Fc-Associated Effector Functions CH 2 Domain of Murine IgG 1 on Impact of a Three Amino Acid Deletion in the Nishimura
暂无分享,去创建一个
S. Nishimura | F. Nimmerjahn | J. Verbeek | S. Izui | L. Baudino | Jeffery V. Ravetch | J. Furukawa | Y. Shinohara | F. Petry | J. Ravetch
[1] J. Ravetch,et al. Differential Contribution of Three Activating IgG Fc Receptors (FcγRI, FcγRIII, and FcγRIV) to IgG2a- and IgG2b-Induced Autoimmune Hemolytic Anemia in Mice1 , 2008, The Journal of Immunology.
[2] M. Nakano,et al. Comprehensive approach to structural and functional glycomics based on chemoselective glycoblotting and sequential tag conversion. , 2008, Analytical chemistry.
[3] A. Blom,et al. Endoglycosidase treatment abrogates IgG arthritogenicity: Importance of IgG glycosylation in arthritis , 2007, European journal of immunology.
[4] Yoshiaki Miura,et al. Quantitative Glycomics of Human Whole Serum Glycoproteins Based on the Standardized Protocol for Liberating N-Glycans *S , 2007, Molecular & Cellular Proteomics.
[5] Y. Miura,et al. Rapid and simple solid-phase esterification of sialic acid residues for quantitative glycomics by mass spectrometry. , 2007, Chemistry.
[6] J. Ravetch,et al. Agalactosylated IgG antibodies depend on cellular Fc receptors for in vivo activity , 2007, Proceedings of the National Academy of Sciences.
[7] J. Ravetch,et al. Anti-Inflammatory Activity of Immunoglobulin G Resulting from Fc Sialylation , 2006, Science.
[8] M. Madaio,et al. The Journal of Experimental Medicine CORRESPONDENCE , 2005 .
[9] J. Ravetch,et al. Divergent Immunoglobulin G Subclass Activity Through Selective Fc Receptor Binding , 2005, Science.
[10] Hiroaki Nakagawa,et al. High Throughput Quantitative Glycomics and Glycoform-focused Proteomics of Murine Dermis and Epidermis* , 2005, Molecular & Cellular Proteomics.
[11] P. Bruhns,et al. FcγRIV : A novel FcR with distinct IgG subclass specificity , 2005 .
[12] M. Walport,et al. Complement Activation Selectively Potentiates the Pathogenicity of the IgG2b and IgG3 Isotypes of a High Affinity Anti-Erythrocyte Autoantibody , 2002, The Journal of experimental medicine.
[13] M. Walport,et al. Reconstitution of the Complement Function in C1q-Deficient (C1qa−/−) Mice with Wild-Type Bone Marrow Cells1 , 2001, The Journal of Immunology.
[14] P. Parren,et al. The IgG Fc Contains Distinct Fc Receptor (FcR) Binding Sites: The Leukocyte Receptors FcγRI and FcγRIIa Bind to a Region in the Fc Distinct from That Recognized by Neonatal FcR and Protein A1 , 2000, The Journal of Immunology.
[15] T. Honjo,et al. High Pathogenic Potential of Low-Affinity Autoantibodies in Experimental Autoimmune Hemolytic Anemia , 1999, The Journal of experimental medicine.
[16] R. Schmidt,et al. FcγRIII (CD16)-Deficient Mice Show IgG Isotype-Dependent Protection to Experimental Autoimmune Hemolytic Anemia , 1998 .
[17] R. Jefferis,et al. Multiple interactions of IgG with its core oligosaccharide can modulate recognition by complement and human Fc gamma receptor I and influence the synthesis of its oligosaccharide chains. , 1996, Journal of immunology.
[18] R. Schmidt,et al. Impaired IgG-Dependent Anaphylaxis and Arthus Reaction in FcγRIII (CD16) Deficient Mice , 1996 .
[19] M. Ono,et al. Augmented humoral and anaphylactic responses in FcγRII-deficient mice , 1996, Nature.
[20] R. Dwek,et al. Glycosylation changes of IgG associated with rheumatooid arthritis can activate complement via the mannose-binding protein , 1995, Nature Medicine.
[21] S L Morrison,et al. Effect of altered CH2-associated carbohydrate structure on the functional properties and in vivo fate of chimeric mouse-human immunoglobulin G1 , 1994, The Journal of experimental medicine.
[22] J. Ravetch,et al. FcR γ chain deletion results in pleiotrophic effector cell defects , 1994, Cell.
[23] S. Morrison,et al. Structural features of human immunoglobulin G that determine isotype- specific differences in complement activation , 1993, The Journal of experimental medicine.
[24] M. Klein,et al. Identification of the Fc gamma receptor class I binding site in human IgG through the use of recombinant IgG1/IgG2 hybrid and point-mutated antibodies. , 1991, Proceedings of the National Academy of Sciences of the United States of America.
[25] S. Morrison,et al. The binding affinity of human IgG for its high affinity Fc receptor is determined by multiple amino acids in the CH2 domain and is modulated by the hinge region , 1991, The Journal of experimental medicine.
[26] T. Berney,et al. Monoclonal anti-erythrocyte autoantibodies derived from NZB mice cause autoimmune hemolytic anemia by two distinct pathogenic mechanisms. , 1990, International immunology.
[27] K. Titani,et al. Structural changes in the oligosaccharide chains of IgG in autoimmune MRL/Mp-lpr/lpr mice. , 1990, Journal of immunology.
[28] D. Sears,et al. Molecular cloning and expression of the mouse high affinity Fc receptor for IgG. , 1990, Journal of immunology.
[29] S. Ho,et al. Site-directed mutagenesis by overlap extension using the polymerase chain reaction. , 1989, Gene.
[30] J. Ravetch,et al. Function and regulation of a murine macrophage-specific IgG Fc receptor, Fc gamma R-alpha , 1988, The Journal of experimental medicine.
[31] G. Winter,et al. The binding site for C1q on IgG , 1988, Nature.
[32] D. Burton,et al. Localization of the binding site for the human high-affinity Fc receptor on IgG , 1988, Nature.
[33] R. Dwek,et al. Association of rheumatoid arthritis and primary osteoarthritis with changes in the glycosylation pattern of total serum IgG , 1985, Nature.
[34] H. Wigzell,et al. Biological significance of carbohydrate chains on monoclonal antibodies. , 1983, Proceedings of the National Academy of Sciences of the United States of America.
[35] M. Pepys,et al. Activation of mouse complement by different classes of mouse antibody. , 1979, Immunology.
[36] J. Ravetch,et al. Fcgamma receptors: old friends and new family members. , 2006, Immunity.
[37] Hiroaki Nakagawa,et al. High-throughput protein glycomics: combined use of chemoselective glycoblotting and MALDI-TOF/TOF mass spectrometry. , 2004, Angewandte Chemie.