Evidence map›Paper›PMID 32949987›Full record

ArticleJournal of inorganic biochemistry2020

A family of structural and functional models for the active site of a unique dioxygenase: Acireductone dioxygenase (ARD).

Glenn A Blade, Riffat Parveen, Jennifer L Jaimes, Wrenell Ilustre, Diego Saldaña, Denisa A Ivan, Vincent M Lynch, Thomas R Cundari, Santiago Toledo

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of inorganic biochemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.1field-weighted citation impact, top 62% 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

3 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
  2. Article
  3. Light-induced ODalton transactions (Cambridge, England : 2003) · 2023
    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

9 authors at 3 institutions in 1 country.

Glenn A BladeDepartment of Chemistry, St. Edward's University, 3001 South Congress Ave, Austin, TX 78704, United States of America.
Riffat ParveenDepartment of Chemistry, CASCaM, University of North Texas, 1508 W. Mulberry Street, Denton, TX 76203, United States of America.
Jennifer L JaimesDepartment of Chemistry, St. Edward's University, 3001 South Congress Ave, Austin, TX 78704, United States of America.
Wrenell IlustreDepartment of Chemistry, St. Edward's University, 3001 South Congress Ave, Austin, TX 78704, United States of America.
Diego SaldañaDepartment of Chemistry, St. Edward's University, 3001 South Congress Ave, Austin, TX 78704, United States of America.
Denisa A IvanDepartment of Chemistry, St. Edward's University, 3001 South Congress Ave, Austin, TX 78704, United States of America.
Vincent M LynchDepartment of Chemistry, The University of Texas at Austin, 120 Inner Campus Dr Stop G2500, Austin, TX 78712, United States of America.
Thomas R CundariDepartment of Chemistry, CASCaM, University of North Texas, 1508 W. Mulberry Street, Denton, TX 76203, United States of America.
Santiago ToledoDepartment of Chemistry, St. Edward's University, 3001 South Congress Ave, Austin, TX 78704, United States of America. Electronic address: stoledoc@stedwards.edu.
St. Edward's University · USUniversity of North Texas · USThe University of Texas at Austin · US

Funding

A Biomimetic Approach to Elucidating the Role in Disease of the Oxygenase Enzyme Acireductone Dioxygenase (ARD)SC2GM130438 · NIGMS · ST. EDWARD'S UNIVERSITY · PI TOLEDO CARRION, SANTIAGO ANDRES · 2020 to 2022
$331k
NIGMS NIH HHS SC2 GM130438
6 · The paper itself

Abstract

We report the synthesis and biomimetic activity of a family of model complexes with relevance to acireductone dioxygenase (ARD), an enzyme that displays dual function based on metal identity found in the methionine salvage pathway (MSP). Three complexes with related structural motifs were synthesized and characterized derived from phenolate, and pyridine N

Indexed as

BiomimeticsCatalytic DomainDensity Functional TheoryDioxygenasesModels, MolecularNickelOxidation-ReductionProof of Concept StudyProtein ConformationStructure-Activity RelationshipThermodynamicsaci-reductone oxidase (CO-forming)DioxygenasesNickelComputational studiesInorganic chemistryMetalloenzyemesModeling chemistryOxygenasesSchiff-base Ni coordination complexes

Identifiers

PMID32949987
PMCPMC7680382
OpenAlexW3085004807

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.