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pubmed-article:16618412pubmed:abstractTextHelicobacter pylori CagA-positive strain is associated with gastric adenocarcinoma. CagA is delivered into gastric epithelial cells, where it undergoes tyrosine phosphorylation at the EPIYA sites by Src family kinases (SFKs). Owing to homologous recombination within the 3'-region of the cagA gene, 4 distinct EPIYA sites, each of which is defined by surrounding sequences, are variably assembled in both number and order among CagA proteins from different clinical H pylori isolates. Tyrosine-phosphorylated CagA specifically binds and deregulates SHP-2 via the Western CagA-specific EPIYA-C or East Asian CagA-specific EPIYA-D site, and C-terminal Src kinase (Csk) via the EPIYA-A or EPIYA-B site. Here we investigated the influence of EPIYA-repeat polymorphism on the CagA activity.lld:pubmed
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pubmed-article:16618412pubmed:articleTitleInfluence of EPIYA-repeat polymorphism on the phosphorylation-dependent biological activity of Helicobacter pylori CagA.lld:pubmed
pubmed-article:16618412pubmed:affiliationDivision of Molecular Oncology, Institute for Genetic Medicine, Hokkaido University, Sapporo, Japan.lld:pubmed
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pubmed-article:16618412pubmed:publicationTypeComparative Studylld:pubmed
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