Evidence map›Paper›PMID 32234764›Full record

ArticleThe Journal of biological chemistry2020

Roles of active-site residues in catalysis, substrate binding, cooperativity, and the reaction mechanism of the quinoprotein glycine oxidase.

Kyle J Mamounis, Erik T Yukl, Victor L Davidson

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 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.2field-weighted citation impact, top 51% 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

2 citing papers in PubMed, 7 citations in OpenAlex.

  1. Review
  2. 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

3 authors at 2 institutions in 1 country.

Kyle J MamounisBurnett School of Biomedical Sciences, College of Medicine, University of Central Florida, Orlando, Florida 32827.ORCID 0000-0002-5489-0198
Erik T YuklDepartment of Chemistry and Biochemistry, New Mexico State University, Las Cruces, New Mexico 88003.ORCID 0000-0001-6519-6938
Victor L DavidsonBurnett School of Biomedical Sciences, College of Medicine, University of Central Florida, Orlando, Florida 32827 victor.davidson@ucf.edu.ORCID 0000-0002-1966-7302
University of Central Florida · USNew Mexico State University · US

Funding

Mechanisms of Catalysis and Cofactor Biosynthesis of Redox Enzymes with Unusual CofactorsR35GM130173 · NIGMS · UNIVERSITY OF CENTRAL FLORIDA · PI DAVIDSON, VICTOR L · 2019 to 2023
$1.8M
NIGMS NIH HHS R35 GM130173
6 · The paper itself

Abstract

The quinoprotein glycine oxidase from the marine bacterium

Indexed as

Amino Acid OxidoreductasesAmino Acid SubstitutionBacterial ProteinsCatalysisCatalytic DomainCrystallography, X-RayMutation, MissensePseudoalteromonasSubstrate SpecificityAmino Acid OxidoreductasesBacterial Proteinsglycine oxidaseacid-base chemistrycooperativitycysteine tryptophylquinoneenzyme catalysisenzyme kineticsenzyme mechanismGoxALodA-like proteinoxidasequinonesite-directed mutagenesisstructure-function

Identifiers

PMID32234764
PMCPMC7212659
OpenAlexW3014561961

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.