Structure of the Ca2+-dependent PP2A heterotrimer and insights into Cdc6 dephosphorylation
about
PP2A: more than a reset switch to activate pRB proteins during the cell cycle and in response to signaling cues.Mechanisms of the scaffold subunit in facilitating protein phosphatase 2A methylationStructural and biochemical characterization of human PR70 in isolation and in complex with the scaffolding subunit of protein phosphatase 2AStriatins contain a noncanonical coiled coil that binds protein phosphatase 2A A subunit to form a 2:2 heterotetrameric core of striatin-interacting phosphatase and kinase (STRIPAK) complex.B56δ-related protein phosphatase 2A dysfunction identified in patients with intellectual disability.Crystal structures and mutagenesis of PPP-family ser/thr protein phosphatases elucidate the selectivity of cantharidin and novel norcantharidin-based inhibitors of PP5C.PR65A phosphorylation regulates PP2A complex signaling.Protein phosphatases PP2A, PP4 and PP6: mediators and regulators in development and responses to environmental cues.All roads lead to PP2A: exploiting the therapeutic potential of this phosphatase.PP2A as a master regulator of the cell cycle.PP2A binds to the LIM domains of lipoma-preferred partner through its PR130/B″ subunit to regulate cell adhesion and migration.TRPV3 Channel Negatively Regulates Cell Cycle Progression and Safeguards the Pluripotency of Embryonic Stem Cells.Protein Phosphatase 2A: a Double-Faced Phosphatase of Cellular System and Its Role in Neurodegenerative Disorders.Phosphorylation Regulates Id2 Degradation and Mediates the Proliferation of Neural Precursor CellsPP2A-B' holoenzyme substrate recognition, regulation and role in cytokinesis.Interactions of AsCy3 with cysteine-rich peptidesThe B″ regulatory subunit of protein phosphatase 2A mediates the dephosphorylation of rice retinoblastoma-related protein-1.Methylation-regulated decommissioning of multimeric PP2A complexes.Therapeutic Targeting of PP2A.Bidirectional regulation of fragile X mental retardation protein phosphorylation controls rhodopsin homoeostasis.Positive selection analysis highlights key positions in plant PP2A regulatory subunits.
P2860
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P2860
Structure of the Ca2+-dependent PP2A heterotrimer and insights into Cdc6 dephosphorylation
description
2013 nî lūn-bûn
@nan
2013 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2013 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
name
Structure of the Ca2+-dependen ...... ts into Cdc6 dephosphorylation
@ast
Structure of the Ca2+-dependen ...... ts into Cdc6 dephosphorylation
@en
Structure of the Ca2+-dependen ...... ts into Cdc6 dephosphorylation
@nl
type
label
Structure of the Ca2+-dependen ...... ts into Cdc6 dephosphorylation
@ast
Structure of the Ca2+-dependen ...... ts into Cdc6 dephosphorylation
@en
Structure of the Ca2+-dependen ...... ts into Cdc6 dephosphorylation
@nl
prefLabel
Structure of the Ca2+-dependen ...... ts into Cdc6 dephosphorylation
@ast
Structure of the Ca2+-dependen ...... ts into Cdc6 dephosphorylation
@en
Structure of the Ca2+-dependen ...... ts into Cdc6 dephosphorylation
@nl
P2093
P2860
P356
P1433
P1476
Structure of the Ca2+-dependen ...... ts into Cdc6 dephosphorylation
@en
P2093
Kenneth A Satyshur
Marc C Mumby
Nathan Wlodarchak
Philip D Jeffrey
Tingwan Sun
Vitali Stanevich
Yongna Xing
P2860
P2888
P304
P356
10.1038/CR.2013.77
P577
2013-06-11T00:00:00Z
P5875
P6179
1042687475