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Proteolytic activation of cholera toxin and Escherichia coli labile toxin by entry into host epithelial cells. Signal transduction by a protease-resistant toxin variant

Autor: W I, Lencer, C, Constable, S, Moe, P A, Rufo, A, Wolf, M G, Jobling, S P, Ruston, J L, Madara, R K, Holmes, T R, Hirst

Publikováno v: The Journal of biological chemistry. 272(24)

Cholera and Escherichia coli heat-labile toxins (CT and LT) require proteolysis of a peptide loop connecting two major domains of their enzymatic A subunits for maximal activity (termed "nicking"). To test whether host intestinal epithelial cells may

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::e1db96271abd0fed0fc4821fe83f532c
https://pubmed.ncbi.nlm.nih.gov/9182593

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Kinetics of acid-mediated disassembly of the B subunit pentamer of Escherichia coli heat-labile enterotoxin. Molecular basis of pH stability

Autor: L W, Ruddock, S P, Ruston, S M, Kelly, N C, Price, R B, Freedman, T R, Hirst

Publikováno v: The Journal of biological chemistry. 270(50)

The B-subunit pentamer of Escherichia coli heat-labile enterotoxin (EtxB) is highly stable, maintaining its quaternary structure in a range of conditions that would normally be expected to cause protein denaturation. In this paper the structural stab

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::175519898ea3b5afe7f28750f4895de9
https://pubmed.ncbi.nlm.nih.gov/8530395

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