Syk, a Protein-tyrosine Kinase, Suppresses the Cell Motility and Nuclear Factor κB-mediated Secretion of Urokinase Type Plasminogen Activator by Inhibiting the Phosphatidylinositol 3′-Kinase Activity in Breast Cancer Cells

This publication has 34 references indexed in Scilit:

• The N-terminal SH2 Domains of Syk and ZAP-70 Mediate Phosphotyrosine-independent Binding to Integrin β Cytoplasmic Domains
  Published by Elsevier ,2002
• Functional dissection of BCR signaling pathways
  Current Opinion in Immunology, 2000
• Tyrosine kinase SYK: essential functions for immunoreceptor signalling
  Immunology Today, 2000
• The Syk and ZAP-70 SH2-containing tyrosine kinases are implicated in pre-T cell receptor signaling
  Proceedings of the National Academy of Sciences, 1997
• Molecular Characterization of the Murine SYK Protein Tyrosine Kinase cDNA, Transcripts and Protein
  Biochemical and Biophysical Research Communications, 1995
• The structure and function of nonreceptor tyrosine kinase p72syk expressed in hematopoietic cells
  Cellular Signalling, 1995
• LDL receptor-related protein internalizes and degrades uPA-PAI-1 complexes and is essential for embryo implantation
  Cell, 1992
• The role of urokinase-type plasminogen activator in aggressive tumor cell behavior
  Cancer and Metastasis Reviews, 1990
• Plasminogen activators in tissue remodeling and invasion: mRNA localization in mouse ovaries and implanting embryos.
  The Journal of cell biology, 1989
• Plasminogen activator in early embryogenesis: Enzyme production by trophoblast and parietal endoderm
  Cell, 1976