Cited by 73Alcohol Consumption and Health EffectsAldose Reductase and TaurineRedox biology and oxidative stress

Post-translational modifications of mitochondrial aldehyde dehydrogenase and biomedical implications

Open access
Song, Byoung-Joon, Abdelmegeed, Mohamed A., Yoo, Seong-Ho, Kim, Bong-Jo, Jo, Sangmee A., Jo, Inho, Moon, Kwan-Hoon·2011·Journal of Proteomics

Abstract

Aldehyde dehydrogenases (ALDHs) represent large family members of NAD(P)+-dependent dehydrogenases responsible for the irreversible metabolism of many endogenous and exogenous aldehydes to the corresponding acids. Among 19 ALDH isozymes, mitochondrial ALDH2 is a low Km enzyme responsible for the metabolism of acetaldehyde and lipid peroxides such as malondialdehyde and 4-hydroxynonenal, both of which are highly reactive and toxic. Consequently, inhibition of ALDH2 would lead to elevated levels of acetaldehyde and other reactive lipid peroxides following ethanol intake and/or exposure to toxic chemicals. In addition, many East Asian people with a dominant negative mutation in ALDH2 gene possess a decreased ALDH2 activity with increased risks for various types of cancer, myocardial infarct, alcoholic liver disease, and other pathological conditions. The aim of this review is to briefly describe the multiple post-translational modifications of mitochondrial ALDH2, as an example, after exposure to toxic chemicals or under different disease states and their pathophysiological roles in promoting alcohol/drug-mediated tissue damage. We also briefly mention exciting preclinical translational research opportunities to identify small molecule activators of ALDH2 and its isozymes as potentially therapeutic/preventive agents against various disease states where the expression or activity of ALDH enzymes is altered or inactivated.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1016/j.jprot.2011.05.013

Cites

137 of 137 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Cites

1 retracted

Flagged first, then by citations

Cited by

Sorted by citations

Authors
Song, B.-J., Abdelmegeed, M. A., Yoo, S.-H., Kim, B.-J., Jo, S. A., Jo, I., & Moon, K.-H.
Affiliations
  • National Institutes of Health (US)
  • Dankook University (KR)
  • Ewha Womans University (KR)
Corresponding author
Song, Byoung-Joon
Venue
Journal of Proteomics
Publisher
Elsevier BV
Published
2011-11
Volume
74
Issue
12
Pages
2691-2702
ISSN
1874-3919 (ISSN-L)
OpenAlex
W1995928536
Cited by
73
References
137
Citations by year
2026: 2 · 2025: 3 · 2024: 5 · 2023: 2 · 2022: 7 · 2021: 2 · 2020: 3 · 2019: 3 · 2018: 7 · 2017: 5 · 2016: 5 · 2015: 7 · 2014: 11 · 2013: 7 · 2012: 4
FWCI
0.89
Type
journal article
Language
en
Open access
Locations
  • Journal of Proteomics (publishedVersion)
  • PubMed (publishedVersion)
  • Europe PMC (PubMed Central) (acceptedVersion)
  • PubMed Central (acceptedVersion)
Funders
  • National Institute on Alcohol Abuse and Alcoholism
  • Center for Biological Modulators in South Korea
Topics
  • Health Sciences › Medicine › Pathology and Forensic Medicine › Alcohol Consumption and Health Effects
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Aldose Reductase and Taurine
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Keywords
ALDH2, post-translational modification, mitochondrial enzymes, acetaldehyde metabolism, lipid hydroperoxides, cancer risk, myocardial infarction, alcoholic liver disease
MeSH terms
Aldehyde Dehydrogenase, Mitochondrial, Acetaldehyde, Aldehyde Dehydrogenase, Animals, Genes, Dominant, Humans, Lipid Peroxides, Liver Diseases, Alcoholic, Mutation, Myocardial Infarction, Neoplasms, Protein Processing, Post-Translational, Risk Factors, Enzyme Activators, Mitochondrial Proteins, Asian People

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review