The dephosphorylation characteristics of the receptors for epidermal growth factor and platelet-derived growth factor in Swiss 3T3 cell membranes suggest differential regulation of receptor signalling by endogenous protein-tyrosine phosphatases
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(93)80352-U/fullpdf
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3. Protein phosphotyrosine phosphatase purified from the particulate fraction of human placenta dephosphorylates insulin and growth-factor receptors
4. Characterization of the major protein-tyrosine-phosphatases of human placenta.
5. Insulin receptor and epidermal growth factor receptor dephosphorylation by three major rat liver protein-tyrosine phosphatases expressed in a recombinant bacterial system
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1. α-Hemolysin-induced dephosphorylation of EGF receptor of A431 cells is carried out by rPTPσ;Biochemical and Biophysical Research Communications;2004-12
2. Identification of Epidermal Growth Factor Receptor as a Target of Cdc25A Protein Phosphatase;Journal of Biological Chemistry;2002-05
3. Signal Transduction Pathways of G Protein-coupled Receptors and Their Cross-Talk with Receptor Tyrosine Kinases: Lessons from Bradykinin Signaling;Current Medicinal Chemistry;2000-09-01
4. Perinuclear localization of the protein-tyrosine phosphatase SHP-1 and inhibition of epidermal growth factor-stimulated STAT1/3 activation in A431 cells;European Journal of Cell Biology;2000-04
5. Redox regulation of signal transduction in mammalian cells;Biochemical Pharmacology;2000-01
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