Evidence map›Paper›PMID 32144208›Full record

ReviewThe Journal of biological chemistry2020

Evolution, expression, and substrate specificities of aldehyde oxidase enzymes in eukaryotes.

Mineko Terao, Enrico Garattini, Maria João Romão, Silke Leimkühler

Open access · hybridAbstract readReview
In one paragraph

Review in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
5.0field-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

32 citing papers in PubMed, 64 citations in OpenAlex.

  1. Soft drugs: design principles and topical applications.Nature reviews. Drug discovery · 2026
    Review
  2. Article
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  4. Article
  5. Article
  6. Review
  7. Article
  8. NADNature metabolism · 2025
    Review
  9. Article
  10. Article
  11. Review
  12. Review
  13. Review
  14. Article
  15. Regulation of and challenges in targeting NADNature reviews. Molecular cell biology · 2024
    Review
  16. Requirements for the biogenesis of [2Fe-2S] proteins in the human and yeast cytosol.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  17. Article
  18. Article
  19. Review
  20. Review
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 3 institutions in 3 countries.

Mineko TeraoLaboratory of Molecular Biology, Istituto di Ricerche Farmacologiche Mario Negri IRCCS, via La Masa 19, 20156 Milano, Italy.
Enrico GarattiniLaboratory of Molecular Biology, Istituto di Ricerche Farmacologiche Mario Negri IRCCS, via La Masa 19, 20156 Milano, Italy.
Maria João RomãoUCIBIO-Applied Biomolecular Sciences Unit, Departamento de Química, Faculdade de Ciências e Tecnologia, Universidade NOVA de Lisboa, 2829-516 Caparica, Portugal.
Silke LeimkühlerDepartment of Molecular Enzymology, Institute of Biochemistry and Biology, University of Potsdam, Karl-Liebknecht-Str. 24-25, 14476 Potsdam, Germany. Electronic address: sleim@uni-potsdam.de.
Mario Negri Institute for Pharmacological Research · ITUniversidade Nova de Lisboa · PTUniversity of Potsdam · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Aldehyde oxidases (AOXs) are a small group of enzymes belonging to the larger family of molybdo-flavoenzymes, along with the well-characterized xanthine oxidoreductase. The two major types of reactions that are catalyzed by AOXs are the hydroxylation of heterocycles and the oxidation of aldehydes to their corresponding carboxylic acids. Different animal species have different complements of

Indexed as

Evolution, MolecularAldehyde OxidaseAnimalsHumansLiverSubstrate SpecificityAldehyde Oxidase2Fe-2S clusteraldehyde oxidase (AOX)drug metabolismenzyme evolutionflavin adenine dinucleotide (FAD)flavoproteiniron-sulfur proteinmetal-containing enzymemetalloenzymemolybdenummolybdenum cofactor (Moco)molybdo-flavoenzymemouseoxidaseoxygen radicalsxenobiotic

Identifiers

PMID32144208
PMCPMC7170512
OpenAlexW3010037932

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.