Evidence map›Paper›PMID 29784877›Full record

ArticleThe Journal of biological chemistry2018

Adapting to oxygen: 3-Hydroxyanthrinilate 3,4-dioxygenase employs loop dynamics to accommodate two substrates with disparate polarities.

Yu Yang, Fange Liu, 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 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.8field-weighted citation impact, top 31% 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

11 citing papers in PubMed, 18 citations in OpenAlex.

  1. Characterization of the substrate specificity and regioselectivity of ring-cleavage of Pseudomonas putida DLL-E4 hydroquinone 1,2-dioxygenase (PnpC1C2).Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2025
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  9. Observing 3-hydroxyanthranilate-3,4-dioxygenase in action through a crystalline lens.Proceedings of the National Academy of Sciences of the United States of America · 2020
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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

3 authors at 2 institutions in 1 country.

Yu YangFrom the Department of Chemistry, University of Texas at San Antonio, San Antonio, Texas 78249 and.
Fange Liuthe Department of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104 liufg@pennmedicine.upenn.edu.ORCID 0000-0002-3235-9996
Aimin LiuFrom the Department of Chemistry, University of Texas at San Antonio, San Antonio, Texas 78249 and Feradical@utsa.edu.ORCID 0000-0002-4182-8176
The University of Texas at San Antonio · USUniversity of Pennsylvania · US

Funding

X-ray Absorption Spectroscopy (XAS) pp.711-759P41GM103393 · NIGMS · STANFORD UNIVERSITY · PI HODGSON, KEITH O · 2012 to 2019
$30.6M
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 P41 GM103393NIGMS NIH HHS R01 GM107529NIGMS NIH HHS R01 GM108988NIMH NIH HHS R21 MH107985
6 · The paper itself

Abstract

3-Hydroxyanthranilate 3,4-dioxygenase (HAO) is an iron-dependent protein that activates O

Indexed as

3-Hydroxyanthranilic AcidAmino Acid SequenceBacterial ProteinsCatalysisCatalytic DomainCrystallography, X-RayCupriavidusDioxygenasesLigandsModels, MolecularMutagenesis, Site-DirectedMutationOxygenProtein ConformationSequence HomologySubstrate Specificity3-Hydroxyanthranilic AcidBacterial ProteinsDioxygenasesLigandsOxygenconformational changecrystal structuredioxygenaseenzyme structureExtradiol dioxygenasehydrophobicityironNonheme iron enzymeOxygen activationoxygen bindingTryptophan-kynurenine pathway

Identifiers

PMID29784877
PMCPMC6036192
OpenAlexW2804806832

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.