Evidence map›Paper›PMID 17426950›Full record

ReviewJournal of molecular medicine (Berlin, Germany)2007

Laminin isoforms in development and disease.

Susanne Schéele, Alexander Nyström, Madeleine Durbeej, Jan F Talts, Marja Ekblom, Peter Ekblom

Abstract readReview
PubMed Publisher
In one paragraph

Review in Journal of molecular medicine (Berlin, Germany), 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed, 2 pooled it
6.0field-weighted citation impact, top 3% 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

61 citing papers in PubMed, 2 syntheses or guidelines pooled it, 156 citations in OpenAlex.

  1. Pooled it
  2. Pooled it
  3. Mechanisms of mitral valve development and disease.Frontiers in cardiovascular medicine · 2026
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  8. Molecular Characterization of the Interplay betweenInternational journal of molecular sciences · 2023
    Article
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  14. Comprehensive analysis ofFrontiers in molecular biosciences · 2022
    Article
  15. Review
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  17. Article
  18. Article
  19. Review
  20. Article

1 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

6 authors at 2 institutions in 2 countries.

Susanne SchéeleSection for Cell and Matrix Biology, BMC B12, Department of Experimental Medical Science, Lund University, Sölvegatan 19, 22184, Lund, Sweden. susanne.scheele@med.lu.se
Alexander Nyström
Madeleine Durbeej
Jan F Talts
Marja Ekblom
Peter Ekblom
Lund University · SEUniversity of Copenhagen · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The members of the laminin family of heterotrimers are major constituents of all basement membranes, sheet-like extracellular structures, present in almost all organs. The laminins bind to cell surface receptors and thereby tightly connect the basement membrane to the adjacent cell layer. This provides for the specific basement membrane functions to stabilize cellular structures, to serve as effective physical barriers, and furthermore, to govern cell fate by inducing intracellular signalling cascades. Many different types of diseases involve basement membranes and laminins. Metastasizing solid tumors must pass through basement membranes to reach the vascular system, and various microbes and viruses enter the cells through direct interaction with laminins. Furthermore, whereas mutations in one specific laminin chain lead to a muscular disorder, mutations of other laminin chains cause skin blistering and kidney defects, respectively. This review summarizes recent progress concerning the molecular mechanisms of laminins in development and disease. The current knowledge may lead to clinical treatment of lamininopathies and may include stem-cell approaches as well as gene therapy.

Indexed as

AnimalsBasement MembraneDystroglycansHumansIntegrinsLamininModels, BiologicalMuscular DiseasesMutationProtein IsoformsDystroglycansIntegrinsLamininProtein Isoforms

Identifiers

PMID17426950
OpenAlexW2006831658

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.