Results 211 to 220 of about 153,756 (264)
Some of the next articles are maybe not open access.
International Reviews of Immunology, 1997
Human IgG receptors constitute a family of glycoprotein complexes consisting of ligand-binding, and associated signaling chains. Three leukocyte classes (Fc gamma RI, II, and III) and one separate endothelial Fc gamma R class (FcRB) are defined which are expressed on hematopoietic and endothelial cells.
I A, Heijnen, J G, van de Winkel
openaire +2 more sources
Human IgG receptors constitute a family of glycoprotein complexes consisting of ligand-binding, and associated signaling chains. Three leukocyte classes (Fc gamma RI, II, and III) and one separate endothelial Fc gamma R class (FcRB) are defined which are expressed on hematopoietic and endothelial cells.
I A, Heijnen, J G, van de Winkel
openaire +2 more sources
Immunologic Research, 2007
Immunoglobulin E (IgE) plays a central role in the pathogenesis of allergic diseases by interacting with two membrane receptors: high-affinity FcepsilonRI and low-affinity FcepsilonRII (CD23). Allergeninduced IgE-occupied FcepsilonRI aggregation on the mast cell or basophil cell surface leads to the activation of intracellular signaling events and ...
Ming, Zhang +2 more
openaire +2 more sources
Immunoglobulin E (IgE) plays a central role in the pathogenesis of allergic diseases by interacting with two membrane receptors: high-affinity FcepsilonRI and low-affinity FcepsilonRII (CD23). Allergeninduced IgE-occupied FcepsilonRI aggregation on the mast cell or basophil cell surface leads to the activation of intracellular signaling events and ...
Ming, Zhang +2 more
openaire +2 more sources
American Journal of Hematology, 1987
AbstractThe glycoprotein localization of the platelet binding site for the Fc IgG has been the subject of debate. We attempted to resolve this issue by relating the binding of radiolabeled IgG immune complexes composed of heat‐aggregated IgG to platelets from 1) healthy individuals; 2) an individual with Bernard‐Soulier syndrome lacking glycoproteins ...
J G, Kelton +4 more
openaire +2 more sources
AbstractThe glycoprotein localization of the platelet binding site for the Fc IgG has been the subject of debate. We attempted to resolve this issue by relating the binding of radiolabeled IgG immune complexes composed of heat‐aggregated IgG to platelets from 1) healthy individuals; 2) an individual with Bernard‐Soulier syndrome lacking glycoproteins ...
J G, Kelton +4 more
openaire +2 more sources
Herpesviral Fc receptors and their relationship to the human Fc receptors
Immunologic Research, 1992Nearly two decades ago, it was observed that cells infected with herpes simplex virus (HSV) acquired an IgG Fc binding activity. The properties of the viral Fc receptor (FcR) have now been characterized by several laboratories. The Fc binding activity appears on the surface of the infected cell prior to formation of progeny virions.
V, Litwin, C, Grose
openaire +2 more sources
Glycosylation and Fc Receptors
2014Immunoglobulins and Fc receptors are critical glycoprotein components of the immune system. Fc receptors bind the Fc (effector) region of antibody molecules and communicate information within the innate and adaptive immune systems. Glycosylation of antibodies, particularly in the Fc region of IgG, has been extensively studied in health and disease. The
Jerrard M, Hayes +6 more
openaire +2 more sources
Cell, 1994
Since their initial discovery over 30 years ago, cellular receptors for the Fc domain of immunoglobulins (FcRs) have posed something of an enigma for immunologists. These surface glycoproteins were known to be widely distributed on cells of the immune system, had specificity for different isotypes of immunoglobulin, and could mediate a variety of ...
openaire +2 more sources
Since their initial discovery over 30 years ago, cellular receptors for the Fc domain of immunoglobulins (FcRs) have posed something of an enigma for immunologists. These surface glycoproteins were known to be widely distributed on cells of the immune system, had specificity for different isotypes of immunoglobulin, and could mediate a variety of ...
openaire +2 more sources
Fc Receptor Homologs (FcRH1-5) Extend the Fc Receptor Family
2002Receptors for the Fc portion of immunoglobulins (FcR) are expressed broadly among cells of the immune system (Ravetch and Kinet 1991; Daeron 1997). The differential expression of these Ig isotope-specific receptors enable them to modulate cellular and humoral immunity by linking their antibody ligands with effector cells.
R S, Davis +3 more
openaire +2 more sources
Clinical Immunology and Immunopathology, 1989
Considerable recent progress has been made in our understanding of how IgG immune complexes interact with plasma membrane Fc receptors (FcR) to mediate a diversity of biological responses in man. These responses include endocytosis of antibody complexes; stimulation of the secretion of various inflammatory mediators such as enzymes, oxygen products ...
openaire +2 more sources
Considerable recent progress has been made in our understanding of how IgG immune complexes interact with plasma membrane Fc receptors (FcR) to mediate a diversity of biological responses in man. These responses include endocytosis of antibody complexes; stimulation of the secretion of various inflammatory mediators such as enzymes, oxygen products ...
openaire +2 more sources
Annual Review of Immunology, 2007
Discovery of a large family of Fc receptor-like (FCRL) molecules, homologous to the well-known receptors for the Fc portion of immunoglobulin (FCR), has uncovered an impressive abundance of immunoglobulin superfamily (IgSF) genes in the human 1q21–23 chromosomal region and revealed significant diversity for these genes between humans and mice.
openaire +2 more sources
Discovery of a large family of Fc receptor-like (FCRL) molecules, homologous to the well-known receptors for the Fc portion of immunoglobulin (FCR), has uncovered an impressive abundance of immunoglobulin superfamily (IgSF) genes in the human 1q21–23 chromosomal region and revealed significant diversity for these genes between humans and mice.
openaire +2 more sources
Springer Seminars in Immunopathology, 2006
FcgammaRs are a family of heterogeneous molecules that play opposite roles in immune response and control the effector functions of IgG antibodies. In many cancers, IgG antibodies are produced that recognize cancer cells, form immune complexes and therefore, activate FcgammaR.
Lydie, Cassard +5 more
openaire +2 more sources
FcgammaRs are a family of heterogeneous molecules that play opposite roles in immune response and control the effector functions of IgG antibodies. In many cancers, IgG antibodies are produced that recognize cancer cells, form immune complexes and therefore, activate FcgammaR.
Lydie, Cassard +5 more
openaire +2 more sources