Evidence map›Paper›PMID 23329828›Full record

ReviewThe Journal of biological chemistry2013

Mucin-type O-glycosylation during development.

Duy T Tran, Kelly G Ten Hagen

Open access · hybridAbstract readReview
In one paragraph

Review in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 156 papers.

0numbers the graph read from it
0cells of the map it votes in
156citing papers in PubMed
8.2field-weighted citation impact, top 2% 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

156 citing papers in PubMed, 270 citations in OpenAlex.

  1. Article
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  11. Neuromuscular Defects in aBiomolecules · 2025
    Article
  12. Association of theBiology of sport · 2025
    Article
  13. Implications of Mucin-TypeMolecules (Basel, Switzerland) · 2025
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Article

96 more citing papers are in PubMed but not listed here.

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.

Duy T TranDevelopmental Glycobiology Section, NIDCR, National Institutes of Health, Bethesda, Maryland 20892-4370, USA.
Kelly G Ten Hagen
National Institutes of Health · US

Funding

Role of O-glycosylation in Animal DevelopmentZIADE000713 · NIDCR · NATIONAL INSTITUTE OF DENTAL & CRANIOFACIAL RESEARCH · PI TEN HAGEN, KELLY G · 2009 to 2025
$30.6M
Intramural NIH HHS
6 · The paper itself

Abstract

Mucin-type O-glycosylation is an evolutionarily conserved protein modification present on membrane-bound and secreted proteins. Aberrations in O-glycosylation are responsible for certain human diseases and are associated with disease risk factors. Recent studies have demonstrated essential roles for mucin-type O-glycosylation in protein secretion, stability, processing, and function. Here, we summarize our current understanding of the diverse roles of mucin-type O-glycosylation during eukaryotic development. Appreciating how this conserved modification operates in developmental processes will provide insight into its roles in human disease and disease susceptibilities.

Indexed as

AcetylgalactosamineAnimalsGlycosylationGlycosyltransferasesHumansMembrane GlycoproteinsModels, BiologicalMucinsN-AcetylgalactosaminyltransferasesPolysaccharidesAcetylgalactosamineGlycosyltransferasesMembrane GlycoproteinsMucinsN-AcetylgalactosaminyltransferasesPolysaccharides

Identifiers

PMID23329828
PMCPMC3591602
OpenAlexW2074235202

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.