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Structural mechanisms determining inhibition of the collagen receptor DDR1 by selective and multi-targeted type II kinase inhibitors

Abstract:

The discoidin domain receptors (DDRs), DDR1 and DDR2, form a unique subfamily of receptor tyrosine kinases that are activated by the binding of triple-helical collagen. Excessive signaling by DDR1 and DDR2 has been linked to the progression of various human diseases, including fibrosis, atherosclerosis and cancer. We report the inhibition of these unusual receptor tyrosine kinases by the multi-targeted cancer drugs imatinib and ponatinib, as well as the selective type II inhibitor DDR1-IN-1. ...

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Publisher copy:
10.1016/j.jmb.2014.04.014

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Publisher:
Academic Press
Journal:
Journal of Molecular Biology
Volume:
426
Issue:
13
Pages:
2457-2470
Publication date:
2014-06-26
DOI:
EISSN:
1089-8638
ISSN:
0022-2836
Source identifiers:
470233
Language:
English
Keywords:
Pubs id:
pubs:470233
UUID:
uuid:1175950c-22bb-4294-9627-bc0c9db69c4b
Local pid:
pubs:470233
Deposit date:
2014-07-03

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