Selective effect of poly(lysine) on the enhancement of the lyn tyrosine protein kinase activity. Increased specificity toward src peptides
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1992.tb16742.x/fullpdf
Reference26 articles.
1. 1. J. A. Cooper, and B. E. Kemp (1990 ) inPeptides and protein phosphorylation () pp.85 -113 , CRC Press, Boca Raton, FL.
2. Cloning of a complementary DNA for a protein-tyrosine kinase that specifically phosphorylates a negative regulatory site of p60c-src
3. Dephosphorylation or antibody binding to the carboxy terminus stimulates pp60c-src.
4. Regulation by the autophosphorylation site in overexpressed pp60c-src.
5. Phosphorylation of synthetic peptides by a tyrosine protein kinase from the particulate fraction of a lymphoma cell line.
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1. Synthetic Tyr-phospho and non-hydrolyzable phosphonopeptides as PTKs and TC-PTP inhibitors*;International Journal of Peptide and Protein Research;2009-01-12
2. Linear and cyclic synthetic peptides related to the main autophosphorylation site of the Src tyrosine kinases as substrates and inhibitors of Lyn †;International Journal of Peptide and Protein Research;2009-01-12
3. Spatial Conformation and Topography of the Tyrosine Aromatic Ring in Substrate Recognition by Protein Tyrosine Kinases;Journal of Medicinal Chemistry;2006-02-16
4. Conformational constraints of tyrosine in protein tyrosine kinase substrates: Information about preferred bioactive side-chain orientation;Biopolymers;2003
5. The C-terminus of NIPP1 (nuclear inhibitor of protein phosphatase-1) contains a novel binding site for protein phosphatase-1 that is controlled by tyrosine phosphorylation and RNA binding;BIOCHEM J;2000
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