title: Exploiting the selectivity of protein phosphatase 1 for pharmacological intervention.
abstract: Selective and reversible phosphorylation is one of the most common post-translational modifications of proteins. Although kinase inhibitors are popular in drug development programmes, selective pharmacological manipulation of phosphatase activity has been challenging to achieve. We review recent advances in the development of selective inhibitors of dephosphorylation events and discuss the potential applications of small-molecule phosphatase inhibitors.
authors.affiliation: MRC Laboratory of Molecular Biology, Cambridge, UK.
authors.forename: Pavel
authors.initials: P
authors.lastname: Tsaytler
authors.forename: Anne
authors.initials: A
authors.lastname: Bertolotti
mesh_terms: D004791:Enzyme Inhibitors / Q000494:pharmacology*; D015852:Eukaryotic Initiation Factor-2 / Q000378:metabolism; D006143:Guanabenz / Q000494:pharmacology; D006801:Humans; D008954:Models, Biological; D010766:Phosphorylation / Q000187:drug effects; D054645:Protein Phosphatase 1 / Q000037:antagonists & inhibitors* / Q000378:metabolism*; D015398:Signal Transduction / Q000187:drug effects*
chemical_list: D004791:Enzyme Inhibitors; D015852:Eukaryotic Initiation Factor-2; C087519:PPP1R15A protein, human; D054645:Protein Phosphatase 1; D006143:Guanabenz