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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
2000-10-4
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pubmed:abstractText |
Numerous bacterial toxins recognize the actin cytoskeleton as a target. The clostridial binary toxins (Iota and C2 families) ADP-ribosylate the actin monomers causing the dissociation of the actin filaments. The large clostridial toxins from Clostridium difficile, Clostridium sordellii and Clostridium novyi inactivate, by glucosylation, proteins from the Rho family that regulate actin polymerization. In contrast, the cytotoxic necrotic factor from Escherichia coli activates Rho by deamidation and increases the formation of actin filaments. The enterotoxin of Bacteroides fragilis is a protease specific for E-cadherin and it promotes the reorganization of the actin cytoskeleton. The bacterial toxins that modify the actin cytoskeleton induce various cell disfunctions including changes in cell barrier permeability and disruption of intercellular junctions.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/ADP Ribose Transferases,
http://linkedlifedata.com/resource/pubmed/chemical/Actins,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Toxins,
http://linkedlifedata.com/resource/pubmed/chemical/Biopolymers,
http://linkedlifedata.com/resource/pubmed/chemical/Botulinum Toxins,
http://linkedlifedata.com/resource/pubmed/chemical/Cadherins,
http://linkedlifedata.com/resource/pubmed/chemical/Cytotoxins,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Poly(ADP-ribose) Polymerases,
http://linkedlifedata.com/resource/pubmed/chemical/botulinum toxin type C,
http://linkedlifedata.com/resource/pubmed/chemical/cytotoxic necrotizing factor type 1,
http://linkedlifedata.com/resource/pubmed/chemical/cytotoxic necrotizing factor type 2,
http://linkedlifedata.com/resource/pubmed/chemical/iota toxin, Clostridium perfringens,
http://linkedlifedata.com/resource/pubmed/chemical/rho GTP-Binding Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
1139-6709
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
2
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
185-94
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:10943412-ADP Ribose Transferases,
pubmed-meshheading:10943412-Actin Cytoskeleton,
pubmed-meshheading:10943412-Actins,
pubmed-meshheading:10943412-Animals,
pubmed-meshheading:10943412-Bacillus,
pubmed-meshheading:10943412-Bacterial Toxins,
pubmed-meshheading:10943412-Binding Sites,
pubmed-meshheading:10943412-Biopolymers,
pubmed-meshheading:10943412-Botulinum Toxins,
pubmed-meshheading:10943412-Cadherins,
pubmed-meshheading:10943412-Cell Line,
pubmed-meshheading:10943412-Clostridium,
pubmed-meshheading:10943412-Cytotoxins,
pubmed-meshheading:10943412-Dogs,
pubmed-meshheading:10943412-Escherichia coli,
pubmed-meshheading:10943412-Escherichia coli Proteins,
pubmed-meshheading:10943412-Glycosylation,
pubmed-meshheading:10943412-Humans,
pubmed-meshheading:10943412-Poly(ADP-ribose) Polymerases,
pubmed-meshheading:10943412-rho GTP-Binding Proteins
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pubmed:year |
1999
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pubmed:articleTitle |
Bacterial toxins modifying the actin cytoskeleton.
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pubmed:affiliation |
Institut des Neurosciences, Université Pierre et Marie Curie, CNRS UMR7624, Paris, France.
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pubmed:publicationType |
Journal Article,
Review,
Research Support, Non-U.S. Gov't
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