PP2A-mediated dephosphorylation of p107 plays a critical role in chondrocyte cell cycle arrest by FGF
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B55alpha PP2A holoenzymes modulate the phosphorylation status of the retinoblastoma-related protein p107 and its activationFibroblast growth factor signaling in skeletal development and diseasePP2A: more than a reset switch to activate pRB proteins during the cell cycle and in response to signaling cues.PP1 and PP2A phosphatases--cooperating partners in modulating retinoblastoma protein activationFibroblast growth factor receptor 1 signaling in adult cardiomyocytes increases contractility and results in a hypertrophic cardiomyopathySixteen years and counting: the current understanding of fibroblast growth factor receptor 3 (FGFR3) signaling in skeletal dysplasiasProtein phosphatase 2A promotes the transition to G0 during terminal differentiation in DrosophilaA Network Map of FGF-1/FGFR Signaling System.The role of muscle cells in regulating cartilage matrix production.p107 in the public eye: an Rb understudy and more.Protein phosphatase 2A acts as a mitogen-activated protein kinase kinase kinase 3 (MEKK3) phosphatase to inhibit lysophosphatidic acid-induced IkappaB kinase beta/nuclear factor-kappaB activation.Cyclin D1 overexpression perturbs DNA replication and induces replication-associated DNA double-strand breaks in acquired radioresistant cellsFGF signaling in the osteoprogenitor lineage non-autonomously regulates postnatal chondrocyte proliferation and skeletal growth.Cell type-specific control of protein synthesis and proliferation by FGF-dependent signaling to the translation repressor 4E-BP.Activation of p107 by fibroblast growth factor, which is essential for chondrocyte cell cycle exit, is mediated by the protein phosphatase 2A/B55α holoenzyme.Cell-cycle control as a target for calcium, hormonal and developmental signals: the role of phosphorylation in the retinoblastoma-centred pathway.Phosphoproteomics of Fibroblast Growth Factor 1 (FGF1) Signaling in Chondrocytes: Identifying the Signature of Inhibitory Response.Achondroplasia: Development, pathogenesis, and therapy.The B55α regulatory subunit of protein phosphatase 2A mediates fibroblast growth factor-induced p107 dephosphorylation and growth arrest in chondrocytes.Overexpression of cyclin E/CDK2 complexes overcomes FGF-induced cell cycle arrest in the presence of hypophosphorylated Rb proteinsReactivating PP2A by FTY720 as a novel therapy for AML with C-KIT tyrosine kinase domain mutation.FGF inhibits the activity of the cyclin B1/CDK1 kinase to induce a transient G₂arrest in RCS chondrocytes.PP2A interaction with Rb2/p130 mediates translocation of Rb2/p130 into the nucleus in all-trans retinoic acid-treated ovarian carcinoma cells.A new mode of cell cycle stimulation: cyclin E and CDK2-mediated cytoplasmic retention of repressive E2F complexesPP2A as the Main Node of Therapeutic Strategies and Resistance Reversal in Triple-Negative Breast Cancer.Clinicopathological effects of protein phosphatase 2, regulatory subunit A, alpha mutations in gastrointestinal stromal tumors.
P2860
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P2860
PP2A-mediated dephosphorylation of p107 plays a critical role in chondrocyte cell cycle arrest by FGF
description
2008 nî lūn-bûn
@nan
2008 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
PP2A-mediated dephosphorylatio ...... ocyte cell cycle arrest by FGF
@ast
PP2A-mediated dephosphorylatio ...... ocyte cell cycle arrest by FGF
@en
type
label
PP2A-mediated dephosphorylatio ...... ocyte cell cycle arrest by FGF
@ast
PP2A-mediated dephosphorylatio ...... ocyte cell cycle arrest by FGF
@en
prefLabel
PP2A-mediated dephosphorylatio ...... ocyte cell cycle arrest by FGF
@ast
PP2A-mediated dephosphorylatio ...... ocyte cell cycle arrest by FGF
@en
P2093
P2860
P1433
P1476
PP2A-mediated dephosphorylatio ...... ocyte cell cycle arrest by FGF
@en
P2093
Claudio Basilico
Emmanuel Laplantine
Victoria Kolupaeva
P2860
P356
10.1371/JOURNAL.PONE.0003447
P407
P577
2008-10-17T00:00:00Z