PP2A/B55 and Fcp1 regulate Greatwall and Ensa dephosphorylation during mitotic exit. - Wikidata - awgldk - TriplyDB

PP2A/B55 and Fcp1 regulate Greatwall and Ensa dephosphorylation during mitotic exit.

PP2A/B55 and Fcp1 regulate Greatwall and Ensa dephosphorylation during mitotic exit.

http://www.wikidata.org/entity/Q35082227

about

A first generation inhibitor of human Greatwall kinase, enabled by structural and functional characterisation of a minimal kinase domain construct Protein phosphatase 1 is essential for Greatwall inactivation at mitotic exit Analysis by live imaging of effects of the adenovirus E4orf4 protein on passage through mitosis of H1299 tumor cells.α-endosulfine (ENSA) regulates exit from prophase I arrest in mouse oocytes Spatial regulation of greatwall by Cdk1 and PP2A-Tws in the cell cycle Role for regulated phosphatase activity in generating mitotic oscillations in Xenopus cell-free extracts.Greatwall-phosphorylated Endosulfine is both an inhibitor and a substrate of PP2A-B55 heterotrimers.Fcp1 phosphatase controls Greatwall kinase to promote PP2A-B55 activation and mitotic progression Cell Cycle Control: A System of Interlinking Oscillators.PP2A as a master regulator of the cell cycle.PP1 initiates the dephosphorylation of MASTL, triggering mitotic exit and bistability in human cells.Bistability of mitotic entry and exit switches during open mitosis in mammalian cells.Mechanisms regulating phosphatase specificity and the removal of individual phosphorylation sites during mitotic exit.Regulation of Cell Division.Two Bistable Switches Govern M Phase Entry.Carboxy-terminal domain phosphatase 1 silencing results in the inhibition of tumor formation ability in gastric cancer cells.PP1 inactivates Greatwall to release PP2A-B55 from mitotic confinement.Cell cycle-dependent regulation of Greatwall kinase by protein phosphatase 1 and regulatory subunit 3B.Protein interactomes of protein phosphatase 2A B55 regulatory subunits reveal B55-mediated regulation of replication protein A under replication stress.Model scenarios for switch-like mitotic transitions.Coordination of Protein Kinase and Phosphoprotein Phosphatase Activities in Mitosis.Preparing a cell for nuclear envelope breakdown: Spatio-temporal control of phosphorylation during mitotic entry.MASTL induces Colon Cancer progression and Chemoresistance by promoting Wnt/β-catenin signaling

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P2860

PP2A/B55 and Fcp1 regulate Greatwall and Ensa dephosphorylation during mitotic exit.

http://www.wikidata.org/entity/Q35082227

description

2014 nî lūn-bûn

@nan

2014 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2014 թվականի հունվարին հրատարակված գիտական հոդված

@hy

2014年の論文

@ja

2014年論文

@yue

2014年論文

@zh-hant

2014年論文

@zh-hk

2014年論文

@zh-mo

2014年論文

@zh-tw

2014年论文

@wuu

name

PP2A/B55 and Fcp1 regulate Greatwall and Ensa dephosphorylation during mitotic exit.

@ast

PP2A/B55 and Fcp1 regulate Greatwall and Ensa dephosphorylation during mitotic exit.

@en

type

label

PP2A/B55 and Fcp1 regulate Greatwall and Ensa dephosphorylation during mitotic exit.

@ast

PP2A/B55 and Fcp1 regulate Greatwall and Ensa dephosphorylation during mitotic exit.

@en

prefLabel

PP2A/B55 and Fcp1 regulate Greatwall and Ensa dephosphorylation during mitotic exit.

@ast

PP2A/B55 and Fcp1 regulate Greatwall and Ensa dephosphorylation during mitotic exit.

@en

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JOURNAL.PGEN.1004004

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P1476

PP2A/B55 and Fcp1 regulate Greatwall and Ensa dephosphorylation during mitotic exit.

@en

P2093

Clare Vesely

http://www.w3.org/2001/XMLSchema#string

Julian Gannon

http://www.w3.org/2001/XMLSchema#string

Nadia Hégarat

http://www.w3.org/2001/XMLSchema#string

Nisha Peter

http://www.w3.org/2001/XMLSchema#string

P2860

Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis

Live-cell imaging RNAi screen identifies PP2A-B55alpha and importin-beta1 as key mitotic exit regulators in human cells

MASTL is the human orthologue of Greatwall kinase that facilitates mitotic entry, anaphase and cytokinesis

The decision to enter mitosis: feedback and redundancy in the mitotic entry network

The substrate of Greatwall kinase, Arpp19, controls mitosis by inhibiting protein phosphatase 2A

Loss of human Greatwall results in G2 arrest and multiple mitotic defects due to deregulation of the cyclin B-Cdc2/PP2A balance

Fcp1-dependent dephosphorylation is required for M-phase-promoting factor inactivation at mitosis exit

Two distinct mechanisms for negative regulation of the Wee1 protein kinase

A quantitative atlas of mitotic phosphorylation

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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e1004004

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scholarly article

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10.1371/JOURNAL.PGEN.1004004

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1

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10

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Antony W. Oliver

Helfrid Hochegger

P577

2014-01-02T00:00:00Z

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259589040

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24391510

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3879168

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