Agency
National Institute of Health (NIH)
Institute
National Cancer Institute (NCI)
Type
Research Project (R01)
Project #
1R01CA071516-01
Application #
2115116
Study Section
Special Emphasis Panel (ZRG2-ALY (01))
Project Start
1996-07-01
Project End
1999-06-30
Budget Start
1996-07-01
Budget End
1997-06-30
Support Year
1
Fiscal Year
1996
Total Cost
Indirect Cost
Name
Washington University
Department
Internal Medicine/Medicine
Type
Schools of Medicine
DUNS #
062761671
City
Saint Louis
State
MO
Country
United States
Zip Code
63130
Kelly, M E; Chan, A C (2000) Regulation of B cell function by linker proteins. Curr Opin Immunol 12:267-75
Denny, M F; Kaufman, H C; Chan, A C et al. (1999) The lck SH3 domain is required for activation of the mitogen-activated protein kinase pathway but not the initiation of T-cell antigen receptor signaling. J Biol Chem 274:5146-52
Pappu, R; Cheng, A M; Li, B et al. (1999) Requirement for B cell linker protein (BLNK) in B cell development. Science 286:1949-54
Ishiai, M; Kurosaki, M; Pappu, R et al. (1999) BLNK required for coupling Syk to PLC gamma 2 and Rac1-JNK in B cells. Immunity 10:117-25
Minegishi, Y; Rohrer, J; Coustan-Smith, E et al. (1999) An essential role for BLNK in human B cell development. Science 286:1954-7
Bubeck-Wardenburg, J; Wong, J; Futterer, K et al. (1999) Regulation of antigen receptor function by protein tyrosine kinases. Prog Biophys Mol Biol 71:373-92
Wong, J; Straus, D; Chan, A C (1998) Genetic evidence of a role for Lck in T-cell receptor function independent or downstream of ZAP-70/Syk protein tyrosine kinases. Mol Cell Biol 18:2855-66
Fu, C; Turck, C W; Kurosaki, T et al. (1998) BLNK: a central linker protein in B cell activation. Immunity 9:93-103
Bubeck Wardenburg, J; Pappu, R; Bu, J Y et al. (1998) Regulation of PAK activation and the T cell cytoskeleton by the linker protein SLP-76. Immunity 9:607-16
Futterer, K; Wong, J; Grucza, R A et al. (1998) Structural basis for Syk tyrosine kinase ubiquity in signal transduction pathways revealed by the crystal structure of its regulatory SH2 domains bound to a dually phosphorylated ITAM peptide. J Mol Biol 281:523-37

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