Abstract
Protein phosphorylation plays a crucial role in regulating a plethora of intracellular biological activities. Because protein phosphorylation is a reversible reaction, it allows living cells to reset to the basal state rapidly after stimulation. There are hundreds of protein kinases involved in this general signaling machinery. These kinases are classified into three different categories based on their abilities to phosphorylate serine/threonine, or tyrosine, or both residues A comparison of primary sequences of protein kinases has indicated that the catalytic site (the kinase domain) is highly conserved, suggesting a common ancestor for these kinases (1) However, different kinases have evolved to function distinctly in response to diverse cellular stimuli. The specificities of protein kinases has thus become a critical issue in understanding signal transduction.
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© 1998 Humana Press Inc., Totowa, NJ
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Songyang, Z., Cantley, L.C. (1998). The Use of Peptide Library for the Determination of Kinase Peptide Substrates. In: Cabilly, S. (eds) Combinatorial Peptide Library Protocols. Methods in Molecular Biology™, vol 87. Humana Press. https://doi.org/10.1385/0-89603-392-9:87
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DOI: https://doi.org/10.1385/0-89603-392-9:87
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