Evidence map›Paper›PMID 25487405›Full record

ReviewCell and tissue research2015

Molecular architecture and function of the hemidesmosome.

Gernot Walko, Maria J Castañón, Gerhard Wiche

Open access · hybridAbstract readReview
In one paragraph

Review in Cell and tissue research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 papers.

0numbers the graph read from it
0cells of the map it votes in
80citing papers in PubMed
5.0field-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

80 citing papers in PubMed, 253 citations in OpenAlex.

  1. Hemidesmosomal Proteins in Oral Cancer Progression: An Immunohistochemical Study of Human and Mouse.Journal of oral pathology & medicine : official publication of the International Association of Oral Pathologists and the American Academy of Oral Pathology · 2026
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  13. Peptide Epitopes of NC16A BP180 in the Diagnostics of Bullous Pemphigoid.JID innovations : skin science from molecules to population health · 2025
    Article
  14. Article
  15. Challenges of Studying Amelogenesis in Gene-Targeted Mouse Models.International journal of molecular sciences · 2025
    Review
  16. Article
  17. Review
  18. The role and regulation of integrins in cell migration and invasion.Nature reviews. Molecular cell biology · 2025
    Review
  19. Review
  20. Article

20 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

3 authors at 3 institutions in 2 countries.

Gernot WalkoCentre for Stem Cells and Regenerative Medicine, King's College London School of Medicine, 28th Floor, Tower Wing, Guy's Hospital, Great Maze Pond, London, SE1 9RT, UK.
Maria J Castañón
Gerhard Wiche
Guy's Hospital · GBMax Perutz Labs · ATUniversity of Vienna · AT

Funding

Austrian Science Fund FWF P 23729
6 · The paper itself

Abstract

Hemidesmosomes are multiprotein complexes that facilitate the stable adhesion of basal epithelial cells to the underlying basement membrane. The mechanical stability of hemidesmosomes relies on multiple interactions of a few protein components that form a membrane-embedded tightly-ordered complex. The core of this complex is provided by integrin α6β4 and P1a, an isoform of the cytoskeletal linker protein plectin that is specifically associated with hemidesmosomes. Integrin α6β4 binds to the extracellular matrix protein laminin-332, whereas P1a forms a bridge to the cytoplasmic keratin intermediate filament network. Other important components are BPAG1e, the epithelial isoform of bullous pemphigoid antigen 1, BPAG2, a collagen-type transmembrane protein and CD151. Inherited or acquired diseases in which essential components of the hemidesmosome are missing or structurally altered result in tissue fragility and blistering. Modulation of hemidesmosome function is of crucial importance for a variety of biological processes, such as terminal differentiation of basal keratinocytes and keratinocyte migration during wound healing and carcinoma invasion. Here, we review the molecular characteristics of the proteins that make up the hemidesmosome core structure and summarize the current knowledge about how their assembly and turnover are regulated by transcriptional and post-translational mechanisms.

Indexed as

AnimalsBasement MembraneHemidesmosomesHumansIntermediate FilamentsKeratinocytesMembrane ProteinsProtein Processing, Post-TranslationalTranscription, GeneticMembrane Proteins

Identifiers

PMID25487405
PMCPMC4544487
OpenAlexW2135951248

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.