Source:http://linkedlifedata.com/resource/pubmed/id/22069620
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
5
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| pubmed:dateCreated |
2011-11-9
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| pubmed:abstractText |
Protease domains within toxins typically act as the primary effector domain within target cells. By contrast, the primary function of the cysteine protease domain (CPD) in Multifunctional Autoprocessing RTX-like (MARTX) and Clostridium sp. glucosylating toxin families is to proteolytically cleave the toxin and release its cognate effector domains. The CPD becomes activated upon binding to the eukaryotic-specific small molecule, inositol hexakisphosphate (InsP(6)), which is found abundantly in the eukaryotic cytosol. This property allows the CPD to spatially and temporally regulate toxin activation, making it a prime candidate for developing anti-toxin therapeutics. In this review, we summarize recent findings related to defining the regulation of toxin function by the CPD and the development of inhibitors to prevent CPD-mediated activation of bacterial toxins.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:status |
PubMed-not-MEDLINE
|
| pubmed:month |
May
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| pubmed:issn |
2072-6651
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| pubmed:author | |
| pubmed:issnType |
Electronic
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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 |
963-77
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| pubmed:dateRevised |
2011-11-14
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| pubmed:year |
2010
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| pubmed:articleTitle |
Autoproteolytic activation of bacterial toxins.
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| pubmed:affiliation |
Department of Pathology, Stanford School of Medicine, 300 Pasteur Drive, Stanford, California 94305, USA; Email: ashen2@stanford.edu ; Tel.: +1-650-736-4099;
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| pubmed:publicationType |
Journal Article
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