Analysis of protein tyrosine phosphatases and substrates
F Mercan, AM Bennett - Current protocols in molecular biology, 2010 - Wiley Online Library
Current protocols in molecular biology, 2010•Wiley Online Library
Protein tyrosine phosphorylation is a reversible post‐translational modification that is
essential for life in eukaryotic cells. The combinatorial action of both protein tyrosine kinases
and protein tyrosine phosphatases (PTPs) determines the net level of cellular tyrosine
phosphorylation. This unit discusses methods to determine the level of protein tyrosine
phosphatase activity and methods for discovering novel substrates for protein tyrosine
phosphatases. Curr. Protoc. Mol. Biol. 91: 18.16. 1‐18.16. 17.© 2010 by John Wiley & Sons …
essential for life in eukaryotic cells. The combinatorial action of both protein tyrosine kinases
and protein tyrosine phosphatases (PTPs) determines the net level of cellular tyrosine
phosphorylation. This unit discusses methods to determine the level of protein tyrosine
phosphatase activity and methods for discovering novel substrates for protein tyrosine
phosphatases. Curr. Protoc. Mol. Biol. 91: 18.16. 1‐18.16. 17.© 2010 by John Wiley & Sons …
Abstract
Protein tyrosine phosphorylation is a reversible post‐translational modification that is essential for life in eukaryotic cells. The combinatorial action of both protein tyrosine kinases and protein tyrosine phosphatases (PTPs) determines the net level of cellular tyrosine phosphorylation. This unit discusses methods to determine the level of protein tyrosine phosphatase activity and methods for discovering novel substrates for protein tyrosine phosphatases. Curr. Protoc. Mol. Biol. 91:18.16.1‐18.16.17. © 2010 by John Wiley & Sons, Inc.
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