Thermodynamic mixing of molecular states of the epidermal growth factor receptor modulates macroscopic ligand binding affinity

Biochemical Journal

Volumn 352, Issue 1, 2000, Pages 99-108

  Holbrook, M R ^a   Slakey, L L ^a   Gross, D J ^a  

^a UNIVERSITY OF MASSACHUSETTS   (United States)

Author keywords

Dissociation constant; Equilibrium; ErbB family; Signalling

Indexed keywords

EPIDERMAL GROWTH FACTOR; EPIDERMAL GROWTH FACTOR RECEPTOR;

ANIMAL CELL; ARTICLE; BINDING AFFINITY; CHO CELL; DISSOCIATION CONSTANT; LIGAND BINDING; NONHUMAN; POINT MUTATION; PRIORITY JOURNAL; PROTEIN CONFORMATION; RECEPTOR AFFINITY; REGULATORY MECHANISM; THERMODYNAMICS;

ANIMALS; CHO CELLS; CRICETINAE; CYTOSOL; GLUTAMIC ACID; HUMANS; KINETICS; LIGANDS; MODELS, CHEMICAL; MUTAGENESIS, SITE-DIRECTED; PHORBOL ESTERS; PHOSPHORYLATION; POINT MUTATION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; RECEPTOR, EPIDERMAL GROWTH FACTOR; TETRADECANOYLPHORBOL ACETATE; THERMODYNAMICS; TUMOR CELLS, CULTURED; TYROSINE;

ANIMALIA; CRICETINAE; CRICETULUS GRISEUS;

EID: 0034668798     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/0264-6021:3520099     Document Type: Article

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