Crystallization and structure determination of an autoimmune anti-poly(dT) immunoglobulin Fab fragment at 3.0 A resolution.
Cygler, M; Boodhoo, A; Lee, J S; Anderson, W F.
J Biol Chem
; 262(2): 643-8, 1987 Jan 15.
Artigo em Inglês | MEDLINE | ID: mdl-3805000
Sweet but dangerous - the role of immunoglobulin G glycosylation in autoimmunity and inflammation.
Immunoglobulin (Ig)G purified from human sera mirrors intravenous Ig human leucocyte antigen (HLA) reactivity and recognizes one's own HLA types, but may be masked by Fab complementarity-determining region peptide in the native sera.
An efficient process of generating bispecific antibodies via controlled Fab-arm exchange using culture supernatants.
The Emerging Importance of IgG Fab Glycosylation in Immunity.
Bispecific Anti-HIV-1 Antibodies with Enhanced Breadth and Potency.
Anti-Hinge Antibodies Recognize IgG Subclass- and Protease-Restricted Neoepitopes.
Molecular Basis of Assembly and Activation of Complement Component C1 in Complex with Immunoglobulin G1 and Antigen.
Biophysical characterization and structure of the Fab fragment from the NIST reference antibody, RM 8671.
Intra-spike crosslinking overcomes antibody evasion by HIV-1.
Influence of IgG Subclass on Human Antimannan Antibody-Mediated Resistance to Hematogenously Disseminated Candidiasis in Mice.