Evidence map›Paper›PMID 12578558›Full record

ReviewThe Biochemical journal2003

Mammalian molybdo-flavoenzymes, an expanding family of proteins: structure, genetics, regulation, function and pathophysiology.

Enrico Garattini, Ralf Mendel, Maria João Romão, Richard Wright, Mineko Terao

Open access · bronzeAbstract readReview
In one paragraph

Review in The Biochemical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.

0numbers the graph read from it
0cells of the map it votes in
71citing papers in PubMed
12.3field-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

71 citing papers in PubMed, 244 citations in OpenAlex.

  1. Trial
  2. Structure of human aldehyde oxidase under tris(2-carboxyethyl)phosphine reducing conditions.Acta crystallographica. Section F, Structural biology communications · 2026
    Article
  3. Article
  4. Review
  5. Metabolomic Profiling Identifies Key Metabolites and Defense Pathways inInternational journal of molecular sciences · 2025
    Article
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  7. Article
  8. Review
  9. Article
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  11. Article
  12. Article
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  17. Article
  18. Review
  19. Article
  20. Time Course of Aldehyde Oxidase and Why It Is Nonlinear.Drug metabolism and disposition: the biological fate of chemicals · 2019
    Article

11 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

5 authors at 3 institutions in 3 countries.

Enrico GarattiniLaboratory of Molecular Biology, Istituto di Ricerche Farmacologiche Mario Negri, via Eritrea 62, 20157 Milan, Italy. egarattini@marionegri.it
Ralf Mendel
Maria João Romão
Richard Wright
Mineko Terao
Mario Negri Institute for Pharmacological Research · ITTechnische Universität Braunschweig · DEUniversidade Nova de Lisboa · PT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The molybdo-flavoenzymes are structurally related proteins that require a molybdopterin cofactor and FAD for their catalytic activity. In mammals, four enzymes are known: xanthine oxidoreductase, aldehyde oxidase and two recently described mouse proteins known as aldehyde oxidase homologue 1 and aldehyde oxidase homologue 2. The present review article summarizes current knowledge on the structure, enzymology, genetics, regulation and pathophysiology of mammalian molybdo-flavoenzymes. Molybdo-flavoenzymes are structurally complex oxidoreductases with an equally complex mechanism of catalysis. Our knowledge has greatly increased due to the recent crystallization of two xanthine oxidoreductases and the determination of the amino acid sequences of many members of the family. The evolution of molybdo-flavoenzymes can now be traced, given the availability of the structures of the corresponding genes in many organisms. The genes coding for molybdo-flavoenzymes are expressed in a cell-specific fashion and are controlled by endogenous and exogenous stimuli. The recent cloning of the genes involved in the biosynthesis of the molybdenum cofactor has increased our knowledge on the assembly of the apo-forms of molybdo-flavoproteins into the corresponding holo-forms. Xanthine oxidoreductase is the key enzyme in the catabolism of purines, although recent data suggest that the physiological function of this enzyme is more complex than previously assumed. The enzyme has been implicated in such diverse pathological situations as organ ischaemia, inflammation and infection. At present, very little is known about the pathophysiological relevance of aldehyde oxidase, aldehyde oxidase homologue 1 and aldehyde oxidase homologue 2, which do not as yet have an accepted endogenous substrate.

Indexed as

Aldehyde OxidaseAldehyde OxidoreductasesAmino Acid SequenceAnimalsEvolution, MolecularFlavoproteinsHumansMiceMolecular Sequence DataMolybdenumOrgan SpecificityOxidoreductasesXanthine OxidaseAldehyde Oxidasealdehyde oxidase homolog 2, mouseAldehyde OxidoreductasesAox3 protein, mouseFlavoproteinsMolybdenumOxidoreductasesXanthine Oxidase

Identifiers

PMID12578558
PMCPMC1223366
OpenAlexW1995023151

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.