Evidence map›Paper›PMID 29703752›Full record

ArticleThe Journal of biological chemistry2018

Reassignment of the human aldehyde dehydrogenase ALDH8A1 (ALDH12) to the kynurenine pathway in tryptophan catabolism.

Ian Davis, Yu Yang, Daniel Wherritt, Aimin Liu

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.1field-weighted citation impact, top 27% 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, 35 citations in OpenAlex.

  1. Review
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  15. Article
  16. Kynurenine pathway, NADExperimental gerontology · 2020
    Review
  17. Article
  18. Retinoic acid signaling pathways.Development (Cambridge, England) · 2019
    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 1 institution in 1 country.

Ian DavisFrom the Department of Chemistry, University of Texas, San Antonio, Texas 78249.
Yu YangFrom the Department of Chemistry, University of Texas, San Antonio, Texas 78249.
Daniel WherrittFrom the Department of Chemistry, University of Texas, San Antonio, Texas 78249.
Aimin LiuFrom the Department of Chemistry, University of Texas, San Antonio, Texas 78249 Feradical@utsa.edu.ORCID 0000-0002-4182-8176
The University of Texas at San Antonio · US

Funding

RCMI Center for Interdiscplinary Health Research CIHRG12MD007591 · NIMHD · UNIVERSITY OF TEXAS SAN ANTONIO · PI PERRY, GEORGE · 2012 to 2016
$10.4M
Heme-dependent chemistry in tyrosine oxidation: Diversity Supplement on 5R01GM108988-08 for supporting Samuel MontoyaR01GM108988 · NIGMS · UNIVERSITY OF TEXAS SAN ANTONIO · PI LIU, AIMIN · 2014 to 2025
$4.2M
NF-kappaB Regulation by Human PirinR01GM107529 · NIGMS · UNIVERSITY OF TEXAS SAN ANTONIO · PI LI, JIAN-DONG, LIU, AIMIN · 2014 to 2017
$1.0M
Kynurenine metabolites and depression: An in vitro and ex vivo studyR21MH107985 · NIMH · UNIVERSITY OF TEXAS SAN ANTONIO · PI LIU, AIMIN, SHAMSI, SHAHAB AHMED · 2016 to 2017
$420k
NIGMS NIH HHS R01 GM107529NIGMS NIH HHS R01 GM108988NIMHD NIH HHS G12 MD007591NIMH NIH HHS R21 MH107985
6 · The paper itself

Abstract

The kynurenine pathway is the primary route for l-tryptophan degradation in mammals. Intermediates and side products of this pathway are involved in immune response and neurodegenerative diseases. This makes the study of enzymes, especially those from mammalian sources, of the kynurenine pathway worthwhile. Recent studies on a bacterial version of an enzyme of this pathway, 2-aminomuconate semialdehyde (2-AMS) dehydrogenase (AMSDH), have provided a detailed understanding of the catalytic mechanism and identified residues conserved for muconate semialdehyde recognition and activation. Findings from the bacterial enzyme have prompted the reconsideration of the function of a previously identified human aldehyde dehydrogenase, ALDH8A1 (or ALDH12), which was annotated as a retinal dehydrogenase based on its ability to preferentially oxidize 9-

Indexed as

MutationAldehyde DehydrogenaseAmino Acid SequenceAmino Acid SubstitutionHumansKynurenineProtein ConformationSequence HomologySubstrate SpecificityTryptophanAldehyde DehydrogenaseALDH8A1 protein, humanKynurenineTryptophan2-aminomuconate semialdehyde dehydrogenasealdehyde dehydrogenasebiodegradationkynurenine pathwayNAD biosynthesisneurological diseaseretinal dehydrogenaseretinal metabolismserotonintryptophan catabolism

Identifiers

PMID29703752
PMCPMC6016481
OpenAlexW2799572336

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.