Search Results - "Chou, Robert Y.‐T."
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Conformational Difference in Human IgG2 Disulfide Isoforms Revealed by Hydrogen/Deuterium Exchange Mass Spectrometry
Published in Biochemistry (Easton) (17-03-2015)“…Both recombinant and natural human IgG2 antibodies have several different disulfide bond isoforms, which possess different global structures, thermal…”
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Field flow fractionation for assessing neonatal Fc receptor and Fcγ receptor binding to monoclonal antibodies in solution
Published in Analytical biochemistry (01-07-2011)“…Analysis of the strength and stoichiometry of immunoglobulin G (IgG) binding to neonatal Fc receptor (FcRn) and Fcγ receptor (FcγR) is important for evaluating…”
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Impact of antibody subclass and disulfide isoform differences on the biological activity of CD200R and βklotho agonist antibodies
Published in Biochemical and biophysical research communications (13-05-2017)“…Agonism of cell surface receptors by monoclonal antibodies is dependent not only on its ability to bind the target, but also to deliver a biological signal…”
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Protected hinge in the immunoglobulin G2‐A2 disulfide isoform
Published in Protein science (01-12-2014)“…Human IgG2 consists of disulfide‐mediated structural isoforms, classified by the number of Fab arms disulfide‐linked to the heavy chain hinge. In the IgG2‐B…”
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Protected hinge in the immunoglobulin G2-A sub(2) disulfide isoform
Published in Protein science (01-12-2014)“…Human IgG2 consists of disulfide-mediated structural isoforms, classified by the number of Fab arms disulfide-linked to the heavy chain hinge. In the IgG2-B…”
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Protected hinge in the immunoglobulin G2‐A 2 disulfide isoform
Published in Protein science (01-12-2014)“…Abstract Human IgG2 consists of disulfide‐mediated structural isoforms, classified by the number of Fab arms disulfide‐linked to the heavy chain hinge. In the…”
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