Evidence map›Paper›PMID 27601598›Full record

ArticleMolecular & cellular proteomics : MCP2016

Direct Mapping of Additional Modifications on Phosphorylated O-glycans of α-Dystroglycan by Mass Spectrometry Analysis in Conjunction with Knocking Out of Causative Genes for Dystroglycanopathy.

Hirokazu Yagi, Chu-Wei Kuo, Takayuki Obayashi, Satoshi Ninagawa, Kay-Hooi Khoo, Koichi Kato

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

18 citing papers in PubMed, 40 citations in OpenAlex.

  1. Pediatric investigation · 2026
    Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Laminin G-like domains: dystroglycan-specific lectins.Current opinion in structural biology · 2019
    Review
  13. Mammalian O-mannosyl glycans: Biochemistry and glycopathology.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2019
    Article
  14. Article
  15. CDP-glycerol inhibits the synthesis of the functionalThe Journal of biological chemistry · 2018
    Article
  16. Distinctive and Complementary MSJournal of the American Society for Mass Spectrometry · 2018
    Article
  17. Review
  18. 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

6 authors at 3 institutions in 2 countries.

Hirokazu YagiFrom the ‡Graduate School of Pharmaceutical Sciences, Nagoya City University, 3-1 Tanabe-dori, Mizuho-ku, Nagoya 467-8603, Japan.ORCID 0000-0001-9296-0225
Chu-Wei Kuo§Institute of Biological Chemistry, Academia Sinica, 128, Academia Road Sec. 2, Nankang, Taipei 115, Taiwan.
Takayuki ObayashiFrom the ‡Graduate School of Pharmaceutical Sciences, Nagoya City University, 3-1 Tanabe-dori, Mizuho-ku, Nagoya 467-8603, Japan.
Satoshi Ninagawa¶Okazaki Institute for Integrative Bioscience and Institute for Molecular Science, National Institutes of Natural Sciences, 5-1 Higashiyama Myodaiji, Okazaki 444-8787, Japan.
Kay-Hooi Khoo§Institute of Biological Chemistry, Academia Sinica, 128, Academia Road Sec. 2, Nankang, Taipei 115, Taiwan; kkato@phar.nagoya-cu.ac.jp.
Koichi KatoFrom the ‡Graduate School of Pharmaceutical Sciences, Nagoya City University, 3-1 Tanabe-dori, Mizuho-ku, Nagoya 467-8603, Japan; kkato@phar.nagoya-cu.ac.jp.
Nagoya City University · JPInstitute of Biological Chemistry, Academia Sinica · TWNational Institutes of Natural Sciences · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Dystroglycanopathy is a major class of congenital muscular dystrophy caused by a deficiency of functional glycans on α-dystroglycan (αDG) with laminin-binding activity. Recent advances have led to identification of several causative gene products of dystroglycanopathy and characterization of their in vitro enzymatic activities. However, the in vivo functional roles remain equivocal for enzymes such as ISPD, FKTN, FKRP, and TMEM5 that are supposed to be involved in post-phosphoryl modifications linking the GalNAc-β3-GlcNAc-β4-Man-6-phosphate core and the outer laminin-binding glycans. Herein, by direct nano-LC-MS

Indexed as

DystroglycansGene Knockout TechniquesGenetic Predisposition to DiseaseHCT116 CellsHEK293 CellsHumansMembrane ProteinsNucleotidyltransferasesPentosyltransferasesPhosphorylationProteinsWalker-Warburg SyndromeCRPPA protein, humanDystroglycansFKRP protein, humanFKTN protein, humanMembrane ProteinsNucleotidyltransferasesPentosyltransferasesProteinsRXYLT1 protein, human

Identifiers

PMID27601598
PMCPMC5098040
OpenAlexW2515784546

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.