Evidence map›Paper›PMID 20624979›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2010

Role of a disintegrin and metalloprotease 10 in Staphylococcus aureus alpha-hemolysin-mediated cellular injury.

Georgia A Wilke, Juliane Bubeck Wardenburg

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 296 papers.

0numbers the graph read from it
0cells of the map it votes in
296citing papers in PubMed
10.5field-weighted citation impact, top 1% 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

296 citing papers in PubMed, 440 citations in OpenAlex.

  1. Trial
  2. Virulence · 2026
    Article
  3. Article
  4. Staphylococcus aureus-vascular endothelium interactions: Mechanisms and therapeutic opportunities.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2026
    Review
  5. Article
  6. Infection and immunity · 2026
    Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Review
  17. Frontiers in microbiology · 2026
    Article
  18. α-hemolysin polymorphisms in methicillin-resistantbioRxiv : the preprint server for biology · 2025
    Article
  19. The Pathogenicity Mechanisms ofInternational journal of molecular sciences · 2025
    Review
  20. Article

236 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.

Georgia A WilkeDepartment of Pediatrics, University of Chicago, Chicago, IL 60637, USA.
Juliane Bubeck Wardenburg
University of Chicago · US

Funding

Vaccines and Therapies Against BotulismU54AI057153 · NIAID · UNIVERSITY OF CHICAGO · PI SHUMAN, HOWARD A · 2003 to 2013
$87.6M
NIAID NIH HHS 2-U54-AI-057153NIAID NIH HHS U54 AI057153
6 · The paper itself

Abstract

Staphylococcus aureus alpha-hemolysin (Hla), a potent cytotoxin, plays an important role in the pathogenesis of staphylococcal diseases, including those caused by methicillin-resistant epidemic strains. Hla is secreted as a water-soluble monomer that undergoes a series of conformational changes to generate a heptameric, beta-barrel structure in host membranes. Structural maturation of Hla depends on its interaction with a previously unknown proteinaceous receptor in the context of the cell membrane. It is reported here that a disintegrin and metalloprotease 10 (ADAM10) interacts with Hla and is required to initiate the sequence of events whereby the toxin is transformed into a cytolytic pore. Hla binding to the eukaryotic cell requires ADAM10 expression. Further, ADAM10 is required for Hla-mediated cytotoxicity, most notably when the toxin is present at low concentrations. These data thus implicate ADAM10 as the probable high-affinity toxin receptor. Upon Hla binding, ADAM10 relocalizes to caveolin 1-enriched lipid rafts that serve as a platform for the clustering of signaling molecules. It is demonstrated that the Hla-ADAM10 complex initiates intracellular signaling events that culminate in the disruption of focal adhesions.

Indexed as

ADAM10 ProteinADAM ProteinsAmino Acid SequenceAmyloid Precursor Protein SecretasesAnimalsBacterial ProteinsCell LineCell Line, TumorCell SurvivalElectrophoresis, Polyacrylamide GelEpithelial CellsErythrocytesFocal AdhesionsHemolysin ProteinsHost-Pathogen InteractionsHumansADAM10 ProteinADAM10 protein, humanADAM ProteinsAmyloid Precursor Protein SecretasesBacterial ProteinsHemolysin ProteinsIntegrin beta1Membrane Proteins

Identifiers

PMID20624979
PMCPMC2922128
OpenAlexW2126467473

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.