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Literature DB >> 8137117

Enterobacterial hemolysins: activation, secretion and pore formation.

Abstract

Two types of enterobacterial hemolysins have been studied in detail: the Escherichia coli alpha-hemolysin and the Serratia marcescens hemolysin. Although they have similar properties, they differ entirely in the number and structure of the proteins that determine their hemolytic activities, in the mechanism and the subcellular location of activation and in their secretion mechanisms.

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Year: 1993 PMID： 8137117 DOI： 10.1016/0966-842x(93)90134-d

Source DB: PubMed Journal: Trends Microbiol ISSN： 0966-842X Impact factor: 17.079

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Cited

13 in total

1. Activation of Serratia marcescens hemolysin through a conformational change.

Authors: Georg Walker; Ralf Hertle; Volkmar Braun
Journal: Infect Immun Date: 2004-01 Impact factor: 3.441

2. Characterization of EspC, a 110-kilodalton protein secreted by enteropathogenic Escherichia coli which is homologous to members of the immunoglobulin A protease-like family of secreted proteins.

Authors: M Stein; B Kenny; M A Stein; B B Finlay
Journal: J Bacteriol Date: 1996-11 Impact factor: 3.490

3. Purification and characterization of a hemolysin-like protein, Sll1951, a nontoxic member of the RTX protein family from the Cyanobacterium Synechocystis sp. strain PCC 6803.

Authors: Tetsushi Sakiyama; Hironori Ueno; Hideya Homma; Osamu Numata; Tomohiko Kuwabara
Journal: J Bacteriol Date: 2006-05 Impact factor: 3.490

4. Characterization of dominantly negative mutant ClyA cytotoxin proteins in Escherichia coli.

Authors: Sun Nyunt Wai; Marie Westermark; Jan Oscarsson; Jana Jass; Elke Maier; Roland Benz; Bernt Eric Uhlin
Journal: J Bacteriol Date: 2003-09 Impact factor: 3.490

5. Clinical and environmental isolates of Vibrio cholerae serogroup O141 carry the CTX phage and the genes encoding the toxin-coregulated pili.

Authors: A Dalsgaard; O Serichantalergs; A Forslund; W Lin; J Mekalanos; E Mintz; T Shimada; J G Wells
Journal: J Clin Microbiol Date: 2001-11 Impact factor: 5.948

6. In vitro proteolytic processing and activation of the recombinant precursor of El Tor cytolysin/hemolysin (pro-HlyA) of Vibrio cholerae by soluble hemagglutinin/protease of V. cholerae, trypsin, and other proteases.

Authors: K Nagamune; K Yamamoto; A Naka; J Matsuyama; T Miwatani; T Honda
Journal: Infect Immun Date: 1996-11 Impact factor: 3.441

Enterobacterial hemolysins: activation, secretion and pore formation.

1. Activation of Serratia marcescens hemolysin through a conformational change.

2. Characterization of EspC, a 110-kilodalton protein secreted by enteropathogenic Escherichia coli which is homologous to members of the immunoglobulin A protease-like family of secreted proteins.

3. Purification and characterization of a hemolysin-like protein, Sll1951, a nontoxic member of the RTX protein family from the Cyanobacterium Synechocystis sp. strain PCC 6803.

4. Characterization of dominantly negative mutant ClyA cytotoxin proteins in Escherichia coli.

5. Clinical and environmental isolates of Vibrio cholerae serogroup O141 carry the CTX phage and the genes encoding the toxin-coregulated pili.

6. In vitro proteolytic processing and activation of the recombinant precursor of El Tor cytolysin/hemolysin (pro-HlyA) of Vibrio cholerae by soluble hemagglutinin/protease of V. cholerae, trypsin, and other proteases.

7. Comparative and functional genomic analyses of iron transport and regulation in Leptospira spp.

Review 8. Pathogenicity islands in bacterial pathogenesis.

9. The secreted Ipa complex of Shigella flexneri promotes entry into mammalian cells.

10. Identification and characterization of two functional domains of the hemolysin translocator protein HlyD.