Evidence map›Paper›PMID 24725594›Full record

ReviewMolecular cell2014

Nonenzymatic protein acylation as a carbon stress regulated by sirtuin deacylases.

Gregory R Wagner, Matthew D Hirschey

Open access · bronzeAbstract readReview
In one paragraph

Review in Molecular cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 200 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
200citing papers in PubMed, 1 pooled it
19.5field-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

200 citing papers in PubMed, 1 synthesis or guideline pooled it, 316 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. SIRT2 deacylase modulators control B cell metabolic reprogramming in EBV infection and mitogenic activation.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  4. Review
  5. Article
  6. Biochemistry and regulation of histone lysine L-lactylation.Nature reviews. Molecular cell biology · 2026
    Review
  7. Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Histone acylation at a glance.Journal of cell science · 2024
    Review
  18. Mitochondrial dysfunction: mechanisms and advances in therapy.Signal transduction and targeted therapy · 2024
    Review
  19. Review
  20. Review

140 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 2 institutions in 1 country.

Gregory R WagnerDuke Molecular Physiology Institute, Duke University Medical Center, Durham, NC 27710, USA.
Matthew D HirscheyDuke Molecular Physiology Institute, Duke University Medical Center, Durham, NC 27710, USA; Sarah W. Stedman Nutrition and Metabolism Center, Duke University Medical Center, Durham, NC 27704, USA; Departments of Medicine and Department of Pharmacology and Cancer Biology, Duke University Medical Center, Durham, NC 27710, USA. Electronic address: matthew.hirschey@duke.edu.
Duke Medical Center · USDuke University · US

Funding

Resource Core 3 - Metabolomics CoreP30AG028716 · NIA · DUKE UNIVERSITY · PI Sarah B. Peskoe · 2006 to 2026
$24.6M
Renal Genomics CoreP30DK096493 · NIDDK · DUKE UNIVERSITY · PI PATEL, UPTAL D · 2012 to 2016
$5.9M
Studies on the Mechanisms by which SIRT5 Regulates Aging and DiseaseR01AG045351 · NIA · DUKE UNIVERSITY · PI HIRSCHEY, MATTHEW D · 2014 to 2023
$4.4M
Ethanol-induced Protein Acylation Regulates MetabolismR01AA022146 · NIAAA · DUKE UNIVERSITY · PI FRITZ, KRISTOFER S, HIRSCHEY, MATTHEW D · 2013 to 2017
$2.3M
NIAAA NIH HHS AA022146NIAAA NIH HHS R01 AA022146NIA NIH HHS AG045351NIA NIH HHS P30AG028716-01NIA NIH HHS R01 AG045351NIDDK NIH HHS P30 DK096493
6 · The paper itself

Abstract

Cellular proteins are decorated with a wide range of acetyl and other acyl modifications. Many studies have demonstrated regulation of site-specific acetylation by acetyltransferases and deacetylases. Acylation is emerging as a new type of lysine modification, but less is known about its overall regulatory role. Furthermore, the mechanisms of lysine acylation, its overlap with protein acetylation, and how it influences cellular function are major unanswered questions in the field. In this review, we discuss the known roles of acetyltransferases and deacetylases and the sirtuins as a conserved family of a nicotinamide adenine dinucleotide (NAD⁺)-dependent protein deacylases that are important for response to cellular stress and homeostasis. We also consider the evidence for an emerging idea of nonenzymatic protein acylation. Finally, we put forward the hypothesis that protein acylation is a form of protein "carbon stress" that the deacylases evolved to remove as a part of a global protein quality-control network.

Indexed as

Protein Processing, Post-TranslationalStress, PhysiologicalAcylationAnimalsCarbonHumansLysineModels, BiologicalProteinsSirtuinsCarbonLysineProteinsSirtuins

Identifiers

PMID24725594
PMCPMC4040445
OpenAlexW2037877475

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.