Structural basis of specific and efficient phosphorylation of peptides derived from p34cdc2 by a pp60src-related protein tyrosine kinase.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference27 articles.
1. Universal control mechanism regulating onset of M-phase
2. Tyrosine phosphorylation of the fission yeast cdc2+ protein kinase regulates entry into mitosis
3. Purification and characterization of a pp60c-src-related tyrosine kinase that effectively phosphorylates a synthetic peptide derived from p34cdc2
4. Protein kinase recognition sequence motifs
5. Phosphorylation of synthetic peptides by a tyrosine protein kinase from the particulate fraction of a lymphoma cell line.
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1. Sensitive FRET Biosensor Reveals Fyn Kinase Regulation by Submembrane Localization;ACS Sensors;2018-12-27
2. Common and differential recognition of structural features in synthetic peptides by the catalytic domain and the Src-Homology 2 (SH2) domain of pp60c-src;The Journal of Peptide Research;2009-01-12
3. Substrate phosphorylation capacities of the major tyrosine protein kinase from the human promyelocytic cell line, HL-60;International Journal of Peptide and Protein Research;2009-01-12
4. Solid-phase synthesis of (tyrosyl-alanyl-glutamyl)n, by segment condensation;International Journal of Peptide and Protein Research;2009-01-12
5. Cyclic peptide substrates of pp60c-src;International Journal of Peptide and Protein Research;2009-01-12
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