标题
Protein phosphatases and their regulation in the control of mitosis
作者
关键词
-
出版物
EMBO REPORTS
Volume 13, Issue 3, Pages 197-203
出版商
Wiley
发表日期
2012-03-01
DOI
10.1038/embor.2011.263
参考文献
相关参考文献
注意:仅列出部分参考文献,下载原文获取全部文献信息。- PP1/Repo-Man Dephosphorylates Mitotic Histone H3 at T3 and Regulates Chromosomal Aurora B Targeting
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- Regulation of Greatwall kinase during Xenopus oocyte maturation
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- Phosphatases: providing safe passage through mitotic exit
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- Beyond the dopamine receptor: regulation and roles of serine/threonine protein phosphatases
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- Suppression of Scant Identifies Endos as a Substrate of Greatwall Kinase and a Negative Regulator of Protein Phosphatase 2A in Mitosis
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- Targeting Mitotic Exit Leads to Tumor Regression In Vivo: Modulation by Cdk1, Mastl, and the PP2A/B55α,δ Phosphatase
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- Shugoshin–PP2A counteracts casein-kinase-1-dependent cleavage of Rec8 by separase
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- Live-cell imaging RNAi screen identifies PP2A–B55α and importin-β1 as key mitotic exit regulators in human cells
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- Loss of human Greatwall results in G2 arrest and multiple mitotic defects due to deregulation of the cyclin B-Cdc2/PP2A balance
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- The Substrate of Greatwall Kinase, Arpp19, Controls Mitosis by Inhibiting Protein Phosphatase 2A
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- Greatwall Phosphorylates an Inhibitor of Protein Phosphatase 2A That Is Essential for Mitosis
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- Greatwall maintains mitosis through regulation of PP2A
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- Regulated activity of PP2A–B55δ is crucial for controlling entry into and exit from mitosis in Xenopus egg extracts
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- The M Phase Kinase Greatwall (Gwl) Promotes Inactivation of PP2A/B55δ, a Phosphatase Directed Against CDK Phosphosites
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- PP1-mediated dephosphorylation of phosphoproteins at mitotic exit is controlled by inhibitor-1 and PP1 phosphorylation
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- -Endosulfine is a conserved protein required for oocyte meiotic maturation in Drosophila
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