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Identification of a tyrosine-phosphorylated 35 kDa carboxy-terminal fragment (p35(CagA)) of the Helicobacter pylori CagA protein in phagocytic cells: Processing or breakage?

MPS-Authors
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Moese,  Stefan
Department of Molecular Biology, Max Planck Institute for Infection Biology, Max Planck Society;

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Selbach,  Matthias
Department of Molecular Biology, Max Planck Institute for Infection Biology, Max Planck Society;

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Zimny-Arndt,  Ursula
Core Facilities / Proteinanalysis, Max Planck Institute for Infection Biology, Max Planck Society;

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Jungblut,  Peter R.
Core Facilities / Proteinanalysis, Max Planck Institute for Infection Biology, Max Planck Society;

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Meyer,  Thomas F.
Department of Molecular Biology, Max Planck Institute for Infection Biology, Max Planck Society;

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Backert,  Steffen
Department of Molecular Biology, Max Planck Institute for Infection Biology, Max Planck Society;

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Citation

Moese, S., Selbach, M., Zimny-Arndt, U., Jungblut, P. R., Meyer, T. F., & Backert, S. (2001). Identification of a tyrosine-phosphorylated 35 kDa carboxy-terminal fragment (p35(CagA)) of the Helicobacter pylori CagA protein in phagocytic cells: Processing or breakage? Proteomics, 1(4), 618-629. doi:10.1002/1615-9861(200104)1:4<618:AID-PROT618>3.0.CO;2-C.


Cite as: http://hdl.handle.net/11858/00-001M-0000-000E-C76D-7
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