Evidence map›Paper›PMID 28272331›Full record

ReviewBiology2017

Ornithine Aminotransferase, an Important Glutamate-Metabolizing Enzyme at the Crossroads of Multiple Metabolic Pathways.

Antonin Ginguay, Luc Cynober, Emmanuel Curis, Ioannis Nicolis

Open access · goldAbstract readReview
In one paragraph

Review in Biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 91 papers.

0numbers the graph read from it
0cells of the map it votes in
91citing papers in PubMed
6.7field-weighted citation impact, top 3% 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

91 citing papers in PubMed, 135 citations in OpenAlex.

  1. Article
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  8. A metabolic basis for motor deficits in mice lacking BCKDK.The Journal of nutritional biochemistry · 2026
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31 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

4 authors at 1 institution in 1 country.

Antonin GinguayClinical Chemistry, Cochin Hospital, GH HUPC, AP-HP, 75014 Paris, France. antonin.ginguay@gmail.com.
Luc CynoberClinical Chemistry, Cochin Hospital, GH HUPC, AP-HP, 75014 Paris, France. luc.cynober@parisdescartes.fr.
Emmanuel CurisLaboratoire de biomathématiques, plateau iB², Faculté de Pharmacie, Université Paris Descartes, 75006 Paris, France. emmanuel.curis@parisdescartes.fr.
Ioannis NicolisLaboratoire de biomathématiques, plateau iB², Faculté de Pharmacie, Université Paris Descartes, 75006 Paris, France. ioannis.nicolis@parisdescartes.fr.
Délégation Paris 5 · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ornithine δ-aminotransferase (OAT, E.C. 2.6.1.13) catalyzes the transfer of the δ-amino group from ornithine (Orn) to α-ketoglutarate (aKG), yielding glutamate-5-semialdehyde and glutamate (Glu), and vice versa. In mammals, OAT is a mitochondrial enzyme, mainly located in the liver, intestine, brain, and kidney. In general, OAT serves to form glutamate from ornithine, with the notable exception of the intestine, where citrulline (Cit) or arginine (Arg) are end products. Its main function is to control the production of signaling molecules and mediators, such as Glu itself, Cit, GABA, and aliphatic polyamines. It is also involved in proline (Pro) synthesis. Deficiency in OAT causes gyrate atrophy, a rare but serious inherited disease, a further measure of the importance of this enzyme.

Indexed as

glutamategyrate atrophyornithineornithine aminotransferase

Identifiers

PMID28272331
PMCPMC5372011
OpenAlexW2594854790

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.