Full-length p40phox structure suggests a basis for regulation mechanism of its membrane binding-Reference-Cited by-同舟云学术

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Full-length p40phox structure suggests a basis for regulation mechanism of its membrane binding

Published:2007-02-08 Issue:4 Volume:26 Page:1176-1186
ISSN:0261-4189
Container-title:The EMBO Journal
language:
Short-container-title:EMBO J

Author:

Honbou Kazuya,Minakami Reiko,Yuzawa Satoru,Takeya Ryu,Suzuki Nobuo N,Kamakura Sachiko,Sumimoto Hideki,Inagaki Fuyuhiko

Publisher

Wiley

Subject

General Immunology and Microbiology,General Biochemistry, Genetics and Molecular Biology,Molecular Biology,General Neuroscience

Reference51 articles.

1. Phosphorylation of p47phox directs phox homology domain from SH3 domain toward phosphoinositides, leading to phagocyte NADPH oxidase activation

2. The PX Domain as a Novel Phosphoinositide- Binding Module

3. p40 Is Phosphorylated on Threonine 154 and Serine 315 during Activation of the Phagocyte NADPH Oxidase

4. The Crystal Structure of the PX Domain from p40phox Bound to Phosphatidylinositol 3-Phosphate

5. Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

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