A quantitative model for ordered Cdk substrate dephosphorylation during mitotic exit.
about
Nur1 dephosphorylation confers positive feedback to mitotic exit phosphatase activation in budding yeastA quantitative model for cyclin-dependent kinase control of the cell cycle: revisitedMitotic exit and separation of mother and daughter cellsQuantitative framework for ordered degradation of APC/C substrates.Global Phosphoproteomic Mapping of Early Mitotic Exit in Human Cells Identifies Novel Substrate Dephosphorylation MotifsCoordination of chromatid separation and spindle elongation by antagonistic activities of mitotic and S-phase CDKs.Cdc14 Early Anaphase Release, FEAR, Is Limited to the Nucleus and Dispensable for Efficient Mitotic Exit.Identification of Cdk targets that control cytokinesisProtein Phosphatases Involved in Regulating Mitosis: Facts and HypothesesResetting a functional G1 nucleus after mitosisChanges in Ect2 localization couple actomyosin-dependent cell shape changes to mitotic progressionFunctional redundancy between Cdc14 phosphatases in zebrafish ciliogenesis.The chromosomal passenger complex (CPC) as a key orchestrator of orderly mitotic exit and cytokinesis.The tumor suppressor CDKN3 controls mitosis.Dual Regulation of the mitotic exit network (MEN) by PP2A-Cdc55 phosphatase.Robustness of cell cycle control and flexible orders of signaling eventsMinimal models for cell-cycle control based on competitive inhibition and multisite phosphorylations of Cdk substrates.Deciphering the New Role of the Greatwall/PP2A Pathway in Cell Cycle Control.A Wee1 checkpoint inhibits anaphase onset.PP2ACdc55 Phosphatase Imposes Ordered Cell-Cycle Phosphorylation by Opposing Threonine Phosphorylation.Sic1 as a timer of Clb cyclin waves in the yeast cell cycle--design principle of not just an inhibitor.Repo-Man-PP1: a link between chromatin remodelling and nuclear envelope reassembly.Chromosome segregation in budding yeast: sister chromatid cohesion and related mechanisms.Dataset from the global phosphoproteomic mapping of early mitotic exit in human cellsThe Cdk/cDc14 module controls activation of the Yen1 holliday junction resolvase to promote genome stability.PP1 initiates the dephosphorylation of MASTL, triggering mitotic exit and bistability in human cells.Cdk1 orders mitotic events through coordination of a chromosome-associated phosphatase switch.Mechanisms regulating phosphatase specificity and the removal of individual phosphorylation sites during mitotic exit.Comprehensive proteomics analysis reveals new substrates and regulators of the fission yeast clp1/cdc14 phosphatase.A PP2A-B55 recognition signal controls substrate dephosphorylation kinetics during mitotic exit.Mitotic exit: Determining the PP2A dephosphorylation programPositive Feedback Keeps Duration of Mitosis Temporally Insulated from Upstream Cell-Cycle Events.Temporal and compartment-specific signals coordinate mitotic exit with spindle position.Multisite phosphorylation networks as signal processors for Cdk1.The BEG (PP2A-B55/ENSA/Greatwall) pathway ensures cytokinesis follows chromosome separationBiphasic responses in multi-site phosphorylation systems.Re-examining the role of Cdc14 phosphatase in reversal of Cdk phosphorylation during mitotic exit.Sequential phosphorylation of CST subunits by different cyclin-Cdk1 complexes orchestrate telomere replication.Phosphoproteome dynamics during mitotic exit in budding yeast.Cdk1 phosphorylation of Esp1/Separase functions with PP2A and Slk19 to regulate pericentric Cohesin and anaphase onset.
P2860
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P2860
A quantitative model for ordered Cdk substrate dephosphorylation during mitotic exit.
description
2011 nî lūn-bûn
@nan
2011 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
A quantitative model for ordered Cdk substrate dephosphorylation during mitotic exit.
@ast
A quantitative model for ordered Cdk substrate dephosphorylation during mitotic exit.
@en
A quantitative model for ordered Cdk substrate dephosphorylation during mitotic exit.
@nl
type
label
A quantitative model for ordered Cdk substrate dephosphorylation during mitotic exit.
@ast
A quantitative model for ordered Cdk substrate dephosphorylation during mitotic exit.
@en
A quantitative model for ordered Cdk substrate dephosphorylation during mitotic exit.
@nl
prefLabel
A quantitative model for ordered Cdk substrate dephosphorylation during mitotic exit.
@ast
A quantitative model for ordered Cdk substrate dephosphorylation during mitotic exit.
@en
A quantitative model for ordered Cdk substrate dephosphorylation during mitotic exit.
@nl
P3181
P1433
P1476
A quantitative model for ordered Cdk substrate dephosphorylation during mitotic exit.
@en
P2093
Céline Bouchoux
P304
P3181
P356
10.1016/J.CELL.2011.09.047
P407
P577
2011-11-11T00:00:00Z