journal of molecular sciences · 2022
    Article
  16. Review
  17. Review
  18. Article
  19. Bromodomain biology and drug discovery.Nature structural & molecular biology · 2019
    Review
  20. Article
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.

Forest H Andrewsa Department of Pharmacology , University of Colorado School of Medicine , Aurora , CO , USA.
Erin K Shanleb Department of Biochemistry & Biophysics , The University of North Carolina School of Medicine , Chapel Hill , NC , USA.
Brian D Strahlb Department of Biochemistry & Biophysics , The University of North Carolina School of Medicine , Chapel Hill , NC , USA.
Tatiana G Kutateladzeb Department of Biochemistry & Biophysics , The University of North Carolina School of Medicine , Chapel Hill , NC , USA.

Funding

SEEDING POSTDOCTORAL INNOVATORS IN RESEARCH &EDUCATIONK12GM000678 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI DONALD T LYSLE, Kathryn Joanna Reissner · 1999 to 2026
$30.9M
BEHAVIORAL PHARMACOGENETICS OF DRUG AND ALCOHOL ABUSET32AA007464 · NIAAA · UNIVERSITY OF COLORADO DENVER · PI HOFFMAN, PAULA · 1987 to 2017
$4.8M
Molecular analysis of methylated p53R01GM101664 · NIGMS · UNIVERSITY OF COLORADO DENVER · PI KUTATELADZE, TATIANA G · 2013 to 2016
$1.7M
Epigenetic regulation by PHF1R01GM106416 · NIGMS · UNIVERSITY OF COLORADO DENVER · PI KUTATELADZE, TATIANA G · 2015 to 2018
$1.5M
Molecular mechanism of chromatin targeting by BRPF1R01GM100907 · NIGMS · UNIVERSITY OF COLORADO DENVER · PI KUTATELADZE, TATIANA G · 2015 to 2018
$1.4M
Factors that regulate chromatin organization and gene transcriptionR01GM110058 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI STRAHL, BRIAN D · 2014 to 2017
$1.2M
NIAAA NIH HHS T32AA007464NIGMS NIH HHS GM100907NIGMS NIH HHS GM101664NIGMS NIH HHS GM106416NIGMS NIH HHS GM110058NIGMS NIH HHS K12 GM000678NIGMS NIH HHS K12-GM000678NIGMS NIH HHS R01 GM100907NIGMS NIH HHS R01 GM101664NIGMS NIH HHS R01 GM106416NIGMS NIH HHS R01 GM110058
6 · The paper itself

Abstract

The YEATS domains of AF9 and Taf14 have recently been found to recognize the histone H3K9ac modification. In this commentary, we discuss the mechanistic and biological implications of this interaction. We compare structures of the YEATS-H3K9ac complexes the highlighting a novel mechanism for the acetyllysine recognition through the aromatic cage. We also summarize the latest findings underscoring a critical role of the acetyllysine binding function of AF9 and Taf14 in transcriptional regulation and DNA repair.

Indexed as

AcetylationBinding SitesGene Expression RegulationHistone-Lysine N-MethyltransferaseHumansLysineMethyltransferasesNuclear ProteinsProtein ConformationProtein Structure, TertiarySaccharomyces cerevisiae ProteinsTranscription Factor TFIIDTranscription, GeneticDOT1L protein, humanHistone-Lysine N-MethyltransferaseLysineMethyltransferasesMLLT3 protein, humanNuclear ProteinsSaccharomyces cerevisiae ProteinsTAF14 protein, S cerevisiaeTranscription Factor TFIIDacetyllysineAF9Taf14transcriptionYEATS domain

Identifiers

PMID26934307
PMCPMC4802754

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.