CDC14/YFR028C Literature Guide Help

Other names published for CDC14: OAF3, YFR028C

CDC14 - Protein Physical Properties (8)

ReferenceOther Genes Addressed
Bremmer SC, et al.  (2012) Cdc14 phosphatases preferentially dephosphorylate a subset of cyclin-dependent kinase (Cdk) sites containing phosphoserine. J Biol Chem 287(3):1662-9
Bouchoux C and Uhlmann F  (2011) A Quantitative Model for Ordered Cdk Substrate Dephosphorylation during Mitotic Exit. Cell 147(4):803-14
Eissler CL, et al.  (2011) A general strategy for studying multisite protein phosphorylation using label-free selected reaction monitoring mass spectrometry. Anal Biochem 418(2):267-75
Jones MH, et al.  (2011) Cell cycle phosphorylation of mitotic exit network (MEN) proteins. Cell Cycle 10(20):3435-40
Holt LJ, et al.  (2007) Evolution of Ime2 phosphorylation sites on Cdk1 substrates provides a mechanism to limit the effects of the phosphatase Cdc14 in meiosis. Mol Cell 25(5):689-702
Wang WQ, et al.  (2004) Kinetic and mechanistic studies of a cell cycle protein phosphatase Cdc14. J Biol Chem 279(29):30459-68
Gray CH, et al.  (2003) The structure of the cell cycle protein Cdc14 reveals a proline-directed protein phosphatase. EMBO J 22(14):3524-35
Taylor GS, et al.  (1997) The activity of Cdc14p, an oligomeric dual specificity protein phosphatase from Saccharomyces cerevisiae, is required for cell cycle progression. J Biol Chem 272(38):24054-63