Evidence map›Paper›PMID 23154401›Full record

ReviewCell adhesion & migration

Laminin-211 in skeletal muscle function.

Johan Holmberg, Madeleine Durbeej

Open access · goldAbstract readReview
In one paragraph

Review in Cell adhesion & migration. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 91 papers.

0numbers the graph read from it
0cells of the map it votes in
91citing papers in PubMed
5.4field-weighted citation impact, top 4% 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

91 citing papers in PubMed, 147 citations in OpenAlex.

  1. Article
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  3. Article
  4. Review
  5. Myotendinous Junction development and repair.Journal of orthopaedic translation · 2026
    Review
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  12. Article
  13. Urinary prostaglandin DScientific reports · 2025
    Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. Review
  19. Review
  20. Article

31 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

2 authors at 1 institution in 1 country.

Johan HolmbergMuscle Biology Unit, Department of Experimental Medical Science, Lund University, Lund, Sweden. johan_k.holmberg@med.lu.se
Madeleine Durbeej
Lund University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A chain is no stronger than its weakest link is an old idiom that holds true for muscle biology. As the name implies, skeletal muscle's main function is to move the bones. However, for a muscle to transmit force and withstand the stress that contractions give rise to, it relies on a chain of proteins attaching the cytoskeleton of the muscle fiber to the surrounding extracellular matrix. The importance of this attachment is illustrated by a large number of muscular dystrophies caused by interruption of the cytoskeletal-extracellular matrix interaction. One of the major components of the extracellular matrix is laminin, a heterotrimeric glycoprotein and a major constituent of the basement membrane. It has become increasingly apparent that laminins are involved in a multitude of biological functions, including cell adhesion, differentiation, proliferation, migration and survival. This review will focus on the importance of laminin-211 for normal skeletal muscle function.

Indexed as

Muscle DevelopmentAnimalsBasement MembraneCell SurvivalDystroglycansExtracellular MatrixHumansLamininMiceMuscle ContractionMuscle, SkeletalMuscular DystrophiesMutationProtein BindingSarcolemmaSignal TransductionDystroglycansLamininlaminin alpha 2

Identifiers

PMID23154401
PMCPMC3544775
OpenAlexW2087248324

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.