Evidence map›Paper›PMID 30131726›Full record

ReviewFrontiers in physiology2018

Acetylation of Mitochondrial Proteins in the Heart: The Role of SIRT3.

Rebecca M Parodi-Rullán, Xavier R Chapa-Dubocq, Sabzali Javadov

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in physiology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 96 papers.

0numbers the graph read from it
0cells of the map it votes in
96citing papers in PubMed
9.7field-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

96 citing papers in PubMed, 156 citations in OpenAlex.

  1. Trial
  2. Review
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  7. Article
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  10. Article
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  12. Atlas of lysine acetylation in the mouse.bioRxiv : the preprint server for biology · 2026
    Article
  13. Review
  14. Review
  15. Review
  16. Article
  17. Review
  18. Roles of SIRT3 in aging and aging-related diseases.International journal of biological sciences · 2025
    Review
  19. Metabolic dysregulation in the heart in obesity-associated HFpEF.Frontiers in cardiovascular medicine · 2025
    Article
  20. Article

36 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

3 authors at 1 institution in 1 country.

Rebecca M Parodi-RullánDepartment of Physiology, University of Puerto Rico School of Medicine, San Juan, PR, United States.
Xavier R Chapa-DubocqDepartment of Physiology, University of Puerto Rico School of Medicine, San Juan, PR, United States.
Sabzali JavadovDepartment of Physiology, University of Puerto Rico School of Medicine, San Juan, PR, United States.
University of Puerto Rico System · PR

Funding

RISE Option III: MBRS RISE at the UPR Medical Sciences CampusR25GM061838 · NIGMS · UNIVERSITY OF PUERTO RICO MED SCIENCES · PI CADILLA, CARMEN LYDIA · 2000 to 2021
$25.5M
Mitochondrial Permeability Transition as a Target for Cardioprotection in Heart FSC1HL118669 · NHLBI · UNIVERSITY OF PUERTO RICO MED SCIENCES · PI JAVADOV, SABZALI · 2012 to 2016
$1.3M
Crosstalk between mitochondrial permeability transition and ETC supercomplexes in myocardial infarctionSC1GM128210 · NIGMS · UNIVERSITY OF PUERTO RICO MED SCIENCES · PI JAVADOV, SABZALI · 2017 to 2019
$1.1M
NHLBI NIH HHS SC1 HL118669NIGMS NIH HHS R25 GM061838NIGMS NIH HHS SC1 GM128210
6 · The paper itself

Abstract

A growing number of studies have demonstrated the role of post-translational modifications of proteins, particularly acetylation, in human diseases including neurodegenerative and cardiovascular diseases, diabetes, cancer, and in aging. Acetylation of mitochondrial proteins has been shown to be involved in the pathogenesis of cardiac diseases such as myocardial infarction (ischemia-reperfusion) and heart failure. Indeed, over 60% of mitochondrial proteins contain acetylation sites, and most of these proteins are involved in mitochondrial bioenergetics. Mitochondrial non-enzymatic acetylation is enabled by acetyl-coenzyme A abundance and serves as the primary pathway of acetylation in mitochondria. Hence, regulation of enzymatic deacetylation becomes the most important mechanism to control acetylation/deacetylation of mitochondrial proteins. Acetylation/deacetylation of mitochondrial proteins has been regarded as a key regulator of mitochondrial metabolism and function. Proteins are deacetylated by NAD

Indexed as

cardiac diseasescardioprotectionmitochondriaprotein acetylationSIRT3sirtuins

Identifiers

PMID30131726
PMCPMC6090200
OpenAlexW2887157456

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.