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http://purl.uniprot.org/citations/12062101http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12062101http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12062101http://www.w3.org/2000/01/rdf-schema#comment"A Yersinia effector known as YopT and a Pseudomonas avirulence protein known as AvrPphB define a family of 19 proteins involved in bacterial pathogenesis. We show that both YopT and AvrPphB are cysteine proteases, and their proteolytic activities are dependent upon the invariant C/H/D residues conserved in the entire YopT family. YopT cleaves the posttranslationally modified Rho GTPases near their carboxyl termini, releasing them from the membrane. This leads to the disruption of actin cytoskeleton in host cells. The proteolytic activity of AvrPphB is essential for autoproteolytic cleavage of an AvrPphB precursor as well as for eliciting the hypersensitive response in plants. These findings provide new insights into mechanisms of animal and plant pathogenesis."xsd:string
http://purl.uniprot.org/citations/12062101http://purl.org/dc/terms/identifier"doi:10.1016/s0092-8674(02)00766-3"xsd:string
http://purl.uniprot.org/citations/12062101http://purl.org/dc/terms/identifier"doi:10.1016/s0092-8674(02)00766-3"xsd:string
http://purl.uniprot.org/citations/12062101http://purl.uniprot.org/core/author"Bao Z."xsd:string
http://purl.uniprot.org/citations/12062101http://purl.uniprot.org/core/author"Bao Z."xsd:string
http://purl.uniprot.org/citations/12062101http://purl.uniprot.org/core/author"Shao F."xsd:string
http://purl.uniprot.org/citations/12062101http://purl.uniprot.org/core/author"Shao F."xsd:string
http://purl.uniprot.org/citations/12062101http://purl.uniprot.org/core/author"Dixon J.E."xsd:string
http://purl.uniprot.org/citations/12062101http://purl.uniprot.org/core/author"Dixon J.E."xsd:string
http://purl.uniprot.org/citations/12062101http://purl.uniprot.org/core/author"Innes R.W."xsd:string
http://purl.uniprot.org/citations/12062101http://purl.uniprot.org/core/author"Innes R.W."xsd:string
http://purl.uniprot.org/citations/12062101http://purl.uniprot.org/core/author"Merritt P.M."xsd:string
http://purl.uniprot.org/citations/12062101http://purl.uniprot.org/core/author"Merritt P.M."xsd:string
http://purl.uniprot.org/citations/12062101http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12062101http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12062101http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/12062101http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/12062101http://purl.uniprot.org/core/pages"575-588"xsd:string
http://purl.uniprot.org/citations/12062101http://purl.uniprot.org/core/pages"575-588"xsd:string
http://purl.uniprot.org/citations/12062101http://purl.uniprot.org/core/title"A Yersinia effector and a Pseudomonas avirulence protein define a family of cysteine proteases functioning in bacterial pathogenesis."xsd:string
http://purl.uniprot.org/citations/12062101http://purl.uniprot.org/core/title"A Yersinia effector and a Pseudomonas avirulence protein define a family of cysteine proteases functioning in bacterial pathogenesis."xsd:string
http://purl.uniprot.org/citations/12062101http://purl.uniprot.org/core/volume"109"xsd:string
http://purl.uniprot.org/citations/12062101http://purl.uniprot.org/core/volume"109"xsd:string