The SH2 domain of Abl kinases regulates kinase autophosphorylation by controlling activation loop accessibility

Nature Communications

Volumn 5, Issue , 2014, Pages

  Lamontanara, Allan Joaquim ^a   Georgeon, Sandrine ^a   Tria, Giancarlo ^b   Svergun, Dmitri I ^b   Hantschel, Oliver ^a,c  

^a EPFL   (Switzerland)

^b EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

^c ISREC Foundation Department in Translational Oncology   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

ABELSON KINASE; PHOSPHOTRANSFERASE INHIBITOR; PROTEIN SH2; BCR ABL PROTEIN; BCR PROTEIN, HUMAN; BREAKPOINT CLUSTER REGION PROTEIN;

ENZYME ACTIVITY; MOLECULAR ANALYSIS; PHOSPHORUS; PROTEIN;

ALLOSTERISM; ARTICLE; AUTOPHOSPHORYLATION; CONFORMATION; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME REGULATION; ESCHERICHIA COLI; GENE EXPRESSION SYSTEM; HUMAN; IN VITRO STUDY; LEUKEMOGENESIS; MUTATION; NONHUMAN; PROTEIN DOMAIN; PROTEIN INTERACTION; PROTEIN PHOSPHORYLATION; SIGNAL TRANSDUCTION; STRUCTURE ACTIVITY RELATION; METABOLISM; PHOSPHORYLATION; PHYSIOLOGY; PROTEIN TERTIARY STRUCTURE; SRC HOMOLOGY DOMAIN;

ENZYME ACTIVATION; FUSION PROTEINS, BCR-ABL; ONCOGENE PROTEINS V-ABL; PHOSPHORYLATION; PROTEIN STRUCTURE, TERTIARY; PROTO-ONCOGENE PROTEINS C-BCR; SRC HOMOLOGY DOMAINS;

EID: 84921336901     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms6470     Document Type: Article

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