Structure of C3b in complex with CRIg gives insights into regulation of complement activation-Reference-Cited by-同舟云学术

Structure of C3b in complex with CRIg gives insights into regulation of complement activation

Published:2006-10-15 Issue:7116 Volume:444 Page:217-220
ISSN:0028-0836
Container-title:Nature
language:en
Short-container-title:Nature

Author:

Wiesmann Christian,Katschke Kenneth J.,Yin JianPing,Helmy Karim Y.,Steffek Micah,Fairbrother Wayne J.,McCallum Scott A.,Embuscado Lizette,DeForge Laura,Hass Philip E.,van Lookeren Campagne Menno

Publisher

Springer Science and Business Media LLC

Subject

Multidisciplinary

Link

http://www.nature.com/articles/nature05263.pdf

Reference23 articles.

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2. Pangburn, M. K. & Muller-Eberhard, H. J. Relation of putative thioester bond in C3 to activation of the alternative pathway and the binding of C3b to biological targets of complement. J. Exp. Med. 152, 1102–1114 (1980)

3. Fishelson, Z., Pangburn, M. K. & Muller-Eberhard, H. J. C3 convertase of the alternative complement pathway. Demonstration of an active, stable C3b, Bb (Ni) complex. J. Biol. Chem. 258, 7411–7415 (1983)

4. Muller-Eberhard, H. J. & Schreiber, R. D. Molecular biology and chemistry of the alternative pathway of complement. Adv. Immunol. 29, 1–53 (1980)

5. Helmy, K. Y. et al. CRIg: a macrophage complement receptor required for phagocytosis of circulating pathogens. Cell 124, 915–927 (2006)

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