The Fab conformations in the solution structure of human immunoglobulin G4 (IgG4) restrict access to its Fc region: implications for functional activity.
Rayner, Lucy E; Hui, Gar Kay; Gor, Jayesh; Heenan, Richard K; Dalby, Paul A; Perkins, Stephen J.
J Biol Chem
; 289(30): 20740-56, 2014 Jul 25.
Artigo em Inglês | MEDLINE | ID: mdl-24876381
Molecular Basis of Assembly and Activation of Complement Component C1 in Complex with Immunoglobulin G1 and Antigen.
Bispecific Anti-HIV-1 Antibodies with Enhanced Breadth and Potency.
The Emerging Importance of IgG Fab Glycosylation in Immunity.
Intra-spike crosslinking overcomes antibody evasion by HIV-1.
Dynamics of inter-heavy chain interactions in human immunoglobulin G (IgG) subclasses studied by kinetic Fab arm exchange.
Improved Fab presentation on phage surface with the use of molecular chaperone coplasmid system.
Mutational landscape of antibody variable domains reveals a switch modulating the interdomain conformational dynamics and antigen binding.
TriFabs--Trivalent IgG-Shaped Bispecific Antibody Derivatives: Design, Generation, Characterization and Application for Targeted Payload Delivery.
Efficient generation of stable bispecific IgG1 by controlled Fab-arm exchange.
Facile single-molecule pull-down assay for analysis of endogenous proteins.