Phosphorylation and structure-based functional studies reveal a positive and a negative role for the activation loop of the c-Abl tyrosine kinase

Oncogene

Volumn 20, Issue 56, 2001, Pages 8075-8084

  Dorey, Karel ^a   Engen, John R ^a,c   Kretzschmar, Jana ^a   Wilm, Matthias ^a   Neubauer, Gitte ^a   Schindler, Thomas ^b,d   Superti Furga, Giulio ^a  

^a EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

^b ROCKEFELLER UNIVERSITY   (United States)

^c LOS ALAMOS NATIONAL LABORATORY   (United States)

^d F HOFFMANN LA ROCHE LTD   (Switzerland)

Author keywords

Activation loop; Crystal structure; Phosphorylation; Tyrosine kinase

Indexed keywords

ABELSON KINASE; IMATINIB; PLATELET DERIVED GROWTH FACTOR; PROTEIN TYROSINE KINASE; UNCLASSIFIED DRUG;

ARTICLE; CATALYSIS; CELL DIFFERENTIATION; CELL GROWTH; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME ACTIVITY; GENE MUTATION; HUMAN; HUMAN CELL; PRIORITY JOURNAL; PROTEIN PHOSPHORYLATION;

BLOTTING, WESTERN; CATALYSIS; CELL LINE; ENZYME ACTIVATION; HUMANS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PHOSPHORYLATION; PHOSPHOTYROSINE; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; PROTO-ONCOGENE PROTEINS C-ABL; PROTO-ONCOGENE PROTEINS PP60(C-SRC); STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 0035819026     PISSN: 09509232     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.onc.1205017     Document Type: Article

References (39)