Evidence map›Paper›PMID 21609791›Full record

ReviewJournal of proteomics2011

Post-translational modifications of mitochondrial aldehyde dehydrogenase and biomedical implications.

Byoung-Joon Song, Mohamed A Abdelmegeed, Seong-Ho Yoo, Bong-Jo Kim, Sangmee A Jo, Inho Jo, Kwan-Hoon Moon

Abstract readReview
In one paragraph

Review in Journal of proteomics, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
4.4field-weighted citation impact, top 6% 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

43 citing papers in PubMed, 72 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. DownregulatedCells · 2025
    Article
  5. Article
  6. The Significance of Aldehyde Dehydrogenase 1 in Cancers.International journal of molecular sciences · 2024
    Review
  7. Review
  8. Article
  9. Review
  10. Review
  11. Review
  12. [Research progress of acetaldehyde dehydrogenase 2 in liver diseases].Zhonghua gan zang bing za zhi = Zhonghua ganzangbing zazhi = Chinese journal of hepatology · 2022
    Article
  13. Article
  14. Article
  15. Review
  16. Ameliorative effect ofFrontiers in pharmacology · 2022
    Article
  17. Brain ethanol metabolism and mitochondria.Current topics in biochemical research · 2022
    Article
  18. Review
  19. Article
  20. 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

7 authors at 4 institutions in 2 countries.

Byoung-Joon SongSection of Molecular Pharmacology and Toxicology, Laboratory of Membrane Biochemistry and Biophysics, National Institute on Alcohol Abuse and Alcoholism, Bethesda, MD 20892-9410, USA. bj.song@nih.gov
Mohamed A Abdelmegeed
Seong-Ho Yoo
Bong-Jo Kim
Sangmee A Jo
Inho Jo
Kwan-Hoon Moon
National Institute on Alcohol Abuse and Alcoholism · USDankook University · KREwha Womans University · KRKorea National Institute of Health · KR

Funding

Alcohol Metabolism, Functional Consequences, Apoptosis Signaling Pathways, and Organ DamageZIAAA000036 · NIAAA · NATIONAL INSTITUTE ON ALCOHOL ABUSE AND ALCOHOLISM · PI SONG, BYOUNG-JOON · 2009 to 2025
$14.8M
Intramural NIH HHS Z99 AA999999Intramural NIH HHS ZIA AA000036
6 · The paper itself

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.

Indexed as

Protein Processing, Post-TranslationalAcetaldehydeAldehyde DehydrogenaseAldehyde Dehydrogenase, MitochondrialAnimalsAsian PeopleEnzyme ActivatorsGenes, DominantHumansLipid PeroxidesLiver Diseases, AlcoholicMitochondrial ProteinsMutationMyocardial InfarctionNeoplasmsRisk FactorsAcetaldehydeAldehyde DehydrogenaseAldehyde Dehydrogenase, MitochondrialALDH2 protein, humanEnzyme ActivatorsLipid PeroxidesMitochondrial Proteins

Identifiers

PMID21609791
PMCPMC3177986
OpenAlexW1995928536

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.