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- W1968369969 endingPage "81" @default.
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- W1968369969 abstract "Phosphorylation regulates the conformation, stability, homo- and heterotypic protein interactions, localization, and activity of the tumor suppressor PTEN. From a simple picture, at the beginning of this millennium, recognizing that CK2 phosphorylated PTEN at the C-terminus and thereby impacted on PTEN stability and activity, research has led to a significantly more complex scenario today, where for instance GSK3, Plk3, ATM, ROCK or Src-family kinases are also gaining the spotlight in this evolving play. Here, we review the current knowledge on the kinases that phosphorylate PTEN, and on the impact that specific phosphorylation events have on PTEN function." @default.
- W1968369969 created "2016-06-24" @default.
- W1968369969 creator A5031794454 @default.
- W1968369969 creator A5038469796 @default.
- W1968369969 date "2015-05-01" @default.
- W1968369969 modified "2023-10-13" @default.
- W1968369969 title "Kinases, tails and more: Regulation of PTEN function by phosphorylation" @default.
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- W1968369969 doi "https://doi.org/10.1016/j.ymeth.2014.10.015" @default.
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- W1968369969 hasPublicationYear "2015" @default.
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