Agency
National Institute of Health (NIH)
Institute
National Cancer Institute (NCI)
Type
Research Project (R01)
Project #
5R01CA027951-18
Application #
2390636
Study Section
Cellular Biology and Physiology Subcommittee 1 (CBY)
Project Start
1980-05-01
Project End
1997-07-14
Budget Start
1997-04-01
Budget End
1997-07-14
Support Year
18
Fiscal Year
1997
Total Cost
Indirect Cost
Name
Ariad Pharmaceuticals, Inc.
Department
Type
DUNS #
City
Cambridge
State
MA
Country
United States
Zip Code
02139
Miranti, C K; Ohno, S; Brugge, J S (1999) Protein kinase C regulates integrin-induced activation of the extracellular regulated kinase pathway upstream of Shc. J Biol Chem 274:10571-81
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Miranti, C K; Leng, L; Maschberger, P et al. (1998) Identification of a novel integrin signaling pathway involving the kinase Syk and the guanine nucleotide exchange factor Vav1. Curr Biol 8:1289-99
Rickles, R J; Botfield, M C; Zhou, X M et al. (1995) Phage display selection of ligand residues important for Src homology 3 domain binding specificity. Proc Natl Acad Sci U S A 92:10909-13
Shiue, L; Zoller, M J; Brugge, J S (1995) Syk is activated by phosphotyrosine-containing peptides representing the tyrosine-based activation motifs of the high affinity receptor for IgE. J Biol Chem 270:10498-502
Weng, Z; Rickles, R J; Feng, S et al. (1995) Structure-function analysis of SH3 domains: SH3 binding specificity altered by single amino acid substitutions. Mol Cell Biol 15:5627-34
Shiue, L; Green, J; Green, O M et al. (1995) Interaction of p72syk with the gamma and beta subunits of the high-affinity receptor for immunoglobulin E, Fc epsilon RI. Mol Cell Biol 15:272-81
Weng, Z; Thomas, S M; Rickles, R J et al. (1994) Identification of Src, Fyn, and Lyn SH3-binding proteins: implications for a function of SH3 domains. Mol Cell Biol 14:4509-21
Rickles, R J; Botfield, M C; Weng, Z et al. (1994) Identification of Src, Fyn, Lyn, PI3K and Abl SH3 domain ligands using phage display libraries. EMBO J 13:5598-604
Clark, E A; Shattil, S J; Brugge, J S (1994) Regulation of protein tyrosine kinases in platelets. Trends Biochem Sci 19:464-9

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