Greatwall phosphorylates an inhibitor of protein phosphatase 2A that is essential for mitosis. - Wikidata - wikimedia - TriplyDB

Greatwall phosphorylates an inhibitor of protein phosphatase 2A that is essential for mitosis.

Greatwall phosphorylates an inhibitor of protein phosphatase 2A that is essential for mitosis.

http://www.wikidata.org/entity/Q34155315

about

Checkpoint recovery in cells: how a molecular understanding can help in the fight against cancer Interlaboratory reproducibility of large-scale human protein-complex analysis by standardized AP-MS Fcp1-dependent dephosphorylation is required for M-phase-promoting factor inactivation at mitosis exit Protein kinases and phosphatases in the control of cell fate Protein phosphatases and Alzheimer's disease Endogenous inhibitor proteins that connect Ser/Thr kinases and phosphatases in cell signaling.The overlooked greatwall: a new perspective on mitotic control LB100, a small molecule inhibitor of PP2A with potent chemo- and radio-sensitizing potential PP1 and PP2A phosphatases--cooperating partners in modulating retinoblastoma protein activation The Renaissance or the cuckoo clock Modulation of cell cycle control during oocyte-to-embryo transitions Feedback loops and reciprocal regulation: recurring motifs in the systems biology of the cell cycle Loss of the Greatwall Kinase Weakens the Spindle Assembly Checkpoint MASTL(Greatwall) regulates DNA damage responses by coordinating mitotic entry after checkpoint recovery and APC/C activation PP2A-twins is antagonized by greatwall and collaborates with polo for cell cycle progression and centrosome attachment to nuclei in drosophila embryos Suppression of scant identifies Endos as a substrate of greatwall kinase and a negative regulator of protein phosphatase 2A in mitosis A first generation inhibitor of human Greatwall kinase, enabled by structural and functional characterisation of a minimal kinase domain construct Spatial regulation of Cdc55-PP2A by Zds1/Zds2 controls mitotic entry and mitotic exit in budding yeast.Budding yeast greatwall and endosulfines control activity and spatial regulation of PP2A(Cdc55) for timely mitotic progression.PhosphoTyrosyl phosphatase activator of Plasmodium falciparum: identification of its residues involved in binding to and activation of PP2A Protein Phosphatases Involved in Regulating Mitosis: Facts and Hypotheses Models in biology: lessons from modeling regulation of the eukaryotic cell cycle The Basic Biology of PP2A in Hematologic Cells and Malignancies Bod1 regulates protein phosphatase 2A at mitotic kinetochores Mastl is required for timely activation of APC/C in meiosis I and Cdk1 reactivation in meiosis II Protein phosphatase 1 is essential for Greatwall inactivation at mitotic exit Cell cycle checkpoint regulators reach a zillion.Protein Ser/Thr phosphatases--the ugly ducklings of cell signalling.LATS1/WARTS phosphorylates MYPT1 to counteract PLK1 and regulate mammalian mitotic progression Bypassing the Greatwall-Endosulfine pathway: plasticity of a pivotal cell-cycle regulatory module in Drosophila melanogaster and Caenorhabditis elegans.Cdc25A activity is required for the metaphase II arrest in mouse oocytes.Cell cycle regulation of Greatwall kinase nuclear localization facilitates mitotic progression Greatwall is essential to prevent mitotic collapse after nuclear envelope breakdown in mammals.Analysis by live imaging of effects of the adenovirus E4orf4 protein on passage through mitosis of H1299 tumor cells.Noise Reduction in Complex Biological Switches.Identification and functional analysis of variant haplotypes in the 5'-flanking region of protein phosphatase 2A-Bδ gene.Entry into mitosis: a solution to the decades-long enigma of MPF Phosphorylation of ARPP19 by protein kinase A prevents meiosis resumption in Xenopus oocytes.TORC1 coordinates the conversion of Sic1 from a target to an inhibitor of cyclin-CDK-Cks1.Protein Phosphatase 2A (PP2A) Regulates EG5 to Control Mitotic Progression

P2860

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P2860

Greatwall phosphorylates an inhibitor of protein phosphatase 2A that is essential for mitosis.

http://www.wikidata.org/entity/Q34155315

description

2010 nî lūn-bûn

@nan

2010 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի դեկտեմբերին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

name

Greatwall phosphorylates an in ...... that is essential for mitosis.

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Greatwall phosphorylates an in ...... that is essential for mitosis.

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Greatwall phosphorylates an in ...... that is essential for mitosis.

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type

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Greatwall phosphorylates an in ...... that is essential for mitosis.

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Greatwall phosphorylates an in ...... that is essential for mitosis.

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Greatwall phosphorylates an in ...... that is essential for mitosis.

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prefLabel

Greatwall phosphorylates an in ...... that is essential for mitosis.

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Greatwall phosphorylates an in ...... that is essential for mitosis.

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Greatwall phosphorylates an in ...... that is essential for mitosis.

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P356

SCIENCE.1195689

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P1476

Greatwall phosphorylates an in ...... that is essential for mitosis.

@en

P2093

Mark Skehel

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

Sarah L Maslen

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

Satoru Mochida

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

Tim Hunt

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

P2860

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

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

Genes required for mitotic spindle assembly in Drosophila S2 cells

Cdk1-dependent regulation of the mitotic inhibitor Wee1.

Localization of alpha-endosulphine in pancreatic somatostatin delta cells and expression during rat pancreas development

Phosphate-binding tag, a new tool to visualize phosphorylated proteins

alpha-Endosulfine is a conserved protein required for oocyte meiotic maturation in Drosophila

Alpha-endosulfine, a potential regulator of insulin secretion, is required for adult tissue growth control in Drosophila.

Multisite M-phase phosphorylation of Xenopus Wee1A

ARPP-16/ARPP-19: a highly conserved family of cAMP-regulated phosphoproteins.

P304

1670-1673

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scholarly article

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10.1126/SCIENCE.1195689

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6011

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330

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2010-12-01T00:00:00Z

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49688936

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21164013

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P921

phosphorylation