Protein tyrosine phosphatases: from genes, to function, to disease

By N. Tonks. Nature reviews. Molecular cell biology, 2006

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A dynamic pathway for calcium-independent activation of CaMKII by methionine oxidation. (2008, background): “, 2006), while oxidation-dependent inactivation of protein phosphatases (Tonks, 2006) and activation of upstream kinase kinases, such as IKK-b (Reynaert et al.”
ROS Function in Redox Signaling and Oxidative Stress (2014, background): “However, RTKs andPI3K are negatively regulated by protein tyrosine phosphatases (PTPs) and the phosphatase (and tumor suppressor) PTEN, respectively, resulting in dampening of mitogenic signaling [19,20].”
Nitric oxide and redox mechanisms in the immune response (2011, background): “PTPs contain cysteinyl residues in their catalytic site, which when oxidized by ROS, results in inactivation of the phosphatase [217, 218].”
The crucial role of protein phosphorylation in cell signaling and its use as targeted therapy (Review) (2017, neutral): “Of all the phosphatases, at least 100 belong to those that dephosphorylate tyrosine residues, such as the Tyr-specific phosphatase subfamily, the Cdc25 family and myotubularin-related phosphatase and low molecular weight Tyr phosphatase (12,14,32,33,39,40).”
Dual-specificity phosphatases: critical regulators with diverse cellular targets. (2009, background): “and Tonks, N. K. (2004) Characterization of two distinct”