Evidence map›Paper›PMID 28810660›Full record

ReviewGlycobiology2017

Recent advancements in understanding mammalian O-mannosylation.

M Osman Sheikh, Stephanie M Halmo, Lance Wells

Abstract readReview
In one paragraph

Review in Glycobiology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing 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

65 citing papers in PubMed.

  1. Article
  2. Glycan-related genes and genetic disorders.Journal of human genetics · 2026
    Review
  3. Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. O-GalNAc glycans are enriched in neuronal tracts and regulate nodes of Ranvier.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  10. Article
  11. Article
  12. Article
  13. Molecular Study of the Fukutin-Related Protein (International journal of molecular sciences · 2024
    Article
  14. Cancers · 2024
    Review
  15. Article
  16. Matriglycan maintains t-tubule structural integrity in cardiac muscle.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  17. Article
  18. Article
  19. Review
  20. Review

5 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

3 authors.

M Osman SheikhComplex Carbohydrate Research Center, University of Georgia, 315 Riverbend Road, Athens, GA 30602, USA.
Stephanie M HalmoComplex Carbohydrate Research Center, University of Georgia, 315 Riverbend Road, Athens, GA 30602, USA.
Lance WellsComplex Carbohydrate Research Center, University of Georgia, 315 Riverbend Road, Athens, GA 30602, USA.

Funding

TR&D1: Stem Cell and Induced Pluripotent Stem Cell Resources (Pages 116-134)P41GM103490 · NIGMS · UNIVERSITY OF GEORGIA · PI PIERCE, J. MICHAEL · 2012 to 2018
$13.7M
Structure and Function in alpha-Dystroglycan GlycosylationR01GM111939 · NIGMS · UNIVERSITY OF GEORGIA · PI Lance Wells · 2014 to 2026
$4.0M
Glycoscience Training ProgramT32GM107004 · NIGMS · UNIVERSITY OF GEORGIA · PI AMSTER, I JONATHAN, HALTIWANGER, ROBERT S. · 2014 to 2021
$1.3M
NIGMS NIH HHS P41 GM103490NIGMS NIH HHS R01 GM111939NIGMS NIH HHS T32 GM107004
6 · The paper itself

Abstract

The post-translational glycosylation of select proteins by O-linked mannose (O-mannose or O-man) is a conserved modification from yeast to humans and has been shown to be necessary for proper development and growth. The most well studied O-mannosylated mammalian protein is α-dystroglycan (α-DG). Hypoglycosylation of α-DG results in varying severities of congenital muscular dystrophies, cancer progression and metastasis, and inhibited entry and infection of certain arenaviruses. Defects in the gene products responsible for post-translational modification of α-DG, primarily glycosyltransferases, are the basis for these diseases. The multitude of clinical phenotypes resulting from defective O-mannosylation highlights the biomedical significance of this unique modification. Elucidation of the various O-mannose biosynthetic pathways is imperative to understanding a broad range of human diseases and for the development of novel therapeutics. In this review, we will focus on recent discoveries delineating the various enzymes, structures and functions associated with O-mannose-initiated glycoproteins. Additionally, we discuss current gaps in our knowledge of mammalian O-mannosylation, discuss the evolution of this pathway, and illustrate the utility and limitations of model systems to study functions of O-mannosylation.

Indexed as

Protein Processing, Post-TranslationalAnimalsArenavirusDystroglycansEvolution, MolecularGlycosylationGlycosyltransferasesHumansMammalsMannoseMuscular DystrophiesNeoplasmsReceptors, VirusDAG1 protein, humanDystroglycansGlycosyltransferasesMannoseReceptors, Viruscongenital muscular dystrophydystroglycanglycosylationO-mannosylation

Identifiers

PMID28810660
PMCPMC6082599

What OpenQuestion holds

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Read underepoch 390

Registered trials

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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.