Evidence map›Paper›PMID 23115008›Full record

ReviewCellular and molecular life sciences : CMLS2013

O-Mannosylation and human disease.

Christina M Dobson, Samuel J Hempel, Stephanie H Stalnaker, Ryan Stuart, Lance Wells

Open access · greenAbstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed, 1 pooled it
3.8field-weighted citation impact, top 6% 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

38 citing papers in PubMed, 1 synthesis or guideline pooled it, 65 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Review
  8. Article
  9. The SHDRA syndrome-associated geneProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  10. Review
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  12. Article
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  17. Review
  18. Article
  19. Article
  20. Facile Chemoenzymatic Synthesis of O-Mannosyl Glycans.Angewandte Chemie (International ed. in English) · 2018
    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

5 authors at 1 institution in 1 country.

Christina M DobsonDepartment of Biochemistry and Molecular Biology, Complex Carbohydrate Research Center, University of Georgia, Athens, GA, USA.
Samuel J Hempel
Stephanie H Stalnaker
Ryan Stuart
Lance Wells
University of Georgia · US

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
ZINC DEFICIENCY &PROTEIN EXPRESSION IN RAT OLFACTORY BULBSP41RR018502 · NCRR · UNIVERSITY OF GEORGIA (UGA) · PI AZADI, PARASTOO · 2003 to 2011
$13.1M
Post-Translation Processing of Alpha-DystroglycanR21AR056055 · NIAMS · UNIVERSITY OF GEORGIA · PI LIVE, DAVID H · 2008 to 2009
$357k
NCRR NIH HHS P41 RR018502NCRR NIH HHS P41RR018502NIAMS NIH HHS R21 AR056055NIAMS NIH HHS R21AR056055NIGMS NIH HHS P41 GM103490
6 · The paper itself

Abstract

Glycosylation of proteins is arguably the most prevalent co- and post-translational modification. It is responsible for increased heterogeneity and functional diversity of proteins. Here we discuss the importance of one type of glycosylation, specifically O-mannosylation and its relationship to a number of human diseases. The most widely studied O-mannose modified protein is alpha-dystroglycan (α-DG). Recent studies have focused intensely on α-DG due to the severity of diseases associated with its improper glycosylation. O-mannosylation of α-DG is involved in cancer metastasis, arenavirus entry, and multiple forms of congenital muscular dystrophy [1, 2]. In this review, we discuss the structural and functional characteristics of O-mannose-initiated glycan structures on α-DG, enzymes involved in the O-mannosylation pathway, and the diseases that are a direct result of disruptions within this pathway.

Indexed as

AnimalsArenaviridae InfectionsDystroglycansGlycosylationHumansMannoseMuscular DystrophiesNeoplasm MetastasisNeoplasmsDystroglycansMannose

Identifiers

PMID23115008
PMCPMC3984002
OpenAlexW2074370393

What OpenQuestion holds

Textmetadata
LicenceTDM
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.