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Mutations in the non-catalytic domains of Fyn and Fgr tyrosine kinases reveal differences in mechanisms of their regulation.

作者信息

Rivero-Lezcano O M, Marcilla A, Robbins K C

机构信息

Laboratory of Cellular Development and Oncology, National Institute of Dental Research, National Institutes of Health, Bethesda, Maryland 20892-4330, USA.

出版信息

Oncogene. 1995 Dec 21;11(12):2675-9.

PMID:8545125
Abstract

Non-catalytic domains of tyrosine kinases from the Src family are believed to be regulated intra- and intermolecularly through protein-protein interactions. We have deleted the SH2 and SH3 domains from Fyn and Fgr and have generated two point mutations in residues completely conserved in all members of the Src family. The dramatically different biological effects of these mutations suggest that non-catalytic domains regulate Src family kinase activities through distinctly different mechanisms.

摘要

相似文献

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Oncogene. 1995 Dec 21;11(12):2675-9.
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