Evidence map›Paper›PMID 32841743›Full record

ReviewBiochimica et biophysica acta. Gene regulatory mechanisms2021

Catalysis by protein acetyltransferase Gcn5.

Brittany N Albaugh, John M Denu

Open access · greenAbstract readReview
In one paragraph

Review in Biochimica et biophysica acta. Gene regulatory mechanisms, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.0field-weighted citation impact, top 21% 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

17 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. 5-Thiohistidine N-Acetyltransferase from Proteiniphilum Saccharofermentans.Chembiochem : a European journal of chemical biology · 2025
    Article
  7. Review
  8. Csn5 Depletion Reverses Mitochondrial Defects in GCN5-NullInternational journal of molecular sciences · 2025
    Article
  9. Article
  10. Review
  11. N-acetyl cysteine through modulation of HDACIBRO neuroscience reports · 2025
    Article
  12. GCN5L: a critical target in energy metabolism pathways.Frontiers in cell and developmental biology · 2025
    Review
  13. Review
  14. Review
  15. Review
  16. Review
  17. 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

2 authors at 2 institutions in 1 country.

Brittany N AlbaughDepartment of Chemistry, Eastern Michigan University, Ypsilanti, MI 48197, USA. Electronic address: balbaug1@emich.edu.
John M DenuWisconsin Institute for Discovery, University of Wisconsin-Madison, Madison, WI 53715, USA; Department of Biomolecular Chemistry, School of Medicine and Public Health, University of Wisconsin-Madison, Madison, WI 53715, USA.
Eastern Michigan University · USUniversity of Wisconsin–Madison · US

Funding

Reversible protein acetylation and sirtuin functionR01GM065386 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI DENU, JOHN M · 2003 to 2022
$7.3M
Molecular mechanisms of histone modification - Alzheimer’s supplement NOT-AG-18-008R37GM059785 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI DENU, JOHN M · 2013 to 2022
$3.7M
Molecular Mechanisms of Histone AcetyltransferasesR01GM059785 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI DENU, JOHN M · 1999 to 2012
$2.9M
NIGMS NIH HHS R01 GM059785NIGMS NIH HHS R01 GM065386NIGMS NIH HHS R37 GM059785
6 · The paper itself

Abstract

Gcn5 serves as the defining member of the Gcn5-related N-acetyltransferase (GNAT) superfamily of proteins that display a common structural fold and catalytic mechanism involving the transfer of the acyl-group, primarily acetyl-, from CoA to an acceptor nucleophile. In the case of Gcn5, the target is the ε-amino group of lysine primarily on histones. Over the years, studies on Gcn5 structure-function have often formed the basis by which we understand the complex activities and regulation of the entire protein acetyltransferase family. It is now appreciated that protein acetylation occurs on thousands of proteins and can reversibly regulate the function of many cellular processes. In this review, we provide an overview of our fundamental understanding of catalysis, regulation of activity and substrate selection, and inhibitor development for this archetypal acetyltransferase.

Indexed as

BiocatalysisAcetylationAcetyl Coenzyme ACrystallographyDrug DevelopmentEnzyme InhibitorsEpigenesis, GeneticGene Expression Regulation, DevelopmentalHistone AcetyltransferasesHistonesLysineModels, MolecularMultienzyme Complexesp300-CBP-Associated Factorp300-CBP Transcription FactorsProtein DomainsAcetyl Coenzyme AEnzyme InhibitorsGCN5 protein, S cerevisiaeHistone AcetyltransferasesHistonesLysineMultienzyme Complexesp300-CBP-Associated Factorp300-CBP Transcription FactorsRecombinant ProteinsSaccharomyces cerevisiae ProteinstGCN5 histone acetyltransferaseCatalysisGcn5HATHistone acetyltransferaseInhibitorKAT

Identifiers

PMID32841743
PMCPMC7854473
OpenAlexW3080446426

What OpenQuestion holds

Textmetadata
LicenceTDM
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.