Biological activity of the Helicobacter pylori virulence factor CagA is determined by variation in the tyrosine phosphorylation sites

By H. Higashi, Ryouhei Tsutsumi, A. Fujita, S. Yamazaki, M. Asaka, T. Azuma, Masanori Hatakeyama. Proceedings of the National Academy of Sciences of the United States of America, 2002

607 citations recorded by the source corpus.

Subfields: Immunology, Small Animals, Surgery

View Paper: https://www.semanticscholar.org/paper/4df6b3366a6941eb537d4990fa82e963205feca2

How researchers see this paper

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In Immunology

1. E. Kuipers
2. A. V. van Vliet
3. J. G. Kusters
4. Masanori Hatakeyama

In Small Animals

1. E. Kuipers
2. A. V. van Vliet
3. J. G. Kusters
4. Masanori Hatakeyama

In Surgery

1. E. Kuipers
2. A. V. van Vliet
3. J. G. Kusters
4. Masanori Hatakeyama

Citations in the corpus

• Pathogenesis of Helicobacter pylori Infection (2006, background): “Tyrosine phosphorylation occurs within the CagA EPIYA motif and is required for the binding of CagA to SHP-2 (27, 594, 636).”
• Oncogenic mechanisms of the Helicobacter pylori CagA protein (2004, background): “Tyrosine phosphorylation of CagA occurs at the EPIYA motif — a 5-amino-acid sequence (Glu-Pro-Ile-Tyr-Alu) that is present in the carboxy-terminal variable region of the protei”