A transforming mutation enhances the activity of the c-Kit soluble tyrosine kinase domain

Biochemical Journal

Volumn 338, Issue 1, 1999, Pages 131-138

  Lam, Lily P Y ^b   Chow, Rowena Y K ^b   Berger, Stuart A ^a  

^a UNIVERSITY HEALTH NETWORK   (Canada)

^b NONE

Author keywords

Dimerization; Growth factor receptor; Mastocytoma; Pichia pastoris

Indexed keywords

ADENOSINE TRIPHOSPHATE; ANTIBODY; COMPLEMENTARY DNA; DIMER; MONOMER; MUTANT PROTEIN; PHOSPHOTYROSINE; PROTEIN TYROSINE KINASE; RECEPTOR; VANADIC ACID;

ARTICLE; AUTOPHOSPHORYLATION; CELL TRANSFORMATION; CONCENTRATION RESPONSE; CONTROLLED STUDY; DIMERIZATION; ENZYME KINETICS; ENZYME STRUCTURE; GEL FILTRATION; NONHUMAN; ONCOGENE C KIT; PICHIA PASTORIS; POINT MUTATION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN PHOSPHORYLATION;

ANIMALS; ANTIBODY AFFINITY; CATALYSIS; CELL FRACTIONATION; CELL TRANSFORMATION, NEOPLASTIC; CHROMATOGRAPHY, GEL; CYTOPLASM; ENZYME ACTIVATION; GENETIC VECTORS; MAST-CELL SARCOMA; MICE; MICROSPHERES; MUTAGENESIS, SITE-DIRECTED; PEPTIDE FRAGMENTS; PEPTIDES; PHOSPHORYLATION; PICHIA; PROTEIN-TYROSINE KINASES; PROTO-ONCOGENE PROTEINS C-KIT; SOLUBILITY; TUMOR CELLS, CULTURED; TYROSINE;

PICHIA PASTORIS;

EID: 0033557902     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/0264-6021:3380131     Document Type: Article

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