Evidence map›Paper›PMID 23263164›Full record

ArticleCellular and molecular life sciences : CMLS2013

Structure and evolution of vertebrate aldehyde oxidases: from gene duplication to gene suppression.

Mami Kurosaki, Marco Bolis, Maddalena Fratelli, Maria Monica Barzago, Linda Pattini, Gemma Perretta, Mineko Terao, Enrico Garattini

Open access · greenAbstract read
In one paragraph

Article in Cellular and molecular life sciences : CMLS, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed, 1 pooled it
1.2field-weighted citation impact, top 20% 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

18 citing papers in PubMed, 1 synthesis or guideline pooled it, 62 citations in OpenAlex.

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  17. Insights into the structural determinants of substrate specificity and activity in mouse aldehyde oxidases.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2015
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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

8 authors at 3 institutions in 1 country.

Mami KurosakiLaboratory of Molecular Biology, Istituto di Ricerche Farmacologiche "Mario Negri", via La Masa 19, 20156, Milan, Italy.
Marco Bolis
Maddalena Fratelli
Maria Monica Barzago
Linda Pattini
Gemma Perretta
Mineko Terao
Enrico Garattini
Mario Negri Institute for Pharmacological Research · ITInstitute of Cell Biology and Neurobiology · ITPolitecnico di Milano · IT

Funding

Telethon GGP13081
6 · The paper itself

Abstract

Aldehyde oxidases (AOXs) and xanthine dehydrogenases (XDHs) belong to the family of molybdo-flavoenzymes. Although AOXs are not identifiable in fungi, these enzymes are represented in certain protists and the majority of plants and vertebrates. The physiological functions and substrates of AOXs are unknown. Nevertheless, AOXs are major drug metabolizing enzymes, oxidizing a wide range of aromatic aldehydes and heterocyclic compounds of medical/toxicological importance. Using genome sequencing data, we predict the structures of AOX genes and pseudogenes, reconstructing their evolution. Fishes are the most primitive organisms with an AOX gene (AOXα), originating from the duplication of an ancestral XDH. Further evolution of fishes resulted in the duplication of AOXα into AOXβ and successive pseudogenization of AOXα. AOXβ is maintained in amphibians and it is the likely precursors of reptilian, avian, and mammalian AOX1. Amphibian AOXγ is a duplication of AOXβ and the likely ancestor of reptilian and avian AOX2, which, in turn, gave rise to mammalian AOX3L1. Subsequent gene duplications generated the two mammalian genes, AOX3 and AOX4. The evolution of mammalian AOX genes is dominated by pseudogenization and deletion events. Our analysis is relevant from a structural point of view, as it provides information on the residues characterizing the three domains of each mammalian AOX isoenzyme. We cloned the cDNAs encoding the AOX proteins of guinea pig and cynomolgus monkeys, two unique species as to the evolution of this enzyme family. We identify chimeric RNAs from the human AOX3 and AOX3L1 pseudogenes with potential to encode a novel microRNA.

Indexed as

Evolution, MolecularAldehyde OxidaseAmino Acid SequenceAnimalsGene DuplicationGene Expression RegulationGenomeHumansInvertebratesMicroRNAsMolecular Sequence DataPhylogenyProtein IsoformsPseudogenesSequence AlignmentVertebratesAldehyde OxidaseMicroRNAsProtein IsoformsXanthine Dehydrogenase

Identifiers

PMID23263164
PMCPMC11113236
OpenAlexW2014797220

What OpenQuestion holds

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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.