Agency
National Institute of Health (NIH)
Institute
National Cancer Institute (NCI)
Type
Research Project (R01)
Project #
5R01CA058667-03
Application #
2099359
Study Section
Medical Biochemistry Study Section (MEDB)
Project Start
1993-02-01
Project End
1997-01-31
Budget Start
1995-02-01
Budget End
1997-01-31
Support Year
3
Fiscal Year
1995
Total Cost
Indirect Cost
Name
University of Nebraska Medical Center
Department
Internal Medicine/Medicine
Type
Schools of Medicine
DUNS #
City
Omaha
State
NE
Country
United States
Zip Code
68198
Delfino, Frank J; Stevenson, Heather; Smithgall, Thomas E (2006) A growth-suppressive function for the c-fes protein-tyrosine kinase in colorectal cancer. J Biol Chem 281:8829-35
Delfino, Frank J; Shaffer, Jonathan M; Smithgall, Thomas E (2006) The KRAB-associated co-repressor KAP-1 is a coiled-coil binding partner, substrate and activator of the c-Fes protein tyrosine kinase. Biochem J 399:141-50
Meyn 3rd, Malcolm A; Schreiner, Steven J; Dumitrescu, Teodora Pene et al. (2005) SRC family kinase activity is required for murine embryonic stem cell growth and differentiation. Mol Pharmacol 68:1320-30
Laurent, Charles E; Delfino, Frank J; Cheng, Haiyun Y et al. (2004) The human c-Fes tyrosine kinase binds tubulin and microtubules through separate domains and promotes microtubule assembly. Mol Cell Biol 24:9351-8
Laurent, Charles E; Smithgall, Thomas E (2004) The c-Fes tyrosine kinase cooperates with the breakpoint cluster region protein (Bcr) to induce neurite extension in a Rac- and Cdc42-dependent manner. Exp Cell Res 299:188-98
Shibata, Annemarie; Laurent, Charles E; Smithgall, Thomas E (2003) The c-Fes protein-tyrosine kinase accelerates NGF-induced differentiation of PC12 cells through a PI3K-dependent mechanism. Cell Signal 15:279-88
Takashima, Yoshio; Delfino, Frank J; Engen, John R et al. (2003) Regulation of c-Fes tyrosine kinase activity by coiled-coil and SH2 domains: analysis with Saccharomyces cerevisiae. Biochemistry 42:3567-74
Cheng, H Y; Schiavone, A P; Smithgall, T E (2001) A point mutation in the N-terminal coiled-coil domain releases c-Fes tyrosine kinase activity and survival signaling in myeloid leukemia cells. Mol Cell Biol 21:6170-80
Kanda, S; Lerner, E C; Tsuda, S et al. (2000) The nonreceptor protein-tyrosine kinase c-Fes is involved in fibroblast growth factor-2-induced chemotaxis of murine brain capillary endothelial cells. J Biol Chem 275:10105-11
Rogers, J A; Cheng, H Y; Smithgall, T E (2000) Src homology 2 domain substitution modulates the kinase and transforming activities of the Fes protein-tyrosine kinase. Cell Growth Differ 11:581-92

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