Evidence map›Paper›PMID 25294000›Full record

ReviewTrends in pharmacological sciences2014

AGXT2: a promiscuous aminotransferase.

Roman N Rodionov, Natalia Jarzebska, Norbert Weiss, Steven R Lentz

Abstract readReview
In one paragraph

Review in Trends in pharmacological sciences, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed, 1 pooled it
3.8field-weighted citation impact, top 6% 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

42 citing papers in PubMed, 1 synthesis or guideline pooled it, 74 citations in OpenAlex.

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  11. SDMA as a marker and mediator in cerebrovascular disease.Clinical science (London, England : 1979) · 2024
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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

4 authors at 2 institutions in 2 countries.

Roman N RodionovUniversity Center for Vascular Medicine and Department of Internal Medicine, Division of Angiology, University Hospital 'Carl Gustav Carus', Technische Universität Dresden, Fetscherstrasse 42, 01307 Dresden, Germany.
Natalia JarzebskaUniversity Hospital 'Carl Gustav Carus', Technische Universität Dresden, Fetscherstrasse 42, 01307 Dresden, Germany.
Norbert WeissUniversity Center for Vascular Medicine and Department of Internal Medicine, Division of Angiology, University Hospital 'Carl Gustav Carus', Technische Universität Dresden, Fetscherstrasse 42, 01307 Dresden, Germany.
Steven R LentzDepartment of Internal Medicine, University of Iowa Carver College of Medicine, 200 Hawkins Drive, Iowa City, IA 52242, USA. Electronic address: steven-lentz@uiowa.edu.
TU Dresden · DEUniversity of Iowa · US

Funding

Transgenic and knockout animalP01NS024621 · NINDS · UNIVERSITY OF IOWA · PI FARACI, FRANK M · 1987 to 2012
$14.9M
Vascular Mechanisms in Homocysteinemia and AtherosclerosisR01HL063943 · NHLBI · UNIVERSITY OF IOWA · PI LENTZ, STEVEN R · 2000 to 2012
$4.0M
NHLBI NIH HHS R01 HL063943NINDS NIH HHS P01 NS024621
6 · The paper itself

Abstract

Alanine-glyoxylate aminotransferase 2 (AGXT2) is a multifunctional mitochondrial aminotransferase that was first identified in 1978. The physiological importance of AGXT2 was largely overlooked for three decades because AGXT2 is less active in glyoxylate metabolism than AGXT1, the enzyme that is deficient in primary hyperoxaluria type I. Recently, several novel functions of AGXT2 have been 'rediscovered' in the setting of modern genomic and metabolomic studies. It is now apparent that AGXT2 has multiple substrates and products and that altered AGXT2 activity may contribute to the pathogenesis of cardiovascular, renal, neurological, and hematological diseases. This article reviews the biochemical properties and physiological functions of AGXT2, its unique role at the intersection of key mitochondrial pathways, and its potential as a drug target.

Indexed as

AnimalsHumansTransaminasesAlanine-glyoxylate transaminaseTransaminasesalanineamino acid metabolismaminotransferaseglyoxylatemethylarginine

Identifiers

PMID25294000
PMCPMC4254113
OpenAlexW2024077658

What OpenQuestion holds

Textmetadata
LicenceTDM
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.