Evidence map›Paper›PMID 22241827›Full record

ArticleGlycobiology2012

Glycoproteomic characterization of recombinant mouse α-dystroglycan.

Rebecca Harrison, Paul G Hitchen, Maria Panico, Howard R Morris, David Mekhaiel, Richard J Pleass, Anne Dell, Jane E Hewitt, Stuart M Haslam

Open access · bronzeAbstract read
In one paragraph

Article in Glycobiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
4.8field-weighted citation impact, top 4% 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

34 citing papers in PubMed, 57 citations in OpenAlex.

  1. Review
  2. Article
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  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Laminin G-like domains: dystroglycan-specific lectins.Current opinion in structural biology · 2019
    Review
  12. Article
  13. Review
  14. MammalianThe Journal of biological chemistry · 2017
    Article
  15. ProteinThe Journal of biological chemistry · 2017
    Article
  16. Article
  17. Article
  18. Article
  19. Review
  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

9 authors at 3 institutions in 1 country.

Rebecca HarrisonDivision of Molecular Biosciences, Faculty of Natural Sciences, Imperial College London, London SW7 2AZ, UK.
Paul G Hitchen
Maria Panico
Howard R Morris
David Mekhaiel
Richard J Pleass
Anne Dell
Jane E Hewitt
Stuart M Haslam
Imperial College London · GBQueen's Medical Centre · GBUniversity of Nottingham · GB

Funding

Biotechnology and Biological Sciences Research Council B19088Biotechnology and Biological Sciences Research Council BB/F008309/1Biotechnology and Biological Sciences Research Council BBF0083091Biotechnology and Biological Sciences Research Council SF19107Medical Research Council G0300145Wellcome Trust 082915/B/07/Z
6 · The paper itself

Abstract

α-Dystroglycan (DG) is a key component of the dystrophin-glycoprotein complex. Aberrant glycosylation of the protein has been linked to various forms of congenital muscular dystrophy. Unusually α-DG has previously been demonstrated to be modified with both O-N-acetylgalactosamine and O-mannose initiated glycans. In the present study, Fc-tagged recombinant mouse α-DG was expressed and purified from human embryonic kidney 293T cells. α-DG glycopeptides were characterized by glycoproteomic strategies using both nano-liquid chromatography matrix-assisted laser desorption ionization and electrospray tandem mass spectrometry. A total of 14 different peptide sequences and 38 glycopeptides were identified which displayed heterogeneous O-glycosylation. These data provide new insights into the complex domain-specific O-glycosylation of α-DG.

Indexed as

ProteomicsAmino Acid SequenceAnimalsCell LineChromatography, LiquidDystroglycansHumansMiceMolecular Sequence DataRecombinant ProteinsSequence Homology, Amino AcidSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationDystroglycansRecombinant Proteins

Identifiers

PMID22241827
PMCPMC3311285
OpenAlexW2167132957

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.