Evidence map›Paper›PMID 29077008›Full record

ReviewInternational journal of molecular sciences2017

The Glycosyltransferases of LPS Core: A Review of Four Heptosyltransferase Enzymes in Context.

Joy M Cote, Erika A Taylor

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

22 citing papers in PubMed, 49 citations in OpenAlex.

  1. Article
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  5. The Journal of organic chemistry · 2024
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  12. Construction of the waaF Subunit and DNA Vaccine AgainstFrontiers in veterinary science · 2022
    Article
  13. Spontaneous Resistance ofFrontiers in microbiology · 2022
    Article
  14. Review
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  18. Opposites Attract:Biochemistry · 2020
    Article
  19. GTDB: an integrated resource for glycosyltransferase sequences and annotations.Database : the journal of biological databases and curation · 2020
    Article
  20. 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

2 authors at 1 institution in 1 country.

Joy M CoteDepartment of Chemistry, Wesleyan University, Middletown, CT 06459, USA. jcote@wesleyan.edu.
Erika A TaylorDepartment of Chemistry, Wesleyan University, Middletown, CT 06459, USA. eataylor@wesleyan.edu.ORCID 0000-0001-5598-640X
Wesleyan University · US

Funding

Inhibition of HeptosyltransferaseI for the treatment of Gram-negative bacterial infectionR15AI119907 · NIAID · WESLEYAN UNIVERSITY · PI TAYLOR, ERIKA A · 2015 to 2015
$493k
NIAID NIH HHS R15 AI119907
6 · The paper itself

Abstract

Bacterial antibiotic resistance is a rapidly expanding problem in the world today. Functionalization of the outer membrane of Gram-negative bacteria provides protection from extracellular antimicrobials, and serves as an innate resistance mechanism. Lipopolysaccharides (LPS) are a major cell-surface component of Gram-negative bacteria that contribute to protecting the bacterium from extracellular threats. LPS is biosynthesized by the sequential addition of sugar moieties by a number of glycosyltransferases (GTs). Heptosyltransferases catalyze the addition of multiple heptose sugars to form the core region of LPS; there are at most four heptosyltransferases found in all Gram-negative bacteria. The most studied of the four is HepI. Cells deficient in HepI display a truncated LPS on their cell surface, causing them to be more susceptible to hydrophobic antibiotics. HepI-IV are all structurally similar members of the GT-B structural family, a class of enzymes that have been found to be highly dynamic. Understanding conformational changes of heptosyltransferases are important to efficiently inhibiting them, but also contributing to the understanding of all GT-B enzymes. Finding new and smarter methods to inhibit bacterial growth is crucial, and the Heptosyltransferases may provide an important model for how to inhibit many GT-B enzymes.

Indexed as

AnimalsCatalytic DomainGlycosyltransferasesHumansLipopolysaccharidesModels, MolecularSequence HomologyStructure-Activity RelationshipGlycosyltransferasesheptosyltransferaseLipopolysaccharidesglycosyltransferaseGT-Bheptosyltransferaseinhibitor designlipopolysaccharideLPSprotein dynamics

Identifiers

PMID29077008
PMCPMC5713226
OpenAlexW2767158766

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.