Evidence map›Paper›PMID 26179745›Full record

ReviewMicrobiology and molecular biology reviews : MMBR2015

Acylation of Biomolecules in Prokaryotes: a Widespread Strategy for the Control of Biological Function and Metabolic Stress.

Kristy L Hentchel, Jorge C Escalante-Semerena

Open access · bronzeAbstract readReview
In one paragraph

Review in Microbiology and molecular biology reviews : MMBR, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 122 papers.

0numbers the graph read from it
0cells of the map it votes in
122citing papers in PubMed
12.4field-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

122 citing papers in PubMed, 185 citations in OpenAlex.

  1. Article
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  3. InJournal of bacteriology · 2026
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  7. InbioRxiv : the preprint server for biology · 2026
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  10. Review
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  15. Structural basis of the catalytic and allosteric mechanism of bacterial acetyltransferase PatZ.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  16. Article
  17. Protein lysine acetylation regulates oral microorganisms.Frontiers in cellular and infection microbiology · 2025
    Review
  18. Article
  19. Review
  20. Review

62 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.

Kristy L HentchelDepartment of Microbiology, University of Georgia, Athens, Georgia, USA.
Jorge C Escalante-SemerenaDepartment of Microbiology, University of Georgia, Athens, Georgia, USA jescala@uga.edu.
University of Georgia · US

Funding

Sirtuins and Metabolic Pathway IntegrationR01GM062203 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI ESCALANTE, JORGE C · 2001 to 2017
$4.7M
NIGMS NIH HHS R01 GM062203
6 · The paper itself

Abstract

Acylation of biomolecules (e.g., proteins and small molecules) is a process that occurs in cells of all domains of life and has emerged as a critical mechanism for the control of many aspects of cellular physiology, including chromatin maintenance, transcriptional regulation, primary metabolism, cell structure, and likely other cellular processes. Although this review focuses on the use of acetyl moieties to modify a protein or small molecule, it is clear that cells can use many weak organic acids (e.g., short-, medium-, and long-chain mono- and dicarboxylic aliphatics and aromatics) to modify a large suite of targets. Acetylation of biomolecules has been studied for decades within the context of histone-dependent regulation of gene expression and antibiotic resistance. It was not until the early 2000s that the connection between metabolism, physiology, and protein acetylation was reported. This was the first instance of a metabolic enzyme (acetyl coenzyme A [acetyl-CoA] synthetase) whose activity was controlled by acetylation via a regulatory system responsive to physiological cues. The above-mentioned system was comprised of an acyltransferase and a partner deacylase. Given the reversibility of the acylation process, this system is also referred to as reversible lysine acylation (RLA). A wealth of information has been obtained since the discovery of RLA in prokaryotes, and we are just beginning to visualize the extent of the impact that this regulatory system has on cell function.

Indexed as

Protein Processing, Post-TranslationalAcylationAcyltransferasesAnimalsArchaeaArchaeal ProteinsBacteriaBacterial ProteinsCatalytic DomainHumansProteomeStress, PhysiologicalAcyltransferasesArchaeal ProteinsBacterial ProteinsProteome

Identifiers

PMID26179745
PMCPMC4503791
OpenAlexW2114770724

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.