Evidence map›Paper›PMID 37686694›Full record

ReviewCancers2023

Human Aldehyde Dehydrogenases: A Superfamily of Similar Yet Different Proteins Highly Related to Cancer.

Vasileios Xanthis, Theodora Mantso, Anna Dimtsi, Aglaia Pappa, Vasiliki E Fadouloglou

Open access · goldAbstract readReview
In one paragraph

Review in Cancers, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
5.5field-weighted citation impact, top 4% 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

22 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
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  5. Alkamines reveal a hidden layer of steroid and drug metabolism.bioRxiv : the preprint server for biology · 2026
    Article
  6. Review
  7. Metabolic trajectories in developing human neocortical neurons.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
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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

5 authors at 1 institution in 1 country.

Vasileios XanthisDepartment of Molecular Biology & Genetics, Democritus University of Thrace, 68100 Alexandroupolis, Greece.ORCID 0000-0002-3525-193X
Theodora MantsoDepartment of Molecular Biology & Genetics, Democritus University of Thrace, 68100 Alexandroupolis, Greece.
Anna DimtsiDepartment of Molecular Biology & Genetics, Democritus University of Thrace, 68100 Alexandroupolis, Greece.
Aglaia PappaDepartment of Molecular Biology & Genetics, Democritus University of Thrace, 68100 Alexandroupolis, Greece.ORCID 0000-0003-0913-4315
Vasiliki E FadouloglouDepartment of Molecular Biology & Genetics, Democritus University of Thrace, 68100 Alexandroupolis, Greece.ORCID 0000-0003-1794-7914
Democritus University of Thrace · GR

Funding

Operational Program "Competitiveness, Entrepreneurship & Innovation" (EPAnEK) MIS Code 5047285
6 · The paper itself

Abstract

The superfamily of human aldehyde dehydrogenases (hALDHs) consists of 19 isoenzymes which are critical for several physiological and biosynthetic processes and play a major role in the organism's detoxification via the NAD(P) dependent oxidation of numerous endogenous and exogenous aldehyde substrates to their corresponding carboxylic acids. Over the last decades, ALDHs have been the subject of several studies as it was revealed that their differential expression patterns in various cancer types are associated either with carcinogenesis or promotion of cell survival. Here, we attempt to provide a thorough review of hALDHs' diverse functions and 3D structures with particular emphasis on their role in cancer pathology and resistance to chemotherapy. We are especially interested in findings regarding the association of structural features and their changes with effects on enzymes' functionalities. Moreover, we provide an updated outline of the hALDHs inhibitors utilized in experimental or clinical settings for cancer therapy. Overall, this review aims to provide a better understanding of the impact of ALDHs in cancer pathology and therapy from a structural perspective.

Indexed as

3D structurealdehyde dehydrogenases (ALDHs)cancerchemotherapy resistancecrystallinsinhibitorspost-translational modificationsquaternary associationtopology

Identifiers

PMID37686694
PMCPMC10650815
OpenAlexW4386423084

What OpenQuestion 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 OpenQuestion graph.