Evidence map›Paper›PMID 26503676›Full record

ReviewNature reviews. Endocrinology2016

Protein acetylation in metabolism - metabolites and cofactors.

Keir J Menzies, Hongbo Zhang, Elena Katsyuba, Johan Auwerx

Open access · greenAbstract readReview
PubMed Publisher
In one paragraph

Review in Nature reviews. Endocrinology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 201 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
201citing papers in PubMed, 1 pooled it
14.7field-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, 1 synthesis or guideline pooled it, 326 citations in OpenAlex.

  1. Pooled it
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  7. Article
  8. Expanding the Genetic Code with Lysine Aminoacylation.Journal of the American Chemical Society · 2026
    Article
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  20. Isoform-specific regulation of PKM by acetylation.Proceedings of the National Academy of Sciences of the United States of America · 2025
    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

4 authors at 1 institution in 1 country.

Keir J MenziesInterdisciplinary School of Health Sciences, University of Ottawa, 501 Smyth Road, Ottawa, ON K1H 8L6, Canada.
Hongbo ZhangLaboratory of Integrative and Systems Physiology, École Polytechnique Fédérale de Lausanne, Station 15, 1015 Lausanne, Switzerland.
Elena KatsyubaLaboratory of Integrative and Systems Physiology, École Polytechnique Fédérale de Lausanne, Station 15, 1015 Lausanne, Switzerland.
Johan AuwerxLaboratory of Integrative and Systems Physiology, École Polytechnique Fédérale de Lausanne, Station 15, 1015 Lausanne, Switzerland.
École Polytechnique Fédérale de Lausanne · CH

Funding

Translational Systems Genetics of Mitochondria, Metabolism, and AgingR01AG043930 · NIA · UNIVERSITY OF TENNESSEE HEALTH SCI CTR · PI WILLIAMS, ROBERT W. · 2013 to 2017
$2.5M
NIA NIH HHS R01AG043930
6 · The paper itself

Abstract

Reversible acetylation was initially described as an epigenetic mechanism regulating DNA accessibility. Since then, this process has emerged as a controller of histone and nonhistone acetylation that integrates key physiological processes such as metabolism, circadian rhythm and cell cycle, along with gene regulation in various organisms. The widespread and reversible nature of acetylation also revitalized interest in the mechanisms that regulate lysine acetyltransferases (KATs) and deacetylases (KDACs) in health and disease. Changes in protein or histone acetylation are especially relevant for many common diseases including obesity, diabetes mellitus, neurodegenerative diseases and cancer, as well as for some rare diseases such as mitochondrial diseases and lipodystrophies. In this Review, we examine the role of reversible acetylation in metabolic control and how changes in levels of metabolites or cofactors, including nicotinamide adenine dinucleotide, nicotinamide, coenzyme A, acetyl coenzyme A, zinc and butyrate and/or β-hydroxybutyrate, directly alter KAT or KDAC activity to link energy status to adaptive cellular and organismal homeostasis.

Indexed as

3-Hydroxybutyric AcidAcetylationAnimalsCoenzymesEnergy MetabolismEpigenesis, GeneticHistone AcetyltransferasesHumansNiacinamideProtein Processing, Post-Translational3-Hydroxybutyric AcidCoenzymesHistone AcetyltransferasesNiacinamide

Identifiers

PMID26503676
OpenAlexW1897794632

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.