pH-dependent binding engineering reveals an FcRn affinity threshold that governs IgG recycling.
about
Targeting FcRn for the modulation of antibody dynamicsPredicting pharmacokinetic profile of therapeutic antibodies after iv injection from only the data after sc injection in cynomolgus monkey.A novel in vitro assay to predict neonatal Fc receptor-mediated human IgG half-life.Engineering a pH responsive pore forming protein.The multiple facets of FcRn in immunity.Utility of a human FcRn transgenic mouse model in drug discovery for early assessment and prediction of human pharmacokinetics of monoclonal antibodies.An antidote approach to reduce risk and broaden utility of antibody-based therapeutics.Enhancement of antibody functions through Fc multiplications.Identification of human IgG1 variant with enhanced FcRn binding and without increased binding to rheumatoid factor autoantibody.Maximizing in vivo target clearance by design of pH-dependent target binding antibodies with altered affinity to FcRn.Conformational Destabilization of Immunoglobulin G Increases the Low pH Binding Affinity with the Neonatal Fc Receptor.DMAb inoculation of synthetic cross reactive antibodies protects against lethal influenza A and B infections.Rapid Purification of Human Bispecific Antibodies via Selective Modulation of Protein A Binding.A human endothelial cell-based recycling assay for screening of FcRn targeted molecules.Changes in complementarity-determining regions significantly alter IgG binding to the neonatal Fc receptor (FcRn) and pharmacokinetics.
P2860
Q28080589-DCA80840-6F99-4826-BF1F-456EA1E080DCQ31091923-11CFA03B-D584-42C3-B90C-80DA7EE8604CQ36211427-39EEE5DC-03BA-4835-82D1-42130B8366F1Q37630482-23FF4DE4-BAD7-46F4-BF10-AE846DC37958Q38615385-DB2F52CA-EAD8-4448-BCD8-E14CBA1E6933Q39731345-5231366B-1180-4109-BBAC-A8395EC72560Q40309222-4C6D5013-3609-4038-9BB3-81CC9422FC91Q40365750-39B566CC-BEF5-4441-90DA-E2836A3C3CF6Q41104888-F4137AED-2A3D-4D46-8F80-154D88176217Q42135303-243EA9B2-3DD6-4C26-9B2F-5B4D47814810Q42690323-D35E85BB-97C2-4EE9-B20E-E54586C6D9FAQ47125106-85510F2B-F40D-47FC-AC42-1B00D96706B2Q47147171-F57D2F70-2F38-416E-A4C1-448AE71E2CAAQ49179176-60169F52-985D-44A9-8401-EC425235FA25Q54979517-8E843DDD-091A-46F9-8A89-4C514C9E7723
P2860
pH-dependent binding engineering reveals an FcRn affinity threshold that governs IgG recycling.
description
2014 nî lūn-bûn
@nan
2014 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2014年の論文
@ja
2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
@wuu
name
pH-dependent binding engineeri ...... ld that governs IgG recycling.
@ast
pH-dependent binding engineeri ...... ld that governs IgG recycling.
@en
type
label
pH-dependent binding engineeri ...... ld that governs IgG recycling.
@ast
pH-dependent binding engineeri ...... ld that governs IgG recycling.
@en
prefLabel
pH-dependent binding engineeri ...... ld that governs IgG recycling.
@ast
pH-dependent binding engineeri ...... ld that governs IgG recycling.
@en
P2093
P2860
P356
P1476
pH-dependent binding engineeri ...... ld that governs IgG recycling.
@en
P2093
M Jack Borrok
Nurten Beyaz
William F Dall'Acqua
Xiang-Qing Yu
P2860
P304
P356
10.1074/JBC.M114.603712
P407
P577
2014-12-23T00:00:00Z