Evidence map›Paper›PMID 25186010›Full record

ReviewAmerican journal of physiology. Cell physiology2014

Understanding the acetylome: translating targeted proteomics into meaningful physiology.

Andrew Philp, Thomas Rowland, Joaquin Perez-Schindler, Simon Schenk

Open access · hybridAbstract readReview
In one paragraph

Review in American journal of physiology. Cell physiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
3.7field-weighted citation impact, top 7% 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

26 citing papers in PubMed, 45 citations in OpenAlex.

  1. Omics Sciences in Regular Physical Activity.International journal of molecular sciences · 2025
    Review
  2. Maintenance of thermogenic adipose tissues despite loss of the H3K27 acetyltransferases p300 or CBP.American journal of physiology. Endocrinology and metabolism · 2024
    Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Review
  16. The dawn of succinylation: a posttranslational modification.American journal of physiology. Cell physiology · 2018
    Review
  17. Article
  18. Review
  19. Article
  20. Review
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 2 institutions in 2 countries.

Andrew PhilpSchool of Sport, Exercise, and Rehabilitation Sciences, University of Birmingham, Birmingham, United Kingdom; and a.philp@bham.ac.uk.
Thomas RowlandSchool of Sport, Exercise, and Rehabilitation Sciences, University of Birmingham, Birmingham, United Kingdom; and.
Joaquin Perez-SchindlerSchool of Sport, Exercise, and Rehabilitation Sciences, University of Birmingham, Birmingham, United Kingdom; and.
Simon SchenkDepartment of Orthopaedic Surgery, University of California, San Diego, La Jolla, California.
University of Birmingham · GBUniversity of California, San Diego · US

Funding

National Center for Muscle Rehabilitation ResearchR24HD050837 · NICHD · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI LIEBER, RICHARD L., WARD, SAMUEL RICHARD · 2005 to 2014
$7.2M
SIRT1 and muscle insulin sensitivityR01AG043120 · NIA · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI SCHENK, SIMON · 2012 to 2016
$1.6M
Muscle Triglyceride Metabolism Core CenterP30AR058878 · NIAMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI LIEBER, RICHARD L. · 2009 to 2010
$925k
Medical Research Council MR/K00414X/1NIAMS NIH HHS P30 AR-058878NIA NIH HHS R01 AG-043120NICHD NIH HHS R24 HD-050837
6 · The paper itself

Abstract

It is well established that exercise elicits a finely tuned adaptive response in skeletal muscle, with contraction frequency, duration, and recovery shaping skeletal muscle plasticity. Given the power of physical activity to regulate metabolic health, numerous research groups have focused on the molecular mechanisms that sense, interpret, and translate this contractile signal into postexercise adaptation. While our current understanding is that contraction-sensitive allosteric factors (e.g., Ca(2+), AMP, NAD(+), and acetyl-CoA) initiate signaling changes, how the muscle translates changes in these factors into the appropriate adaptive response remains poorly understood. During the past decade, systems biology approaches, utilizing "omics" screening techniques, have allowed researchers to define global processes of regulation with incredible sensitivity and specificity. As a result, physiologists are now able to study substrate flux with stable isotope tracers in combination with metabolomic approaches and to coordinate these functional changes with proteomic and transcriptomic analysis. In this review, we highlight lysine acetylation as an important posttranslational modification in skeletal muscle. We discuss the evolution of acetylation research and detail how large proteomic screens in diverse metabolic systems have led to the current hypothesis that acetylation may be a fundamental mechanism to fine-tune metabolic adaptation in skeletal muscle.

Indexed as

Protein Processing, Post-TranslationalAcetylationAcetyltransferasesHistone AcetyltransferasesHumansLysineMitochondrial ProteinsMuscle, SkeletalProteomicsAcetyltransferasesHistone AcetyltransferasesLysineMitochondrial Proteinsadaptationexercisemetabolismmitochondriamuscle

Identifiers

PMID25186010
PMCPMC4216940
OpenAlexW2121919320

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.