Agency
National Institute of Health (NIH)
Institute
National Cancer Institute (NCI)
Type
Method to Extend Research in Time (MERIT) Award (R37)
Project #
3R37CA017542-18S1
Application #
3481763
Study Section
Experimental Virology Study Section (EVR)
Project Start
1978-12-01
Project End
1994-11-30
Budget Start
1992-12-01
Budget End
1993-11-30
Support Year
18
Fiscal Year
1993
Total Cost
Indirect Cost
Name
University of California Berkeley
Department
Type
Schools of Arts and Sciences
DUNS #
094878337
City
Berkeley
State
CA
Country
United States
Zip Code
94704
Gottlieb-Abraham, Efrat; Shvartsman, Dmitry E; Donaldson, John C et al. (2013) Src-mediated caveolin-1 phosphorylation affects the targeting of active Src to specific membrane sites. Mol Biol Cell 24:3881-95
Rodriguez, Elena M; Dunham, Elizabeth E; Martin, G Steven (2009) Atypical protein kinase C activity is required for extracellular matrix degradation and invasion by Src-transformed cells. J Cell Physiol 221:171-82
Martin, G Steven (2009) SRC substrate surprise. Cancer Cell 16:176-8
Shvartsman, Dmitry E; Donaldson, John C; Diaz, Begona et al. (2007) Src kinase activity and SH2 domain regulate the dynamics of Src association with lipid and protein targets. J Cell Biol 178:675-86
Zhu, Qingwei; Krakowski, Ariel R; Dunham, Elizabeth E et al. (2007) Dual role of SnoN in mammalian tumorigenesis. Mol Cell Biol 27:324-39
Jackson, William T; Martin, G Steven (2006) Transcription of the Schizosaccharomyces pombe gene cdc18+: roles of MCB elements and the DSC1 complex. Gene 369:100-8
Prathapam, Tulsiram; Tegen, Sarah; Oskarsson, Thordur et al. (2006) Activated Src abrogates the Myc requirement for the G0/G1 transition but not for the G1/S transition. Proc Natl Acad Sci U S A 103:2695-700
Berdeaux, Rebecca L; Diaz, Begona; Kim, Lomi et al. (2004) Active Rho is localized to podosomes induced by oncogenic Src and is required for their assembly and function. J Cell Biol 166:317-23
Martin, G Steven (2004) The road to Src. Oncogene 23:7910-7
He, Jun; Tegen, Sarah B; Krawitz, Ariel R et al. (2003) The transforming activity of Ski and SnoN is dependent on their ability to repress the activity of Smad proteins. J Biol Chem 278:30540-7

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