Structure of a Protein Phosphatase 2A Holoenzyme: Insights into B55-Mediated Tau Dephosphorylation
about
Protein phosphatase 2A dysfunction in Alzheimer's diseasePhosphatases of α-synuclein, LRRK2, and tau: important players in the phosphorylation-dependent pathology of ParkinsonismLive-cell imaging RNAi screen identifies PP2A-B55alpha and importin-beta1 as key mitotic exit regulators in human cellsA PP4 phosphatase complex dephosphorylates RPA2 to facilitate DNA repair via homologous recombinationParkinson-related parkin reduces α-Synuclein phosphorylation in a gene transfer modelTherapeutic benefits of a component of coffee in a rat model of Alzheimer's disease.B55alpha PP2A holoenzymes modulate the phosphorylation status of the retinoblastoma-related protein p107 and its activationProtein phosphatases and Alzheimer's diseaseStructure and function of the PP2A-shugoshin interactionPP2A: more than a reset switch to activate pRB proteins during the cell cycle and in response to signaling cues.The biogenesis of active protein phosphatase 2A holoenzymes: a tightly regulated process creating phosphatase specificityThe Beta-amyloid protein of Alzheimer's disease: communication breakdown by modifying the neuronal cytoskeletonPP1 and PP2A phosphatases--cooperating partners in modulating retinoblastoma protein activationMechanisms of the scaffold subunit in facilitating protein phosphatase 2A methylationThe Active Site of Oligogalacturonate Lyase Provides Unique Insights into Cytoplasmic Oligogalacturonate -EliminationStructure of the Ca2+-dependent PP2A heterotrimer and insights into Cdc6 dephosphorylationStructural and biochemical characterization of human PR70 in isolation and in complex with the scaffolding subunit of protein phosphatase 2ASeparase biosensor reveals that cohesin cleavage timing depends on phosphatase PP2A(Cdc55) regulationIdentification of a mutation causing a defective spindle assembly checkpoint in high ethyl caproate-producing sake yeast strain K1801.Mechanisms of cancer cell killing by the adenovirus E4orf4 proteinPP2A: The Wolf in Sheep's Clothing?NMR studies of the C-terminus of alpha4 reveal possible mechanism of its interaction with MID1 and protein phosphatase 2AVisualization of subunit interactions and ternary complexes of protein phosphatase 2A in mammalian cellsStructure- and modeling-based identification of the adenovirus E4orf4 binding site in the protein phosphatase 2A B55α subunitThe B55α-containing PP2A holoenzyme dephosphorylates FOXO1 in islet β-cells under oxidative stressThe protein phosphatase 2A regulatory subunits B'beta and B'delta mediate sustained TrkA neurotrophin receptor autophosphorylation and neuronal differentiationStriatins 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.Interactome analysis of the influenza A virus transcription/replication machinery identifies protein phosphatase 6 as a cellular factor required for efficient virus replication.Mapping of protein phosphatase-6 association with its SAPS domain regulatory subunit using a model of helical repeats.Mice lacking phosphatase PP2A subunit PR61/B'delta (Ppp2r5d) develop spatially restricted tauopathy by deregulation of CDK5 and GSK3beta.PR65, the HEAT-repeat scaffold of phosphatase PP2A, is an elastic connector that links force and catalysisMonoubiquitination promotes calpain cleavage of the protein phosphatase 2A (PP2A) regulatory subunit α4, altering PP2A stability and microtubule-associated protein phosphorylation.Bioengineered protein phosphatase 2A: update on needProtein Phosphatase 2A (PP2A) Regulates EG5 to Control Mitotic ProgressionIdentification of O-GlcNAc sites within peptides of the Tau protein and their impact on phosphorylation.Molecular implication of PP2A and Pin1 in the Alzheimer's disease specific hyperphosphorylation of Tau.Altered protein phosphatase 2A methylation and Tau phosphorylation in the young and aged brain of methylenetetrahydrofolate reductase (MTHFR) deficient mice.The role of tau kinases in Alzheimer's disease.Loss of Hsp110 leads to age-dependent tau hyperphosphorylation and early accumulation of insoluble amyloid beta.Molecular determinants for PP2A substrate specificity: charged residues mediate dephosphorylation of tyrosine hydroxylase by the PP2A/B' regulatory subunit
P2860
Q21090465-C6AE9ED6-A9E9-4D5C-8B38-9D6693830C86Q21131229-013CEC9E-2F3B-4400-B0CE-F24BBE52D3E4Q24295682-DADA5E01-487E-409B-B35A-705721635BD0Q24299264-09D8E4B8-C83D-48BF-B839-7BAB605671DCQ24305472-0894848F-8EAC-4A81-88A1-4E3F84EF7C37Q24563378-52691AB1-7E7E-44FF-9871-B6A6F582A512Q24604107-C064A01A-3B11-4A91-B7C4-2F0FE7F68519Q24632495-FF727A85-E6BD-4375-93DD-55F24FFC89A4Q24648497-F920DC57-C93C-4F3C-AEF3-1AAED5044F95Q26823704-5BB9E78E-276B-4EBC-B5DC-7154D55C1DBAQ26824764-E549DA00-903A-4D8F-B1D5-6530A15A3AB6Q26864818-8C9CD109-1654-479A-BAC5-F0532EF3024BQ26991427-D7346E79-7039-4EEE-AD79-F7F5E8CB570CQ27327234-1B1BDFA7-7851-48F4-8DFC-AA8E81284826Q27664585-4F3D08C8-F500-4A41-A81D-5CA7EF570ABAQ27678559-B35B83A2-A114-426E-BCAA-96A4D761773EQ27684630-CB41B6E3-9A9B-44DF-BC7C-BF612960CF25Q27930965-5E87118B-F7BF-4D00-ACF2-ABAD2BD97AD8Q27935018-6DFBF7AC-92B3-4A86-908A-39CB6639192AQ28081729-6D6F9CE5-8182-41CA-8783-CBC8CABCFD48Q28088747-A188C3BF-CC77-43CA-AE02-981A8D0CA91EQ28478425-584353CA-A006-4D7A-B855-2F196CC9F6DFQ28542846-3A7EE266-DCA8-45F4-ADAB-B885412F8B27Q28567810-14DE5608-D318-4926-9CDE-0A2907D7DEDCQ28569593-907DF4AF-CD3E-4D99-ABEA-7B24CA74D554Q28573860-FC3478DE-09A6-44A4-A715-6DAF645BA32EQ30359226-B0467ED9-5CCB-4BD8-8DAB-F5941F7AA1E5Q30366402-9FC69926-19D6-4983-851E-D225DFF65BD3Q30438153-44AF1B38-F459-4BC5-9221-E6B4055D5FEAQ30473576-85B7459E-F9D9-4DFA-9699-EA52A14CAB9AQ30493200-B94F830A-85D8-4BE9-BBF4-BAF8D10CD33CQ30520621-F29C8CFC-E595-43B9-A6A6-34C57AAC4D44Q30574568-E499E2B2-6AEC-4127-81E3-C48A9109688CQ33686351-09999AA8-6567-45B1-9A64-14D92EE80FEDQ33822354-7AE6A39E-0CBA-4D79-8A69-0F71669CDF4AQ33952539-04571B0A-0089-4353-B89A-5B20F2C65F8DQ34077890-9B2254FC-8ABF-4C8C-92C7-6E423559FE64Q34138413-CE56774E-152D-4A31-A0B4-7AC38C016ECFQ34177990-248C817D-B909-4B2B-B768-F8BE2347B671Q34449427-96118411-40CC-42E8-8243-29087E2DDF71
P2860
Structure of a Protein Phosphatase 2A Holoenzyme: Insights into B55-Mediated Tau Dephosphorylation
description
2008 nî lūn-bûn
@nan
2008 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի սեպտեմբերին 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
Structure of a Protein Phospha ...... Mediated Tau Dephosphorylation
@ast
Structure of a Protein Phospha ...... Mediated Tau Dephosphorylation
@en
Structure of a Protein Phospha ...... Mediated Tau Dephosphorylation
@nl
type
label
Structure of a Protein Phospha ...... Mediated Tau Dephosphorylation
@ast
Structure of a Protein Phospha ...... Mediated Tau Dephosphorylation
@en
Structure of a Protein Phospha ...... Mediated Tau Dephosphorylation
@nl
prefLabel
Structure of a Protein Phospha ...... Mediated Tau Dephosphorylation
@ast
Structure of a Protein Phospha ...... Mediated Tau Dephosphorylation
@en
Structure of a Protein Phospha ...... Mediated Tau Dephosphorylation
@nl
P2093
P2860
P3181
P1433
P1476
Structure of a Protein Phospha ...... Mediated Tau Dephosphorylation
@en
P2093
Philip D Jeffrey
Ping Zhang
P2860
P304
P3181
P356
10.1016/J.MOLCEL.2008.08.006
P50
P577
2008-09-26T00:00:00Z