Linked Life Data

21325219

Source:http://linkedlifedata.com/resource/pubmed/id/21325219

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2011-2-17
pubmed:abstractText
IgG FcRs are important mediators of immunity and play a key role during Ab-based immunotherapy. Within the leukocyte IgG receptor family, only Fc?RI is capable of IgG binding with high affinity. Fc?RI exists as a complex of a ligand binding ?-chain and an FcR ?-chain. The receptors' ?-chain can, furthermore, elicit several functions independent of the ITAM-bearing FcR ?-chain. Functional implications of high-affinity IgG binding and mechanisms underlying FcR ?-chain-independent signaling remain unclear to this day. In this paper, we provide an overview of past literature on Fc?RI and address the implications of recently described interactions between cytosolic proteins and the Fc?RI ?-chain, as well as cytokine-enhanced Fc?RI immune complex binding. Furthermore, an analysis of potential polymorphisms within the FCGR1A gene is provided.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1550-6606
pubmed:author
pubmed:issnType
Electronic
pubmed:day
1
pubmed:volume
186
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2699-704
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
Functional characteristics of the high affinity IgG receptor, Fc?RI.
pubmed:affiliation
Immunotherapy Laboratory, Department of Immunology, University Medical Center, 3584 EA Utrecht, The Netherlands.
pubmed:publicationType
Journal Article, Comparative Study, Review