Evidence map›Paper›PMID 35805129›Full record

ReviewCells2022

Biochemical Mechanisms of Sirtuin-Directed Protein Acylation in Hepatic Pathologies of Mitochondrial Dysfunction.

Courtney D McGinnis, Erin Q Jennings, Peter S Harris, James J Galligan, Kristofer S Fritz

Open access · goldAbstract readReview
In one paragraph

Review in Cells, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

8 citing papers in PubMed, 18 citations in OpenAlex.

  1. Review
  2. NADCells · 2025
    Review
  3. Article
  4. Review
  5. Review
  6. The sirtuin family in health and disease.Signal transduction and targeted therapy · 2022
    Review
  7. Article
  8. Article
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

5 authors at 2 institutions in 1 country.

Courtney D McGinnisSkaggs School of Pharmacy and Pharmaceutical Sciences, University of Colorado Anschutz Medical Campus, Aurora, CO 80045, USA.
Erin Q JenningsDepartment of Pharmacology and Toxicology, College of Pharmacy, University of Arizona, Tucson, AZ 85721, USA.
Peter S HarrisSkaggs School of Pharmacy and Pharmaceutical Sciences, University of Colorado Anschutz Medical Campus, Aurora, CO 80045, USA.
James J GalliganDepartment of Pharmacology and Toxicology, College of Pharmacy, University of Arizona, Tucson, AZ 85721, USA.
Kristofer S FritzSkaggs School of Pharmacy and Pharmaceutical Sciences, University of Colorado Anschutz Medical Campus, Aurora, CO 80045, USA.
University of Colorado Anschutz Medical Campus · USUniversity of Arizona · US

Funding

Training in Environmental Toxicology of Human DiseaseT32ES007091 · NIEHS · UNIVERSITY OF ARIZONA · PI Nathan J Cherrington · 1985 to 2026
$10.7M
Establishing Glyoxalase 2 as a Viable Target for the Treatment of Disease [Equipment Supplement]R35GM137910 · NIGMS · UNIVERSITY OF ARIZONA · PI GALLIGAN, JAMES J · 2020 to 2024
$2.1M
Regulation of insulin signaling and sensitivity by the xenobiotic metabolizing enzyme NQO1R01DK109964 · NIDDK · UNIVERSITY OF COLORADO DENVER · PI DE CABO, RAFAEL, FRITZ, KRISTOFER S · 2017 to 2021
$1.9M
Ethanol Metabolism Disrupts Hepatic Thiol Redox Signaling and ControlR21AA026928 · NIAAA · UNIVERSITY OF COLORADO DENVER · PI FRITZ, KRISTOFER S, ROEDE, JAMES R · 2018 to 2019
$423k
Mechanisms of Alcohol Toxicity and Kidney DamageR21AA029218 · NIAAA · UNIVERSITY OF COLORADO DENVER · PI FRITZ, KRISTOFER S · 2021 to 2022
$408k
NIAAA NIH HHS R21 AA026928NIAAA NIH HHS R21 AA029218NIDDK NIH HHS R01 DK109964NIEHS NIH HHS T32 ES007091NIGMS NIH HHS R35 GM137910
6 · The paper itself

Abstract

Mitochondrial protein acetylation is associated with a host of diseases including cancer, Alzheimer's, and metabolic syndrome. Deciphering the mechanisms regarding how protein acetylation contributes to disease pathologies remains difficult due to the complex diversity of pathways targeted by lysine acetylation. Specifically, protein acetylation is thought to direct feedback from metabolism, whereby nutritional status influences mitochondrial pathways including beta-oxidation, the citric acid cycle, and the electron transport chain. Acetylation provides a crucial connection between hepatic metabolism and mitochondrial function. Dysregulation of protein acetylation throughout the cell can alter mitochondrial function and is associated with numerous liver diseases, including non-alcoholic and alcoholic fatty liver disease, steatohepatitis, and hepatocellular carcinoma. This review introduces biochemical mechanisms of protein acetylation in the regulation of mitochondrial function and hepatic diseases and offers a viewpoint on the potential for targeted therapies.

Indexed as

Sirtuin 3SirtuinsAcetylationMitochondriaMitochondrial ProteinsMitochondrial ProteinsSirtuin 3Sirtuinsacetylationalcoholic liver diseasehistone deacetylasemetabolic syndromemitochondrianon-alcoholic liver diseasesirtuin

Identifiers

PMID35805129
PMCPMC9266223
OpenAlexW4283708186

What Socratic 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 Socratic graph.