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Volumn 275, Issue 45, 2000, Pages 35631-35637

c-Abl has high intrinsic tyrosine kinase activity that is stimulated by mutation of the Src homology 3 domain and by autophosphorylation at two distinct regulatory tyrosines

(2) Brasher, Bradley B a Van Etten, Richard A a,b

a HARVARD MEDICAL SCHOOL (United States)

b CENTER FOR BLOOD RESEARCH (United States)

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN TYROSINE KINASE;

AMINO ACID SUBSTITUTION; ARTICLE; AUTOPHOSPHORYLATION; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME KINETICS; ENZYME PHOSPHORYLATION; GENE MUTATION; HUMAN; HUMAN CELL; PRIORITY JOURNAL; PROTEIN DOMAIN; SEQUENCE HOMOLOGY;

ANIMALS; BINDING SITES; CATALYTIC DOMAIN; DNA, COMPLEMENTARY; DOSE-RESPONSE RELATIONSHIP, DRUG; KINETICS; MICE; MODELS, BIOLOGICAL; MUTATION; PEPTIDES; PHENYLALANINE; PHOSPHORYLATION; POINT MUTATION; PROTEIN-TYROSINE KINASES; PROTO-ONCOGENE PROTEINS C-ABL; SRC HOMOLOGY DOMAINS; TIME FACTORS; TYROSINE;

EID: 0034634597 PISSN: 00219258 EISSN: None Source Type: Journal
DOI: 10.1074/jbc.M005401200 Document Type: Article

Times cited : (230)

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