Evidence map›Paper›PMID 30038465›Full record

ReviewWorld journal of gastroenterology2018

Role of aldehyde dehydrogenase 2 in ischemia reperfusion injury: An update.

Arnau Panisello-Roselló, Alexandre Lopez, Emma Folch-Puy, Teresa Carbonell, Anabela Rolo, Carlos Palmeira, René Adam, Marc Net, Joan Roselló-Catafau

Open access · hybridAbstract readReview
In one paragraph

Review in World journal of gastroenterology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

38 citing papers in PubMed, 61 citations in OpenAlex.

  1. Article
  2. ALDH2 Mediated Ferroptosis Regulation in Ischemia-Reperfusion Injury.Journal of cellular and molecular medicine · 2026
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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

9 authors at 4 institutions in 3 countries.

Arnau Panisello-RosellóDepartment of Experimental Pathology, Institute of Biomedical Research of Barcelona (IIBB)-CSIC, Barcelona 08036, Spain.
Alexandre LopezCentre Hepatobiliare, AP-HP Hôpital Paul Brousse, Villejuif 75008, France.
Emma Folch-PuyDepartment of Experimental Pathology, Institute of Biomedical Research of Barcelona (IIBB)-CSIC, Barcelona 08036, Spain.
Teresa CarbonellDepartment of Physiology, Faculty of Biology, Universitat de Barcelona, Barcelona 08036, Spain.
Anabela RoloCenter for Neuroscience and Cell Biology, University of Coimbra, Coimbra 3004-517, Portugal.
Carlos PalmeiraCenter for Neuroscience and Cell Biology, University of Coimbra, Coimbra 3004-517, Portugal.
René AdamCentre Hepatobiliare, AP-HP Hôpital Paul Brousse, Villejuif 75008, France.
Marc NetInstitute Georges Lopez, Lissieu 69380, France.
Joan Roselló-CatafauDepartment of Experimental Pathology, Institute of Biomedical Research of Barcelona (IIBB)-CSIC, Barcelona 08036, Spain. jrcbam@iibb.csic.es.
Assistance Publique – Hôpitaux de Paris · FRInstitut d'Investigacions Biomèdiques de Barcelona · ESUniversity of Coimbra · PTUniversitat de Barcelona · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Aldehyde dehydrogenase 2 (ALDH2) is best known for its critical detoxifying role in liver alcohol metabolism. However, ALDH2 dysfunction is also involved in a wide range of human pathophysiological situations and is associated with complications such as cardiovascular diseases, diabetes mellitus, neurodegenerative diseases and aging. A growing body of research has shown that ALDH2 provides important protection against oxidative stress and the subsequent loading of toxic aldehydes such as 4-hydroxy-2-nonenal and adducts that occur in human diseases, including ischemia reperfusion injury (IRI). There is increasing evidence of its role in IRI pathophysiology in organs such as heart, brain, small intestine and kidney; however, surprisingly few studies have been carried out in the liver, where ALDH2 is found in abundance. This study reviews the role of ALDH2 in modulating the pathways involved in the pathophysiology of IRI associated with oxidative stress, autophagy and apoptosis. Special emphasis is placed on the role of ALDH2 in different organs, on therapeutic "preconditioning" strategies, and on the use of ALDH2 agonists such as Alda-1, which may become a useful therapeutic tool for preventing the deleterious effects of IRI in organ transplantation.

Indexed as

Aldehyde Dehydrogenase, MitochondrialAldehydesAnimalsApoptosisAutophagyBenzamidesBenzodioxolesEnzyme ActivatorsHumansLipid PeroxidesLiverMetabolic Clearance RateOrgan TransplantationOxidative StressReactive Oxygen SpeciesReperfusion Injury4-hydroxy-2-nonenalAldehyde Dehydrogenase, MitochondrialAldehydesALDH2 protein, humanBenzamidesBenzodioxolesEnzyme ActivatorsLipid PeroxidesN-(1,3-benzodioxol-5-ylmethyl)-2,6-dichlorobenzamideReactive Oxygen Species4-hydroxy-2-nonenal autophagyAldehyde dehydrogenase 2ApoptosisIschemia reperfusion injuryPreconditioning

Identifiers

PMID30038465
PMCPMC6054945
OpenAlexW2884737578

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.