Agency
National Institute of Health (NIH)
Institute
National Cancer Institute (NCI)
Type
First Independent Research Support & Transition (FIRST) Awards (R29)
Project #
5R29CA061951-03
Application #
2102847
Study Section
Pathology B Study Section (PTHB)
Project Start
1994-01-18
Project End
1998-12-31
Budget Start
1996-01-01
Budget End
1996-12-31
Support Year
3
Fiscal Year
1996
Total Cost
Indirect Cost
Name
University of North Carolina Chapel Hill
Department
Pharmacology
Type
Schools of Medicine
DUNS #
078861598
City
Chapel Hill
State
NC
Country
United States
Zip Code
27599
Hansen, Malene; Rusyn, Elena V; Hughes, Paul E et al. (2002) R-Ras C-terminal sequences are sufficient to confer R-Ras specificity to H-Ras. Oncogene 21:4448-61
Cox, A D; Der, C J (1997) Farnesyltransferase inhibitors and cancer treatment: targeting simply Ras? Biochim Biophys Acta 1333:F51-71
Willumsen, B M; Cox, A D; Solski, P A et al. (1996) Novel determinants of H-Ras plasma membrane localization and transformation. Oncogene 13:1901-9
Cox, A D (1995) Mutation and analysis of prenylation signal sequences. Methods Enzymol 250:105-21
Lerner, E C; Qian, Y; Blaskovich, M A et al. (1995) Ras CAAX peptidomimetic FTI-277 selectively blocks oncogenic Ras signaling by inducing cytoplasmic accumulation of inactive Ras-Raf complexes. J Biol Chem 270:26802-6
Cox, A D; Solski, P A; Jordan, J D et al. (1995) Analysis of Ras protein expression in mammalian cells. Methods Enzymol 255:195-220
Cox, A D; Garcia, A M; Westwick, J K et al. (1994) The CAAX peptidomimetic compound B581 specifically blocks farnesylated, but not geranylgeranylated or myristylated, oncogenic ras signaling and transformation. J Biol Chem 269:19203-6
Cox, A D; Brtva, T R; Lowe, D G et al. (1994) R-Ras induces malignant, but not morphologic, transformation of NIH3T3 cells. Oncogene 9:3281-8
Cox, A D; Der, C J (1994) Biological assays for cellular transformation. Methods Enzymol 238:277-94