Evidence map›Paper›PMID 22626763›Full record

ReviewMetabolism: clinical and experimental2013

Acetylation and deacetylation--novel factors in muscle wasting.

Nima Alamdari, Zaira Aversa, Estibaliz Castillero, Per-Olof Hasselgren

Open access · greenAbstract readReview
In one paragraph

Review in Metabolism: clinical and experimental, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
3.4field-weighted citation impact, top 8% 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

24 citing papers in PubMed, 71 citations in OpenAlex.

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  15. Immobilization induces nuclear accumulation of HDAC4 in rat skeletal muscle.The journal of physiological sciences : JPS · 2016
    Article
  16. Cardiac cachexia: hic et nunc.Journal of cachexia, sarcopenia and muscle · 2016
    Review
  17. Article
  18. 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

4 authors at 2 institutions in 1 country.

Nima AlamdariDepartment of Surgery, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA, USA.
Zaira Aversa
Estibaliz Castillero
Per-Olof Hasselgren
Beth Israel Deaconess Medical Center · USHarvard University · US

Funding

MUSCLE PROTEIN TURNOVER AND AMINO ACID UPTAKE IN SEPSISR01DK037908 · NIDDK · UNIVERSITY OF CINCINNATI · PI HASSELGREN, PER-OLOF J · 1987 to 2010
$2.6M
NIDDK NIH HHS R01 DK037908NIDDK NIH HHS R01 DK37908
6 · The paper itself

Abstract

We review recent evidence that acetylation and deacetylation of cellular proteins, including transcription factors and nuclear cofactors, may be involved in the regulation of muscle mass. The level of protein acetylation is balanced by histone acetyltransferases (HATs) and histone deacetylases (HDACs) and studies suggest that this balance is perturbed in muscle wasting. Hyperacetylation of transcription factors and nuclear cofactors regulating gene transcription in muscle wasting may influence muscle mass. In addition, hyperacetylation may render proteins susceptible to degradation by different mechanisms, including intrinsic ubiquitin ligase activity exerted by HATs and by dissociation of proteins from cellular chaperones. In recent studies, inhibition of p300/HAT expression and activity and stimulation of SIRT1-dependent HDAC activity reduced glucocorticoid-induced catabolic response in skeletal muscle, providing further evidence that hyperacetylation plays a role in muscle wasting. It should be noted, however, that although several studies advocate a role of hyperacetylation in muscle wasting, apparently contradictory results have also been reported. For example, muscle atrophy caused by denervation or immobilization may be associated with reduced, rather than increased, protein acetylation. In addition, whereas hyperacetylation results in increased degradation of certain proteins, other proteins may be stabilized by increased acetylation. Thus, the role of acetylation and deacetylation in the regulation of muscle mass may be both condition- and protein-specific. The influence of HATs and HDACs on the regulation of muscle mass, as well as methods to modulate protein acetylation, is an important area for continued research aimed at preventing and treating muscle wasting.

Indexed as

AcetylationHistone AcetyltransferasesHistone DeacetylasesHumansMuscle ProteinsMuscle, SkeletalMuscular AtrophyHistone AcetyltransferasesHistone DeacetylasesMuscle Proteins

Identifiers

PMID22626763
PMCPMC3430797
OpenAlexW2038815796

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.