Evidence map›Paper›PMID 34872657›Full record

ReviewAdvances in carbohydrate chemistry and biochemistry2021

Recent advances on glycosyltransferases involved in the biosynthesis of the proteoglycan linkage region.

Jia Gao, Xuefei Huang

Abstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Advances in carbohydrate chemistry and biochemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
–field-weighted citation impact
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

5 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. Review
  5. 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.

Jia GaoDepartment of Chemistry, Michigan State University, East Lansing, MI, United States; Institute for Quantitative Health Science and Engineering, Michigan State University, East Lansing, MI, United States.
Xuefei HuangDepartment of Chemistry, Michigan State University, East Lansing, MI, United States; Institute for Quantitative Health Science and Engineering, Michigan State University, East Lansing, MI, United States; Department of Biomedical Engineering, Michigan State University, East Lansing, MI, United States. Electronic address: huangxu2@msu.edu.

Funding

Homogeneous Heparan Sulfate Glycopeptides: Synthetic and Functional StudiesR01GM072667 · NIGMS · UNIVERSITY OF TOLEDO · PI HUANG, XUEFEI · 2005 to 2024
$5.1M
NIGMS NIH HHS R01 GM072667
6 · The paper itself

Abstract

Proteoglycans (PGs) are an essential family of glycoproteins, which can play roles in many important biological events including cell proliferation, cancer development, and pathogen infections. Proteoglycans consist of a core protein with one or multiple glycosaminoglycan (GAG) chains, which are covalently attached to serine residues of serine-glycine dipeptide within the core protein through a common tetrasaccharide linkage. In the past three decades, four key glycosyl transferases involved in the biosynthesis of PG linkage have been discovered and investigated. This review aims to provide an overview on progress made on these four enzymes, with foci on enzyme expression/purification, substrate specificity, activity determination, product characterization, and structure-activity relationship analysis.

Indexed as

GlycosyltransferasesProteoglycansGlycosaminoglycansOligosaccharidesSubstrate SpecificityGlycosaminoglycansGlycosyltransferasesOligosaccharidesProteoglycansBiosynthesisChemoenzymatic synthesisEnzymesLinkage regionProteoglycan

Identifiers

PMID34872657
PMCPMC9112072

What OpenQuestion holds

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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.