Fc Receptors edited by Marc Daeron, Falk Nimmerjahn.

This volume provides a state-of-the-art update on Fc Receptors (FcRs). It is divided into five parts. Part I, Old and New FcRs, deals with the long-sought-after FcµR and the recently discovered FCRL family and TRIM21. Part II, FcR Signaling, presents a computational model of FcεRI signaling, novel c...

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Bibliographic Details
Corporate Author: SpringerLink (Online service)
Other Authors: Daeron, Marc (Editor), Nimmerjahn, Falk (Editor)
Format: eBook
Language:English
Published: Cham : Springer International Publishing : Imprint: Springer, 2014.
Edition:1st ed. 2014.
Series:Current Topics in Microbiology and Immunology, 382
Springer eBook Collection.
Subjects:
Online Access:Click to view e-book
Holy Cross Note:Loaded electronically.
Electronic access restricted to members of the Holy Cross Community.
Table of Contents:
  • The Old but New IgM Fc Receptor (FcμR)
  • Emerging Roles for FCRL Family Members in Lymphocyte Biology and Disease
  • Intracellular antibody immunity and the cytosolic Fc receptor TRIM21
  • Computational modeling of the main signaling pathways involved in mast cell activation
  • Calcium channels in FcR signaling
  • Regulation of FcεRI signaling by lipid phosphatases
  • Fc Receptors as Adaptive Immunoreceptors
  • Glycosylation and Fc Receptors
  • Antibodies as natural adjuvants
  • IgA, IgA receptors and their anti-inflammatory properties
  • Humanized mice to study FcγR function
  • FcRn: from molecular interactions to regulation of IgG pharmacokinetics and functions
  • Human FcR polymorphism and disease
  • Bridging auto-antibodies and arthritis; the role of Fc Receptors
  • The FcγR of humans and non-human primates and their interaction with IgG: Implications for induction of inflammation, resistance to infection and the use of therapeutic monoclonal antibodies
  • FcgRIIB as a key determinant of agonistic antibody efficacy
  • Fc receptor dependent mechanisms of monoclonal antibody therapy of cancer; professionals at work
  • Sweet and Sour: The role of glycosylation for the anti-inflammatory activity of immunoglobulin G.