<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">van der Poel, Cees E</style></author><author><style face="normal" font="default" size="100%">Spaapen, Robbert M</style></author><author><style face="normal" font="default" size="100%">van de Winkel, Jan G J</style></author><author><style face="normal" font="default" size="100%">Leusen, Jeanette H W</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Functional characteristics of the high affinity IgG receptor, FcγRI.</style></title><secondary-title><style face="normal" font="default" size="100%">J Immunol</style></secondary-title><alt-title><style face="normal" font="default" size="100%">J. Immunol.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Amino Acid Sequence</style></keyword><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Antigen Presentation</style></keyword><keyword><style  face="normal" font="default" size="100%">Antigen-Antibody Complex</style></keyword><keyword><style  face="normal" font="default" size="100%">Binding Sites, Antibody</style></keyword><keyword><style  face="normal" font="default" size="100%">Disease Models, Animal</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Molecular Sequence Data</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Binding</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Structure, Tertiary</style></keyword><keyword><style  face="normal" font="default" size="100%">Receptors, IgG</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2011</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2011 Mar 1</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">186</style></volume><pages><style face="normal" font="default" size="100%">2699-704</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;IgG FcRs are important mediators of immunity and play a key role during Ab-based immunotherapy. Within the leukocyte IgG receptor family, only FcγRI is capable of IgG binding with high affinity. FcγRI exists as a complex of a ligand binding α-chain and an FcR γ-chain. The receptors&#039; α-chain can, furthermore, elicit several functions independent of the ITAM-bearing FcR γ-chain. Functional implications of high-affinity IgG binding and mechanisms underlying FcR γ-chain-independent signaling remain unclear to this day. In this paper, we provide an overview of past literature on FcγRI and address the implications of recently described interactions between cytosolic proteins and the FcγRI α-chain, as well as cytokine-enhanced FcγRI immune complex binding. Furthermore, an analysis of potential polymorphisms within the FCGR1A gene is provided.&lt;/p&gt;
</style></abstract><issue><style face="normal" font="default" size="100%">5</style></issue><custom1><style face="normal" font="default" size="100%">&lt;p&gt;http://www.ncbi.nlm.nih.gov/pubmed/21325219?dopt=Abstract&lt;/p&gt;
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