Evidence map›Paper›PMID 28618168›Full record

ArticleThe FEBS journal2017

Streptococcus pyogenes quinolinate-salvage pathway-structural and functional studies of quinolinate phosphoribosyl transferase and NH

William T Booth, Trevor L Morris, David P Mysona, Milan J Shah, Linda K Taylor, Taylor W Karlin, Kathryn Clary, Karolina A Majorek, Lesa R Offermann, Maksymilian Chruszcz

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

Article in The FEBS journal, 2017. 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
0.3field-weighted citation impact, top 40% 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, 8 citations in OpenAlex.

  1. Article
  2. Article
  3. 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

10 authors at 2 institutions in 1 country.

William T BoothDepartment of Chemistry and Biochemistry, University of South Carolina, Columbia, SC, USA.
Trevor L MorrisDepartment of Chemistry and Biochemistry, University of South Carolina, Columbia, SC, USA.
David P MysonaDepartment of Chemistry and Biochemistry, University of South Carolina, Columbia, SC, USA.
Milan J ShahDepartment of Chemistry and Biochemistry, University of South Carolina, Columbia, SC, USA.
Linda K TaylorDepartment of Chemistry and Biochemistry, University of South Carolina, Columbia, SC, USA.
Taylor W KarlinDepartment of Chemistry and Biochemistry, University of South Carolina, Columbia, SC, USA.
Kathryn ClaryDepartment of Chemistry and Biochemistry, University of South Carolina, Columbia, SC, USA.
Karolina A MajorekDepartment of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, VA, USA.
Lesa R OffermannDepartment of Chemistry and Biochemistry, University of South Carolina, Columbia, SC, USA.
Maksymilian ChruszczDepartment of Chemistry and Biochemistry, University of South Carolina, Columbia, SC, USA.
University of South Carolina · USUniversity of Virginia · US

Funding

Metallopolymer and Antibiotic Bioconjugates against Multidrug Resistant BacteriaR01AI120987 · NIAID · UNIVERSITY OF SOUTH CAROLINA AT COLUMBIA · PI TANG, CHUANBING · 2016 to 2019
$1.4M
NIAID NIH HHS R01 AI120987
6 · The paper itself

Abstract

Streptococcus pyogenes, also known as Group A Strep (GAS), is an obligate human pathogen that is responsible for millions of infections and numerous deaths per year. Infection manifestations can range from simple, acute pharyngitis to more complex, necrotizing fasciitis. To date, most treatments for GAS infections involve the use of common antibiotics including tetracycline and clindamycin. Unfortunately, new strains have been identified that are resistant to these drugs, therefore, new targets must be identified to treat drug-resistant strains. This work is focused on the structural and functional characterization of three proteins: spNadC, spNadD, and spNadE. These enzymes are involved in the biosynthesis of nicotinamide adenine dinucleotide (NAD ENZYMES: Quinolinate phosphoribosyltransferase: EC2.4.2.19 and NAD synthetase: EC6.3.1.5. DATABASE: Protein structures for spNadC, spNadC

Indexed as

Models, MolecularAdenosine TriphosphateAmide SynthasesApoenzymesBacterial ProteinsBinding SitesCatalytic DomainCluster AnalysisComputational BiologyCrystallography, X-RayDimerizationGene DeletionNicotinamide-Nucleotide AdenylyltransferaseNicotinate-Nucleotide Diphosphorylase (Carboxylating)PentosyltransferasesProtein ConformationAdenosine TriphosphateAmide SynthasesApoenzymesBacterial ProteinsNAD+ synthaseNicotinamide-Nucleotide AdenylyltransferaseNicotinate-Nucleotide Diphosphorylase (Carboxylating)nicotinic acid mononucleotide adenylyltransferasePentosyltransferasesQuinolinic AcidRecombinant ProteinsNAD+ biosynthesisNH3-dependent NAD+ synthetasequinolinate phosphoribosyltansferasequinolinate- salvage pathway

Identifiers

PMID28618168
PMCPMC5551413
OpenAlexW2624931521

What OpenQuestion holds

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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.