Book ChapterDOI
Interactions of immunoglobulins outside the antigen-combining site.
Roald Nezlin,Victor Ghetie +1 more
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This article is published in Advances in Immunology.The article was published on 2004-01-01. It has received 79 citations till now.read more
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Journal ArticleDOI
Post-translational modifications in the context of therapeutic proteins
Gary Walsh,Royston Jefferis +1 more
TL;DR: A better understanding of the relationship between structure and function is understood for many PTMs but remains incomplete for others, particularly in the case of complex PTMs, such as glycosylation.
Journal ArticleDOI
Glycosylation as a strategy to improve antibody-based therapeutics
TL;DR: Current knowledge of methods and avenues for their exploitation in the clinic are summarized, which allow the production of rMAbs bearing pre-selected oligosaccharides — glycoforms — to provide maximum efficacy for a given disease indication.
Journal ArticleDOI
An overview of the last advances in probiotic and prebiotic field
TL;DR: The present review summarizes guidelines reported on the literature in regard to clinician or therapeutic trials of probiotic and prebiotic.
Journal ArticleDOI
Recombinant antibody therapeutics: the impact of glycosylation on mechanisms of action
TL;DR: It is demonstrated that, although accounting for only 2-3% of antibody mass, glycosylation of the IgG-Fc is essential to the activation of downstream biologic mechanisms (effector functions) and the precise structure of the attached oligosaccharide can influence biologic efficacy.
Journal ArticleDOI
Antibody therapeutics: isotype and glycoform selection.
TL;DR: The present understanding of the molecular interactions between IgG-Fc and effector ligands in vitro has allowed the generation of new antibody structures with altered/improved effector function profiles that may prove optimal for given disease indications.
References
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Journal ArticleDOI
The atomic structure of protein-protein recognition sites.
TL;DR: In this paper, the authors performed an analysis of the recognition sites seen in 75 protein-protein complexes of known three-dimensional structure: 24 protease-inhibitor, 19 antibody-antigen and 32 other complexes, including nine enzymeinhibitors and 11 that are involved in signal transduction.
Journal ArticleDOI
Chromatin–IgG complexes activate B cells by dual engagement of IgM and Toll-like receptors
Elizabeth A. Leadbetter,Ian R. Rifkin,Andreas Hohlbaum,Britte C. Beaudette,Mark J. Shlomchik,Ann Marshak-Rothstein +5 more
TL;DR: It is shown that effective activation of RF+ B cells is mediated by IgG2a–chromatin immune complexes and requires the synergistic engagement of the antigen receptor and a member of the MyD88-dependent Toll-like receptor (TLR) family.
Journal ArticleDOI
High Resolution Mapping of the Binding Site on Human IgG1 for FcγRI, FcγRII, FcγRIII, and FcRn and Design of IgG1 Variants with Improved Binding to the FcγR
Robert L. Shields,Angela K. Namenuk,Kyu Hong,Y. Gloria Meng,Julie Rae,Josephine P. Briggs,Dong Xie,Jadine Lai,Andrew Stadlen,Betty Li,Judith A. Fox,Leonard G. Presta +11 more
TL;DR: Select IgG1 variants with improved binding to FcγRIIIA exhibited up to 100% enhancement in antibody-dependent cell cytotoxicity using human effector cells; these variants included changes at residues not found at the binding interface in the IgG/Fcγ RIIIA co-crystal structure.
Journal ArticleDOI
IgG Fc Receptors
TL;DR: Fc gamma Rs offer a paradigm for the biological significance of balancing activation and inhibitory signaling in the expanding family of activation/inhibitory receptor pairs found in the immune system.
Journal ArticleDOI
Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A from Staphylococcus aureus at 2.9- and 2.8-A resolution.
TL;DR: The model of human Fc fragment was refined at 2.9-A resolution and the R value of the model is 0.24, with strong arguments that contact 1 is the fragment B-Fc contact formed in solution under physiological conditions, while contact 2 is a crystal contact.