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XB-ART-37763
Cell. January 25, 2002; 108 (2): 247-59.

Autoinhibition of c-Abl.

Pluk H , Dorey K , Superti-Furga G .


Abstract
Despite years of investigation, the molecular mechanism responsible for regulation of the c-Abl tyrosine kinase has remained elusive. We now report inhibition of the catalytic activity of purified c-Abl in vitro, demonstrating that regulation is an intrinsic property of the molecule. We show that the interaction of the N-terminal 80 residues with the rest of the protein mediates autoregulation. This N-terminal "cap" is required to achieve and maintain inhibition, and its loss turns c-Abl into an oncogenic protein and contributes to deregulation of BCR-Abl.

PubMed ID: 11832214
Article link: Cell.

Genes referenced: abl1 bcr
Antibodies referenced:
Morpholinos referenced:

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