Conformational changes in IgE contribute to its uniquely slow dissociation rate from receptor FcɛRI-Reference-Cited by-同舟云学术

Conformational changes in IgE contribute to its uniquely slow dissociation rate from receptor FcɛRI

Published:2011-04-24 Issue:5 Volume:18 Page:571-576
ISSN:1545-9993
Container-title:Nature Structural & Molecular Biology
language:en
Short-container-title:Nat Struct Mol Biol

Author:

Holdom Mary D,Davies Anna M,Nettleship Joanne E,Bagby Sarah C,Dhaliwal Balvinder,Girardi Enrico,Hunt James,Gould Hannah J,Beavil Andrew J,McDonnell James M,Owens Ray J,Sutton Brian J

Publisher

Springer Science and Business Media LLC

Subject

Molecular Biology,Structural Biology

Link

http://www.nature.com/articles/nsmb.2044.pdf

Reference57 articles.

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2. Holgate, S. et al. The use of omalizumab in the treatment of severe allergic asthma: A clinical experience update. Respir. Med. 103, 1098–1113 (2009).

3. Gould, H.J. & Sutton, B.J. IgE in allergy and asthma today. Nat. Rev. Immunol. 8, 205–217 (2008).

4. Maenaka, K., van der Merwe, P.A., Stuart, D.I., Jones, E.Y. & Sondermann, P. The human low affinity Fcγ receptors IIa, IIb and III bind IgG with fast kinetics and distinct thermodynamic properties. J. Biol. Chem. 276, 44898–44904 (2001).

5. Gould, H.J. et al. The biology of IgE and the basis of allergic disease. Annu. Rev. Immunol. 21, 579–628 (2003).

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