Agency
National Institute of Health (NIH)
Institute
National Cancer Institute (NCI)
Type
Unknown (R35)
Project #
5R35CA044356-10
Application #
2091449
Study Section
Special Emphasis Panel (SRC (88))
Project Start
1994-07-26
Project End
2001-04-30
Budget Start
1996-05-01
Budget End
1997-04-30
Support Year
10
Fiscal Year
1996
Total Cost
Indirect Cost
Name
Rockefeller University
Department
Internal Medicine/Medicine
Type
Other Domestic Higher Education
DUNS #
071037113
City
New York
State
NY
Country
United States
Zip Code
10065
Kirsch, Kathrin; Kensinger, Margaret; Hanafusa, Hidesaburo et al. (2002) A p130Cas tyrosine phosphorylated substrate domain decoy disrupts v-crk signaling. BMC Cell Biol 3:18
Kirsch, K H; Georgescu, M M; Shishido, T et al. (2001) The adapter type protein CMS/CD2AP binds to the proto-oncogenic protein c-Cbl through a tyrosine phosphorylation-regulated Src homology 3 domain interaction. J Biol Chem 276:4957-63
Shishido, T; Akagi, T; Chalmers, A et al. (2001) Crk family adaptor proteins trans-activate c-Abl kinase. Genes Cells 6:431-40
Shishido, T; Akagi, T; Ouchi, T et al. (2000) The kinase-deficient Src acts as a suppressor of the Abl kinase for Cbl phosphorylation. Proc Natl Acad Sci U S A 97:6439-44
Akagi, T; Shishido, T; Murata, K et al. (2000) v-Crk activates the phosphoinositide 3-kinase/AKT pathway in transformation. Proc Natl Acad Sci U S A 97:7290-5
Wong, B R; Besser, D; Kim, N et al. (1999) TRANCE, a TNF family member, activates Akt/PKB through a signaling complex involving TRAF6 and c-Src. Mol Cell 4:1041-9
Georgescu, M M; Kirsch, K H; Shishido, T et al. (1999) Biological effects of c-Mer receptor tyrosine kinase in hematopoietic cells depend on the Grb2 binding site in the receptor and activation of NF-kappaB. Mol Cell Biol 19:1171-81
Besser, D; Bromberg, J F; Darnell Jr, J E et al. (1999) A single amino acid substitution in the v-Eyk intracellular domain results in activation of Stat3 and enhances cellular transformation. Mol Cell Biol 19:1401-9
Kirsch, K H; Georgescu, M M; Ishimaru, S et al. (1999) CMS: an adapter molecule involved in cytoskeletal rearrangements. Proc Natl Acad Sci U S A 96:6211-6
Georgescu, M M; Kirsch, K H; Akagi, T et al. (1999) The tumor-suppressor activity of PTEN is regulated by its carboxyl-terminal region. Proc Natl Acad Sci U S A 96:10182-7

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