Results 211 to 220 of about 159,070 (244)
Some of the next articles are maybe not open access.
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
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
openaire +2 more sources
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
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
Fc Receptors in Human Placenta
Scandinavian Journal of Immunology, 1975Cryostat sections of placental tissue strongly adsorbed erythrocytes sensitized with IgG antibodies of human, rabbit, and guinea pig origin No adsorption occurred using erythrocytes sensitized with F(ab')2fragments The reaction was strongly inhibited by intact IgG and by Fc fragments, weakly inhibited by pFc' fragments, and not inhibited by Facb and F ...
R, Matre, O, Tönder, C, Endresen
openaire +2 more sources
Scandinavian Journal of Immunology, 1976
The function of Fc receptors (FcR) on mouse spleen cells as detected by a sensitive resetting system using antibody‐labeled bovine erythrocytes as indicator cells was shown to be inhibited by anti‐Ia antiserum. Furthermore, the la specificities of each I‐region sublocus (I‐1A, I‐1B I‐C) seem to be associated with FcR, since FcR function was also ...
P H, Krammer, B, Pernis
openaire +2 more sources
The function of Fc receptors (FcR) on mouse spleen cells as detected by a sensitive resetting system using antibody‐labeled bovine erythrocytes as indicator cells was shown to be inhibited by anti‐Ia antiserum. Furthermore, the la specificities of each I‐region sublocus (I‐1A, I‐1B I‐C) seem to be associated with FcR, since FcR function was also ...
P H, Krammer, B, Pernis
openaire +2 more sources
Antibodies, Fc receptors and cancer
Current Opinion in Immunology, 2007Since the first report of the successful use of a monoclonal antibody for the treatment of human B cell lymphoma in 1982, several antibodies have become incorporated into standard treatment protocols for cancer. One of the most important factors that determine antibody activity in vivo is the efficient interaction with cellular Fc-receptors on innate ...
Falk, Nimmerjahn, Jeffrey V, Ravetch
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
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
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
Fc receptors in livestock species
Veterinary Immunology and Immunopathology, 2004Many of the receptors for the Fc domain of immunoglobulins in cattle, sheep, pigs and horses have been cloned and characterized recently. This review summarises recent developments and relates them to the current understanding of the primary structure, cellular specificity and binding properties of Fc receptors (FcRs).
openaire +2 more sources