Evidence map›Paper›PMID 23742047›Full record

ReviewThe FEBS journal2013

Structure and mechanism of non-histone protein acetyltransferase enzymes.

David R Friedmann, Ronen Marmorstein

Open access · bronzeAbstract readReview
In one paragraph

Review in The FEBS journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
3.5field-weighted citation impact, top 6% 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

45 citing papers in PubMed, 79 citations in OpenAlex.

  1. Article
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  11. The role of acetylation in obesity-induced cardiac metabolic alterations.Journal of pharmacy & pharmaceutical sciences : a publication of the Canadian Society for Pharmaceutical Sciences, Societe canadienne des sciences pharmaceutiques · 2024
    Review
  12. Review
  13. Genetic Analyses of Seed Longevity inPlants (Basel, Switzerland) · 2023
    Article
  14. Article
  15. Review
  16. Article
  17. Review
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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.

David R FriedmannProgram in Gene Expression and Regulation, The Wistar Institute, Philadelphia, PA, 19104, USA.
Ronen Marmorstein
The Wistar Institute · US

Funding

TRAINING PROGRAM IN BASIC CANCER RESEARCHT32CA009171 · NCI · WISTAR INSTITUTE · PI Alessandro Gardini · 1985 to 2026
$15.3M
Structure/Function of Histone AcetyltransferasesR01GM060293 · NIGMS · WISTAR INSTITUTE · PI MARMORSTEIN, RONEN · 2000 to 2016
$5.3M
NCI NIH HHS T32 CA009171NIGMS NIH HHS R01 GM060293
6 · The paper itself

Abstract

Post-translational modification of proteins is ubiquitous and mediates many cellular processes, including intracellular localization, protein-protein interactions, enzyme activity, transcriptional regulation and protein stability. While the role of phosphorylation as a key post-translational modification has been well studied, the more evolutionarily conserved post-translational modification acetylation has only recently attracted attention as a key regulator of cellular events. Protein acetylation has been largely studied in the context of its role in histone modification and gene regulation, where histones are modified by histone acetyltransferases to promote transcription. However, more recent acetylomic and biochemical studies have revealed that acetylation is mediated by a broader family of protein acetyltransferases. The recent structure determination of several protein acetyltransferases has provided a wealth of molecular information regarding structural features of protein acetyltransferases, their enzymatic mechanisms, their mode of substrate-specific recognition and their regulatory elements. In this review, we briefly describe what is known about non-histone protein substrates, but mainly focus on a few recent structures of protein acetyltransferases to compare and contrast them with histone acetyltransferases to better understand the molecular basis for protein recognition and modification by this family of protein modification enzymes.

Indexed as

AcetylationAcetyl Coenzyme AAcetyltransferasesAnimalsCatalytic DomainHistone AcetyltransferasesHumansModels, MolecularMolecular StructureProtein Processing, Post-TranslationalProteinsSubstrate SpecificityAcetyl Coenzyme AAcetyltransferasesHistone AcetyltransferasesProteinsAcCoAenzyme mechanismepigeneticsHATsNATsPATspost-translational modification enzymesprotein acetyltransferasesstructuresubstrate-binding

Identifiers

PMID23742047
PMCPMC4013100
OpenAlexW2134813391

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.