Engineered soluble monomeric IgG1 CH3 domain generation, mechanisms of function, and implications for design of biological therapeutics

Journal of Biological Chemistry

Volumn 288, Issue 35, 2013, Pages 25154-25164

  Ying, Tianlei ^a   Chen, Weizao ^a   Feng, Yang ^a   Wang, Yanping ^a,b   Gong, Rui ^a   Dimitrov, Dimiter S ^a  

^a NATIONAL CANCER INSTITUTE   (United States)

^b SAIC FREDERICK INC   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL THERAPEUTICS; FUSION PARTNERS; HOMODIMERS; PH-DEPENDENT; THERAPEUTIC EFFICACY; THERAPEUTIC PROTEIN;

SCAFFOLDS;

PROTEINS;

FC RECEPTOR; HYBRID PROTEIN; IMMUNOGLOBULIN G1; SOLUBLE MONOMERIC IGG1 CH3; UNCLASSIFIED DRUG;

ARTICLE; BINDING KINETICS; DIMERIZATION; DISULFIDE BOND; ESCHERICHIA COLI; HALF LIFE TIME; PH; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN ENGINEERING; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN ISOLATION; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; SOLUBILITY; THERMOSTABILITY; WILD TYPE;

ANTIBODY ENGINEERING; FUSION PROTEIN; PROTEIN ENGINEERING; PROTEIN STABILITY; SURFACE PLASMON RESONANCE (SPR);

CASPASE 7; ESCHERICHIA COLI; GENE EXPRESSION; HISTOCOMPATIBILITY ANTIGENS CLASS I; HUMANS; IMMUNOGLOBULIN G; PROTEIN BINDING; PROTEIN ENGINEERING; PROTEIN STABILITY; PROTEIN STRUCTURE, TERTIARY; RECEPTORS, FC; RECOMBINANT FUSION PROTEINS;

EID: 84883404242     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.484154     Document Type: Article

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