Analysis of the SlyA-controlled expression, subcellular localization and pore-forming activity of a 34 kDa haemolysin (ClyA) from Escherichia coli K-12-Reference-Cited by-同舟云学术

Analysis of the SlyA-controlled expression, subcellular localization and pore-forming activity of a 34 kDa haemolysin (ClyA) from Escherichia coli K-12

Published:1999-01 Issue:2 Volume:31 Page:557-567
ISSN:0950-382X
Container-title:Molecular Microbiology
language:en
Short-container-title:Mol Microbiol

Author:

Ludwig Albrecht,Bauer Susanne,Benz Roland,Bergmann Birgit,Goebel Werner

Publisher

Wiley

Subject

Molecular Biology,Microbiology

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1046/j.1365-2958.1999.01196.x/fullpdf

Reference27 articles.

1. Characterization of an RTX toxin from enterohemorrhagic Escherichia coli O157:H7

2. Formation of large, ion-permeable membrane channels by the matrix protein (porin) of Escherichia coli

3. Ionic selectivity of pores formed by the matrix protein (porin) of Escherichia coli

4. Pore formation by the Escherichia coli hemolysin: evidence for an association-dissociation equilibrium of the pore-forming aggregates

5. Staphylococcal alpha-toxin, streptolysin-O, and Escherichia coli hemolysin: prototypes of pore-forming bacterial cytolysins

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