A carboxyl-terminal mutation of the epidermal growth factor receptor alters tyrosine kinase activity and substrate specificity as measured by a fluorescence polarization assay

Journal of Biological Chemistry

Volumn 278, Issue 29, 2003, Pages 26810-26816

  Beebe, Jane A ^a   Wiepz, Gregory J ^b   Guadarrama, Arturo G ^b   Bertics, Paul J ^b   Burke, Thomas J ^a,c  

^a INVITROGEN CORPORATION   (United States)

^b UNIVERSITY OF WISCONSIN MADISON   (United States)

^c NONE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; COPOLYMERS; FLUORESCENCE; POLARIZATION; PROTEINS; SUBSTRATES;

RECEPTORS;

CELLS;

ADAPTOR PROTEIN; ANGIOTENSIN; EPIDERMAL GROWTH FACTOR RECEPTOR; ISOENZYME; PHOSPHOLIPASE C; PROTEIN SHC; PROTEIN TYROSINE KINASE;

ARTICLE; AUTOPHOSPHORYLATION; BINDING SITE; CARBOXY TERMINAL SEQUENCE; CELL TRANSFORMATION; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME SPECIFICITY; FILTRATION; FLUORESCENCE POLARIZATION IMMUNOASSAY; GENE MUTATION; HUMAN; HUMAN CELL; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN PHOSPHORYLATION; STEADY STATE;

BINDING SITES; BINDING, COMPETITIVE; CELL LINE; CELL TRANSFORMATION, NEOPLASTIC; FLUORESCENCE POLARIZATION; HUMANS; KINETICS; PHOSPHORYLATION; RECEPTOR, EPIDERMAL GROWTH FACTOR; RECOMBINANT PROTEINS; SEQUENCE DELETION; SUBSTRATE SPECIFICITY;

CHEN;

EID: 0037698027     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M301397200     Document Type: Article

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