Evidence map›Paper›PMID 27733679›Full record

ArticleThe Journal of biological chemistry2016

The Muscular Dystrophy Gene TMEM5 Encodes a Ribitol β1,4-Xylosyltransferase Required for the Functional Glycosylation of Dystroglycan.

Hiroshi Manya, Yoshiki Yamaguchi, Motoi Kanagawa, Kazuhiro Kobayashi, Michiko Tajiri, Keiko Akasaka-Manya, Hiroko Kawakami, Mamoru Mizuno, Yoshinao Wada, Tatsushi Toda and 1 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
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

45 citing papers in PubMed, 80 citations in OpenAlex.

  1. Review
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  5. UDP-glucose dehydrogenase variants cause dystroglycanopathy.Annals of clinical and translational neurology · 2025
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  15. Classification of domains in predicted structures of the human proteome.Proceedings of the National Academy of Sciences of the United States of America · 2023
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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

11 authors at 5 institutions in 1 country.

Hiroshi ManyaFrom the Molecular Glycobiology, Research Team for Mechanism of Aging, Tokyo Metropolitan Geriatric Hospital and Institute of Gerontology, Tokyo 173-0015, Japan.
Yoshiki Yamaguchithe Structural Glycobiology Team, Systems Glycobiology Research Group, RIKEN-Max Planck Joint Research Center for Systems Chemical Biology, RIKEN Global Research Cluster, Wako, Saitama 351-0198, Japan.
Motoi Kanagawathe Division of Neurology/Molecular Brain Science, Kobe University Graduate School of Medicine, Kobe, Hyogo 650-0017, Japan.
Kazuhiro Kobayashithe Division of Neurology/Molecular Brain Science, Kobe University Graduate School of Medicine, Kobe, Hyogo 650-0017, Japan.
Michiko Tajirithe Department of Molecular Medicine, Osaka Medical Center and Research Institute for Maternal and Child Health, Izumi, Osaka 594-1101, Japan, and.
Keiko Akasaka-ManyaFrom the Molecular Glycobiology, Research Team for Mechanism of Aging, Tokyo Metropolitan Geriatric Hospital and Institute of Gerontology, Tokyo 173-0015, Japan.
Hiroko Kawakamithe Laboratory of Glyco-organic Chemistry, The Noguchi Institute, Itabashi, Tokyo 173-0003, Japan.
Mamoru Mizunothe Laboratory of Glyco-organic Chemistry, The Noguchi Institute, Itabashi, Tokyo 173-0003, Japan.
Yoshinao Wadathe Department of Molecular Medicine, Osaka Medical Center and Research Institute for Maternal and Child Health, Izumi, Osaka 594-1101, Japan, and.
Tatsushi Todathe Division of Neurology/Molecular Brain Science, Kobe University Graduate School of Medicine, Kobe, Hyogo 650-0017, Japan.
Tamao EndoFrom the Molecular Glycobiology, Research Team for Mechanism of Aging, Tokyo Metropolitan Geriatric Hospital and Institute of Gerontology, Tokyo 173-0015, Japan,. Electronic address: endo@tmig.or.jp.
Kobe University · JPTokyo Metropolitan Geriatric Hospital · JPNoguchi Institute · JPOsaka Medical Center for Cancer and Cardiovascular Diseases · JPRIKEN · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A defect in O-mannosyl glycan is the cause of α-dystroglycanopathy, a group of congenital muscular dystrophies caused by aberrant α-dystroglycan (α-DG) glycosylation. Recently, the entire structure of O-mannosyl glycan, [3GlcAβ1-3Xylα1]

Indexed as

Cell LineDystroglycansGlycosylationHumansMembrane ProteinsMuscular DystrophiesMutation, MissenseNuclear Magnetic Resonance, BiomolecularPentosyltransferasesTransferases (Other Substituted Phosphate Groups)DystroglycansMembrane ProteinsPentosyltransferasesRXYLT1 protein, humanTransferases (Other Substituted Phosphate Groups)dystroglycanglycoconjugateglycosylationglycosyltransferasemuscular dystrophyO-mannosyl glycanTMEM5xylosyltransferase

Identifiers

PMID27733679
PMCPMC5114413
OpenAlexW2530711020

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.