Agency
National Institute of Health (NIH)
Institute
National Cancer Institute (NCI)
Type
Exploratory Grants (P20)
Project #
5P20CA060171-03
Application #
2339025
Study Section
Project Start
Project End
Budget Start
Budget End
Support Year
3
Fiscal Year
1995
Total Cost
Indirect Cost
Name
Case Western Reserve University
Department
Type
DUNS #
077758407
City
Cleveland
State
OH
Country
United States
Zip Code
44106
Chen, W S; Kung, H J; Yang, W K et al. (1999) Comparative tyrosine-kinase profiles in colorectal cancers: enhanced arg expression in carcinoma as compared with adenoma and normal mucosa. Int J Cancer 83:579-84
Qiu, Y; Robinson, D; Pretlow, T G et al. (1998) Etk/Bmx, a tyrosine kinase with a pleckstrin-homology domain, is an effector of phosphatidylinositol 3'-kinase and is involved in interleukin 6-induced neuroendocrine differentiation of prostate cancer cells. Proc Natl Acad Sci U S A 95:3644-9
McKeon, R J; Silver, J; Large, T H (1997) Expression of full-length trkB receptors by reactive astrocytes after chronic CNS injury. Exp Neurol 148:558-67
Zhang, D; Jacobberger, J W (1996) TGF-beta 1 perturbation of the fibroblast cell cycle during exponential growth: switching between negative and positive regulation. Cell Prolif 29:289-307
Garner, A S; Menegay, H J; Boeshore, K L et al. (1996) Expression of TrkB receptor isoforms in the developing avian visual system. J Neurosci 16:1740-52
Ling, L; Templeton, D; Kung, H J (1996) Identification of the major autophosphorylation sites of Nyk/Mer, an NCAM-related receptor tyrosine kinase. J Biol Chem 271:18355-62
Ling, L; Kung, H J (1995) Mitogenic signals and transforming potential of Nyk, a newly identified neural cell adhesion molecule-related receptor tyrosine kinase. Mol Cell Biol 15:6582-92
Garner, A S; Large, T H (1994) Isoforms of the avian TrkC receptor: a novel kinase insertion dissociates transformation and process outgrowth from survival. Neuron 13:457-72
Shu, H K; Chang, C M; Ravi, L et al. (1994) Modulation of erbB kinase activity and oncogenic potential by single point mutations in the glycine loop of the catalytic domain. Mol Cell Biol 14:6868-78