Evidence map›Paper›PMID 31092689›Full record

ReviewEssays in biochemistry2019

Structural biology of laminins.

Erhard Hohenester

Open access · hybridAbstract readReview
In one paragraph

Review in Essays in biochemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed, 1 pooled it
7.0field-weighted citation impact, top 2% 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

64 citing papers in PubMed, 1 synthesis or guideline pooled it, 112 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Mechanisms of mitral valve development and disease.Frontiers in cardiovascular medicine · 2026
    Review
  11. Basement membrane structure and function: Relating biology to mechanics.Matrix biology : journal of the International Society for Matrix Biology · 2025
    Review
  12. Invasin-functionalized PIC hydrogels enable long-term 3D culture of epithelial organoids.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  13. Article
  14. Basement membranes at a glance.Journal of cell science · 2025
    Review
  15. Review
  16. Article
  17. Article
  18. Laminins and the blood-brain barrier.Matrix biology : journal of the International Society for Matrix Biology · 2025
    Review
  19. Article
  20. Review

4 more citing papers are in PubMed but not listed here.

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, U.K. e.hohenester@imperial.ac.uk.ORCID 0000-0002-0813-7218
Imperial College London · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

Laminins are large cell-adhesive glycoproteins that are required for the formation and function of basement membranes in all animals. Structural studies by electron microscopy in the early 1980s revealed a cross-shaped molecule, which subsequently was shown to consist of three distinct polypeptide chains. Crystallographic studies since the mid-1990s have added atomic detail to all parts of the laminin heterotrimer. The three short arms of the cross are made up of continuous arrays of disulphide-rich domains. The globular domains at the tips of the short arms mediate laminin polymerization; the surface regions involved in this process have been identified by structure-based mutagenesis. The long arm of the cross is an α-helical coiled coil of all three chains, terminating in a cell-adhesive globular region. The molecular basis of cell adhesion to laminins has been revealed by recent structures of heterotrimeric integrin-binding fragments and of a laminin fragment bound to the carbohydrate modification of dystroglycan. The structural characterization of the laminin molecule is essentially complete, but we still have to find ways of imaging native laminin polymers at molecular resolution.

Indexed as

AnimalsBinding SitesDystroglycansHumansIntegrinsLamininMembrane GlycoproteinsPolymerizationProtein BindingProtein DomainsProtein MultimerizationDystroglycansIntegrinsLamininMembrane Glycoproteinsnidogencell adhesioncrystallographyextracellular matrix

Identifiers

PMID31092689
PMCPMC6744579
OpenAlexW2945712417

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.