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Article

Assembly of alpha-hemolysin on A431 cells leads to clustering of Caveolin-1.

Biochemical and biophysical research communications - 19 Nov 2004

Vijayvargia Ravi, Kaur Surinder, Sangha Navneet, Sahasrabuddhe Anagh A, Surolia Ira, Shouche Yogesh, Krishnasastry Musti V

Abstract excerpt

Assembly and penetration of 14-strand beta-barrel of staphylococcal alpha-hemolysin (alpha-HL) is an intriguing phenomenon due to its water soluble property. alpha-HL interacts with the Caveolin-1 of A431 cells for its rapid assembly. A nine amino acid, non-hydrophobic peptide derived from alpha-HL has been shown to block the interaction of alpha-HL with the scaffolding domain of Caveolin-1. alpha-HL's presence...

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Identifiers

PMID: 15485671
DOI: 10.1016/j.bbrc.2004.09.165

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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