Source:http://linkedlifedata.com/resource/pubmed/id/22069620
| Subject | Predicate | Object | Context |
|---|---|---|---|
| pubmed-article:22069620 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:22069620 | lifeskim:mentions | umls-concept:C0004630 | lld:lifeskim |
| pubmed-article:22069620 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:22069620 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:22069620 | pubmed:dateCreated | 2011-11-9 | lld:pubmed |
| pubmed-article:22069620 | 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. | lld:pubmed |
| pubmed-article:22069620 | pubmed:language | eng | lld:pubmed |
| pubmed-article:22069620 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:22069620 | pubmed:status | PubMed-not-MEDLINE | lld:pubmed |
| pubmed-article:22069620 | pubmed:month | May | lld:pubmed |
| pubmed-article:22069620 | pubmed:issn | 2072-6651 | lld:pubmed |
| pubmed-article:22069620 | pubmed:author | pubmed-author:ShenAimeeA | lld:pubmed |
| pubmed-article:22069620 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:22069620 | pubmed:volume | 2 | lld:pubmed |
| pubmed-article:22069620 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:22069620 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:22069620 | pubmed:pagination | 963-77 | lld:pubmed |
| pubmed-article:22069620 | pubmed:dateRevised | 2011-11-14 | lld:pubmed |
| pubmed-article:22069620 | pubmed:year | 2010 | lld:pubmed |
| pubmed-article:22069620 | pubmed:articleTitle | Autoproteolytic activation of bacterial toxins. | lld:pubmed |
| pubmed-article:22069620 | 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; | lld:pubmed |
| pubmed-article:22069620 | pubmed:publicationType | Journal Article | lld:pubmed |