Evidence map›Paper›PMID 24382882›Full record

ReviewPhysiological reviews2014

Targeting aldehyde dehydrogenase 2: new therapeutic opportunities.

Che-Hong Chen, Julio Cesar Batista Ferreira, Eric R Gross, Daria Mochly-Rosen

Open access · greenAbstract readReview
In one paragraph

Review in Physiological reviews, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 353 papers, 3 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
353citing papers in PubMed, 3 pooled it
24.1field-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

353 citing papers in PubMed, 3 syntheses or guidelines pooled it, 616 citations in OpenAlex.

  1. Pooled it
  2. Pooled it
  3. Pooled it
  4. Trial
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Effect ofBJPsych open · 2026
    Article
  13. Alcohol Interaction and ALDH2: Missing Links in EMPHASIS.Cerebrovascular diseases (Basel, Switzerland) · 2026
    Article
  14. Article
  15. Article
  16. Review
  17. Biphasic regulation of myogenesis by ALDH2, aldosterone, and oxidative stress.Pflugers Archiv : European journal of physiology · 2026
    Article
  18. Article
  19. Article
  20. The role of KPNA3 in multiple myeloma: implications for targeting nuclear import.Apoptosis : an international journal on programmed cell death · 2026
    Article

293 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

4 authors at 2 institutions in 2 countries.

Che-Hong Chen
Julio Cesar Batista Ferreira
Eric R Gross
Daria Mochly-Rosen
Stanford University · USUniversidade de São Paulo · BR

Funding

Mechanisms of Ethanol-Induced Cardiac ProtectionR37AA011147 · NIAAA · STANFORD UNIVERSITY · PI MOCHLY-ROSEN, DARIA · 2009 to 2018
$5.3M
Role of the TRPV1 channel in myocardial salvage from ischemia-reperfusion injuryR00HL109212 · NHLBI · STANFORD UNIVERSITY · PI GROSS, ERIC RICHARD · 2014 to 2016
$772k
Role of the TRPV1 channel in myocardial salvage from ischemia-reperfusion injuryK99HL109212 · NHLBI · STANFORD UNIVERSITY · PI GROSS, ERIC RICHARD · 2011 to 2012
$266k
NHLBI NIH HHS HL-109212NHLBI NIH HHS K99 HL109212NHLBI NIH HHS R00 HL109212NIAAA NIH HHS R37 AA011147NIAAA NIH HHS R37 AA11147
6 · The paper itself

Abstract

A family of detoxifying enzymes called aldehyde dehydrogenases (ALDHs) has been a subject of recent interest, as its role in detoxifying aldehydes that accumulate through metabolism and to which we are exposed from the environment has been elucidated. Although the human genome has 19 ALDH genes, one ALDH emerges as a particularly important enzyme in a variety of human pathologies. This ALDH, ALDH2, is located in the mitochondrial matrix with much known about its role in ethanol metabolism. Less known is a new body of research to be discussed in this review, suggesting that ALDH2 dysfunction may contribute to a variety of human diseases including cardiovascular diseases, diabetes, neurodegenerative diseases, stroke, and cancer. Recent studies suggest that ALDH2 dysfunction is also associated with Fanconi anemia, pain, osteoporosis, and the process of aging. Furthermore, an ALDH2 inactivating mutation (termed ALDH2*2) is the most common single point mutation in humans, and epidemiological studies suggest a correlation between this inactivating mutation and increased propensity for common human pathologies. These data together with studies in animal models and the use of new pharmacological tools that activate ALDH2 depict a new picture related to ALDH2 as a critical health-promoting enzyme.

Indexed as

AgingAldehyde DehydrogenaseAldehyde Dehydrogenase, MitochondrialAnimalsHumansLiverMutationNeoplasmsAldehyde DehydrogenaseAldehyde Dehydrogenase, MitochondrialALDH2 protein, human

Identifiers

PMID24382882
PMCPMC3929114
OpenAlexW2110549318

What OpenQuestion holds

Textmetadata
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.