Structure of protein phosphatase 2A core enzyme bound to tumor-inducing toxins
about
A PP2A phosphatase high density interaction network identifies a novel striatin-interacting phosphatase and kinase complex linked to the cerebral cavernous malformation 3 (CCM3) proteinVAC14 nucleates a protein complex essential for the acute interconversion of PI3P and PI(3,5)P(2) in yeast and mouse.Protein phosphatase 6 regulates mitotic spindle formation by controlling the T-loop phosphorylation state of Aurora A bound to its activator TPX2Over expression of PPP2R2C inhibits human glioma cells growth through the suppression of mTOR pathwayExome sequencing identifies recurrent somatic RAC1 mutations in melanomaPP2A: 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 Basis of PP2A Inhibition by Small t AntigenStructure of a Protein Phosphatase 2A Holoenzyme: Insights into B55-Mediated Tau DephosphorylationCrystal Structures of Protein Phosphatase-1 Bound to Nodularin-R and Tautomycin: A Novel Scaffold for Structure-based Drug Design of Serine/Threonine Phosphatase InhibitorsThe structural basis for tight control of PP2A methylation and function by LCMT-1.Structural basis of protein phosphatase 2A stable latencyStructure of the Ca2+-dependent PP2A heterotrimer and insights into Cdc6 dephosphorylationStructural basis of PP2A activation by PTPA, an ATP-dependent activation chaperone.Structural and biochemical characterization of human PR70 in isolation and in complex with the scaffolding subunit of protein phosphatase 2ACrystal Structure of Okadaic Acid Binding Protein 2.1: A Sponge Protein Implicated in Cytotoxin AccumulationTranscriptional regulation of PP2A-A alpha is mediated by multiple factors including AP-2alpha, CREB, ETS-1, and SP-1Mapping of protein phosphatase-6 association with its SAPS domain regulatory subunit using a model of helical repeats.PP2A regulates the pro-apoptotic activity of FOXO1.Ligand binding to the androgen receptor induces conformational changes that regulate phosphatase interactionsHigh yield expression of serine/threonine protein phosphatase type 5, and a fluorescent assay suitable for use in the detection of catalytic inhibitors.Specificity of RCN1-mediated protein phosphatase 2A regulation in meristem organization and stress response in roots.Targeted disruption of the PME-1 gene causes loss of demethylated PP2A and perinatal lethality in mice.Specialized functions of the PP2A subfamily II catalytic subunits PP2A-C3 and PP2A-C4 in the distribution of auxin fluxes and development in Arabidopsis.The algal hepatoxoxin okadaic acid is a substrate for human cytochromes CYP3A4 and CYP3A5.Molecular mechanisms of microcystin toxicity in animal cells.Cyanobacterial cyclopeptides as lead compounds to novel targeted cancer drugsPP2A:B56{epsilon}, a substrate of caspase-3, regulates p53-dependent and p53-independent apoptosis during development.Molecular Cloning of the Genes Encoding the PR55/Bβ/δ Regulatory Subunits for PP-2A and Analysis of Their Functions in Regulating Development of Goldfish, Carassius auratus.Phenylarsine oxide binding reveals redox-active and potential regulatory vicinal thiols on the catalytic subunit of protein phosphatase 2A.Microcystin-LR (MCLR) induces a compensation of PP2A activity mediated by α4 protein in HEK293 cells.Viewing serine/threonine protein phosphatases through the eyes of drug designersHuman cancer-associated mutations in the Aα subunit of protein phosphatase 2A increase lung cancer incidence in Aα knock-in and knockout mice.KIBRA protein phosphorylation is regulated by mitotic kinase aurora and protein phosphatase 1.Effect of microcystin-LR on protein phosphatase 2A and its function in human amniotic epithelial cells.Mouse model for probing tumor suppressor activity of protein phosphatase 2A in diverse signaling pathways.Insights into the key interactions between human protein phosphatase 5 and cantharidin using molecular dynamics and site-directed mutagenesis bioassays.Structural basis for protein phosphatase 1 regulation and specificityRegulation of autophagy by coordinated action of mTORC1 and protein phosphatase 2A.Serine 15 phosphorylation of p53 directs its interaction with B56gamma and the tumor suppressor activity of B56gamma-specific protein phosphatase 2A
P2860
Q24311685-575226B4-B346-4F0C-BE4D-5A43D061C4ADQ24318746-883ED1D3-D9D9-40F8-9191-495735A68BC6Q24321572-556B925D-E8B3-498F-8743-2F116D141366Q24338396-10B71684-3283-457C-B9F7-B89BFF90BA66Q24607661-ED66C58A-1494-4496-A8A7-12E3491F78E3Q26823704-73CB2BFA-7FA6-401B-8E5F-370BECBAF242Q27327234-DF11D8C7-C151-4D70-83C1-2D57289B7842Q27646534-A20BD430-FAC1-4ABC-8F6B-1AF17A605579Q27652517-A3B7D4C0-0866-4072-8E60-7A2CDB0659DDQ27652817-8DE9A795-D18A-4D9B-BA59-38F59D9B9E1DQ27666843-787C9AAC-334B-40BC-995C-50122584D700Q27677410-40DB0C48-5E2E-4CCE-AC91-9E71C6732466Q27678559-D0A96985-7964-449B-AB8D-0E8130D704EEQ27680173-FE55C507-685D-4A53-B0E0-FEBBE999E73EQ27684630-B44D11FF-4C3A-477F-AF4B-8E645825E01CQ27700834-019BFB35-D72F-43FE-B376-107992BEDF5FQ28593741-ABC81ADF-3053-4499-8CC8-ABA81577EE82Q30438153-E4E3E46F-2FA6-48DA-BD3D-A468A98072F4Q30440004-022BDE7C-D626-4621-AE35-DF7D0887D654Q30443046-0A673FF0-2B46-464C-AC20-9201B818386BQ33302853-BC748FB4-53D5-4136-BDC2-7BFE12E45485Q33345022-5B8820BF-6AB1-445D-B2B9-DB9F572C6DF2Q33348585-73B4E99F-B9EB-48C6-89AF-F689E2515AF9Q33354740-022F800E-5BCB-42B6-97F8-E93A0AA7E87DQ33620648-B7956708-1BFB-4674-B35C-9B032D0131A6Q33649241-191B059A-E808-47BB-960E-702F7C22F0D4Q33801128-9C488B74-5B6C-4C5A-AE3C-E3867C83C4C4Q34251140-E4E64AA3-3B0A-492E-B76D-9677E1C0A70AQ34485379-C169640C-E5E9-4B16-AEA7-F6F294845BA8Q34600549-D4E67D54-6A9B-4CD5-9553-5FBAC2402440Q35059243-0123D75B-F2E4-48C6-AEAF-6CA72A1474D7Q35146774-93157987-748D-4905-8699-3D54A7B49F93Q35192607-3A0AB42D-1FDF-45A7-A41C-468DAC9CC2F7Q35378440-2898267F-1371-439E-B908-82EE484E75E8Q35597474-31625C4E-1737-4B01-BD82-9BACEB4DF78DQ35859963-6176FA69-8027-4458-8D6D-6F4FE0F2A29EQ35865497-4DCBA9A5-9C15-40C7-B028-748B200BF5B9Q35954007-BD387A24-5059-4E86-8C9A-BB07A58C3858Q36003000-08A3C71C-D464-4A31-9E14-AFFE795BE266Q36421078-E7BA1C57-7B7B-4DDF-80E7-28BF9D023117
P2860
Structure of protein phosphatase 2A core enzyme bound to tumor-inducing toxins
description
2006 nî lūn-bûn
@nan
2006 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
Structure of protein phosphatase 2A core enzyme bound to tumor-inducing toxins
@ast
Structure of protein phosphatase 2A core enzyme bound to tumor-inducing toxins
@en
Structure of protein phosphatase 2A core enzyme bound to tumor-inducing toxins
@en-gb
Structure of protein phosphatase 2A core enzyme bound to tumor-inducing toxins
@nl
type
label
Structure of protein phosphatase 2A core enzyme bound to tumor-inducing toxins
@ast
Structure of protein phosphatase 2A core enzyme bound to tumor-inducing toxins
@en
Structure of protein phosphatase 2A core enzyme bound to tumor-inducing toxins
@en-gb
Structure of protein phosphatase 2A core enzyme bound to tumor-inducing toxins
@nl
prefLabel
Structure of protein phosphatase 2A core enzyme bound to tumor-inducing toxins
@ast
Structure of protein phosphatase 2A core enzyme bound to tumor-inducing toxins
@en
Structure of protein phosphatase 2A core enzyme bound to tumor-inducing toxins
@en-gb
Structure of protein phosphatase 2A core enzyme bound to tumor-inducing toxins
@nl
P2093
P921
P3181
P1433
P1476
Structure of protein phosphatase 2A core enzyme bound to tumor-inducing toxins
@en
P2093
Jeffry B Stock
Philip D Jeffrey
Stefan Strack
Yongna Xing
P304
P3181
P356
10.1016/J.CELL.2006.09.025
P407
P50
P577
2006-10-20T00:00:00Z