High affinity IgG binding by FcγRI (CD64) is modulated by two distinct IgSF domains and the transmembrane domain of the receptor

Protein Engineering

Volumn 11, Issue 3, 1998, Pages 225-232

  Harrison, Patrick T ^a,b   Allen, Janet M ^a  

^a UNIVERSITY OF GLASGOW   (United Kingdom)

^b UNIVERSITY OF EDINBURGH   (United Kingdom)

Author keywords

chain; CD64; Fc RI; IgG; Receptor chimeras

Indexed keywords

FC RECEPTOR; IMMUNOGLOBULIN G ANTIBODY; MONOCLONAL ANTIBODY;

ANIMAL CELL; ANTIGEN BINDING; ARTICLE; BINDING SITE; CHIMERA; CONTROLLED STUDY; DIMERIZATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; RECEPTOR AFFINITY;

AMINO ACID SUBSTITUTION; ANIMALS; ANTIBODIES, MONOCLONAL; ANTIGEN-ANTIBODY REACTIONS; BINDING SITES; COS CELLS; EPITOPE MAPPING; GENE EXPRESSION; HUMANS; IMMUNOGLOBULIN G; IMMUNOGLOBULIN GAMMA-CHAINS; LIGANDS; MEMBRANE PROTEINS; PROTEIN BINDING; PROTEIN ENGINEERING; PROTEIN STRUCTURE, TERTIARY; RECEPTORS, IGG; RECOMBINANT FUSION PROTEINS; RESEARCH DESIGN; STRUCTURE-ACTIVITY RELATIONSHIP;

ANIMALIA; TRIXIS;

EID: 0031942822     PISSN: 02692139     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

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