Results 201 to 210 of about 153,756 (258)
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Current Opinion in Immunology, 1991
In the past year, significant progress in the area of Fc receptor biology has been made in three areas: identification of the protective FcR for serum IgG half-life (Brambell receptor), characterization of the mechanism(s) of inhibitory receptor Fc gamma RIIB signaling, and dissection of the in vivo roles of FcRs in inflammation.
J V, Ravetch, J P, Kinet
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In the past year, significant progress in the area of Fc receptor biology has been made in three areas: identification of the protective FcR for serum IgG half-life (Brambell receptor), characterization of the mechanism(s) of inhibitory receptor Fc gamma RIIB signaling, and dissection of the in vivo roles of FcRs in inflammation.
J V, Ravetch, J P, Kinet
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Annual Review of Immunology, 2001
Since the description of the first mouse knockout for an IgG Fc receptor seven years ago, considerable progress has been made in defining the in vivo functions of these receptors in diverse biological systems. The role of activating FcγRs in providing a critical link between ligands and effector cells in type II and type III inflammation is now well ...
J V, Ravetch, S, Bolland
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Since the description of the first mouse knockout for an IgG Fc receptor seven years ago, considerable progress has been made in defining the in vivo functions of these receptors in diverse biological systems. The role of activating FcγRs in providing a critical link between ligands and effector cells in type II and type III inflammation is now well ...
J V, Ravetch, S, Bolland
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1994
Immune complex cross-linking of cell surface receptors for immunoglobulin (Ig) triggers pleiotropic cellular events that underpin a wide variety of immune responses. In this fashion receptors for immunoglobulin form a molecular bridge between the humoral and cellular immune responses.
D, Brooks, J V, Ravetch
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Immune complex cross-linking of cell surface receptors for immunoglobulin (Ig) triggers pleiotropic cellular events that underpin a wide variety of immune responses. In this fashion receptors for immunoglobulin form a molecular bridge between the humoral and cellular immune responses.
D, Brooks, J V, Ravetch
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2005
Fc receptors for immunoglobulin A (IgA) have been recognized functionally for many years. The myeloid receptor, FcαRI, is the most thoroughly characterized. It is structurally related to the FcγRs and Fce{open}RI and also associates with the FcR γ chain dimer.
Woof, Jenny M. +2 more
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Fc receptors for immunoglobulin A (IgA) have been recognized functionally for many years. The myeloid receptor, FcαRI, is the most thoroughly characterized. It is structurally related to the FcγRs and Fce{open}RI and also associates with the FcR γ chain dimer.
Woof, Jenny M. +2 more
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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
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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
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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
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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
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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
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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
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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
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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
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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 ...
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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 ...
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