Evidence map›Paper›PMID 30530204›Full record

ReviewCurrent opinion in structural biology2019

Laminin G-like domains: dystroglycan-specific lectins.

Erhard Hohenester

Open access · greenAbstract readReview
In one paragraph

Review in Current opinion in structural biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
3.1field-weighted citation impact, top 9% 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

33 citing papers in PubMed, 64 citations in OpenAlex.

  1. Article
  2. Article
  3. X-Ray Exposure Induces Structural Changes in Human Breast Proteins.International journal of molecular sciences · 2025
    Article
  4. Laminin α5: a key factor in tumor metastasis.Clinical & experimental metastasis · 2025
    Review
  5. The Link between Oxygen and Basement Membranes.Reviews of physiology, biochemistry and pharmacology · 2025
    Review
  6. Review
  7. Review
  8. Review
  9. Review
  10. Review
  11. Article
  12. Review
  13. Article
  14. The SHDRA syndrome-associated geneProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  15. Article
  16. Article
  17. Article
  18. Review
  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

1 author at 1 institution in 1 country.

Erhard HohenesterDepartment of Life Sciences, Imperial College London, London SW7 2AZ, United Kingdom. Electronic address: e.hohenester@imperial.ac.uk.
Imperial College London · GB

Funding

Wellcome TrustWellcome Trust 101748/Z/13/Z
6 · The paper itself

Abstract

A unique O-mannose-linked glycan on the transmembrane protein dystroglycan binds a number of extracellular matrix proteins containing laminin G-like (LG) domains. The dystroglycan-matrix interaction is essential for muscle function: disrupted biosynthesis of the matrix-binding modification causes several forms of muscular dystrophy. The complete chemical structure of this modification has been deciphered in the past few years. We now know that LG domains bind to a glycosaminoglycan-like polysaccharide of [-3GlcAβ1,3Xylα1-] units, termed matriglycan, that is attached to a highly unusual heptasaccharide linker. X-ray crystallography has revealed the principles of Ca

Indexed as

Amino Acid SequenceAnimalsDystroglycansHumansLamininLectinsProtein DomainsDystroglycansLamininLectins

Identifiers

PMID30530204
PMCPMC6925595
OpenAlexW2905528384

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.