Evidence map›Paper›PMID 32601061›Full record

ArticleThe Journal of biological chemistry2020

Characterization of the nonheme iron center of cysteamine dioxygenase and its interaction with substrates.

Yifan Wang, Ian Davis, Yan Chan, Sunil G Naik, Wendell P Griffith, Aimin Liu

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

24 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
  2. A Dinuclear Iron(II) Persulfide Complex Reacts with OJournal of the American Chemical Society · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Influence of the second coordination sphere on OJournal of inorganic biochemistry · 2025
    Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Spectroscopic, electrochemical, and kinetic trends in Fe(III)-thiolate disproportionation near physiologic pH.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2024
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. OvoAChemical science · 2022
    Article
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

6 authors at 2 institutions in 1 country.

Yifan WangDepartment of Chemistry, University of Texas at San Antonio, Texas, USA.ORCID 0000-0003-0378-2469
Ian DavisDepartment of Chemistry, University of Texas at San Antonio, Texas, USA.ORCID 0000-0002-1566-4972
Yan ChanDepartment of Chemistry, Georgia State University, Atlanta, Georgia, USA.
Sunil G NaikDepartment of Chemistry, University of Texas at San Antonio, Texas, USA.
Wendell P GriffithDepartment of Chemistry, University of Texas at San Antonio, Texas, USA.ORCID 0000-0003-2633-6103
Aimin LiuDepartment of Chemistry, University of Texas at San Antonio, Texas, USA Feradical@utsa.edu.ORCID 0000-0002-4182-8176
Georgia State University · USThe 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
NIGMS NIH HHS R01 GM108988NIMHD NIH HHS G12 MD007591
6 · The paper itself

Abstract

Cysteamine dioxygenase (ADO) has been reported to exhibit two distinct biological functions with a nonheme iron center. It catalyzes oxidation of both cysteamine in sulfur metabolism and N-terminal cysteine-containing proteins or peptides, such as regulator of G protein signaling 5 (RGS5). It thereby preserves oxygen homeostasis in a variety of physiological processes. However, little is known about its catalytic center and how it interacts with these two types of primary substrates in addition to O

Indexed as

AnimalsCatalytic DomainCysteamineDioxygenasesHumansMiceModels, MolecularOxygenPeptidesProtein BindingRGS ProteinsSubstrate SpecificityCysteaminecysteamine dioxygenaseDioxygenasesOxygenPeptidesRGS5 protein, humanRGS Proteinscysteamine dioxygenase (ADO)cysteine dioxygenase (CDO)dioxygenaseelectron paramagnetic resonance (EPR)EPR spectroscopymetalloenzymenitric oxideoxygen activationoxygen bindingoxygen sensingsulfursulfur metabolismthiolthiol dioxygenasethiol regulation

Identifiers

PMID32601061
PMCPMC7450127
OpenAlexW3038245377

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.