A specific protein carboxyl methylesterase that demethylates phosphoprotein phosphatase 2A in bovine brain
about
Protein phosphatase 2A dysfunction in Alzheimer's diseaseThe metabolic advantage of tumor cellsA protein phosphatase methylesterase (PME-1) is one of several novel proteins stably associating with two inactive mutants of protein phosphatase 2ALeucine carboxyl methyltransferase-1 is necessary for normal progression through mitosis in mammalian cellsCarboxymethylation of nuclear protein serine/threonine phosphatase XProtein phosphatase 2A: a highly regulated family of serine/threonine phosphatases implicated in cell growth and signallingCarboxyl methylation regulates phosphoprotein phosphatase 2A by controlling the association of regulatory B subunitsCarboxyl methylation of the phosphoprotein phosphatase 2A catalytic subunit promotes its functional association with regulatory subunits in vivoPhosphoprotein phosphatase 2A: a novel druggable target for Alzheimer's diseasePP2A: more than a reset switch to activate pRB proteins during the cell cycle and in response to signaling cues.The pharmacological landscape and therapeutic potential of serine hydrolasesCircumventing embryonic lethality with Lcmt1 deficiency: generation of hypomorphic Lcmt1 mice with reduced protein phosphatase 2A methyltransferase expression and defects in insulin signalingMechanisms of the scaffold subunit in facilitating protein phosphatase 2A methylationChanges in Carboxy Methylation and Tyrosine Phosphorylation of Protein Phosphatase PP2A Are Associated with Epididymal Sperm Maturation and MotilityStructural basis of protein phosphatase 2A stable latencyMethionine inhibits autophagy and promotes growth by inducing the SAM-responsive methylation of PP2ACarboxymethylation of the PP2A catalytic subunit in Saccharomyces cerevisiae is required for efficient interaction with the B-type subunits Cdc55p and Rts1pATM-dependent dissociation of B55 regulatory subunit from nuclear PP2A in response to ionizing radiation.Protein Ser/Thr phosphatases--the ugly ducklings of cell signalling.Targeted disruption of the PME-1 gene causes loss of demethylated PP2A and perinatal lethality in mice.Effects of serine/threonine protein phosphatases on ion channels in excitable membranes.Cytoplasmic SET induces tau hyperphosphorylation through a decrease of methylated phosphatase 2A.Altered protein phosphatase 2A methylation and Tau phosphorylation in the young and aged brain of methylenetetrahydrofolate reductase (MTHFR) deficient mice.A new role for protein methylation: switching partners at the phosphatase ball.Reactivation of the tumour suppressor RASSF1A in breast cancer by simultaneous targeting of DNA and E2F1 methylation.Methylation of the protein phosphatase 2A catalytic subunit is essential for association of Balpha regulatory subunit but not SG2NA, striatin, or polyomavirus middle tumor antigenDeterminants for Substrate Specificity of Protein Phosphatase 2A.Discovery and optimization of sulfonyl acrylonitriles as selective, covalent inhibitors of protein phosphatase methylesterase-1.Circumventing cellular control of PP2A by methylation promotes transformation in an Akt-dependent mannerFusarochromanone-induced reactive oxygen species results in activation of JNK cascade and cell death by inhibiting protein phosphatases 2A and 5.An extract of Urtica dioica L. mitigates obesity induced insulin resistance in mice skeletal muscle via protein phosphatase 2A (PP2A).PP2A methylation controls sensitivity and resistance to β-amyloid-induced cognitive and electrophysiological impairments.p21-Activated kinase-1 and its role in integrated regulation of cardiac contractility.PP2A ligand ITH12246 protects against memory impairment and focal cerebral ischemia in mice.Enhanced phosphatase activity attenuates α-synucleinopathy in a mouse modelDysregulation of protein phosphatase 2A in parkinson disease and dementia with lewy bodies.Assembly and structure of protein phosphatase 2A.Protein carboxyl methylation and the biochemistry of memory.Phosphoinositide 3-kinase γ inhibits cardiac GSK-3 independently of Akt.Microtubule-associated protein tau as a therapeutic target in Alzheimer's disease.
P2860
Q21090465-DF1DB495-0AD1-44B5-A512-34C968A41BB9Q21245765-7B127B67-E53B-47FC-BC12-645905DF398FQ22009542-59819453-487C-4119-8D75-7B218ABC299FQ24338461-C04DF479-33D7-4FDB-AF7D-30F0BA882BBDQ24530551-EA51C22E-910B-4903-9A9B-F2AB962C6305Q24532278-30534A84-02E3-4978-B305-1DEAFCF674BBQ24598280-0ECF0366-E1ED-49FF-A167-94530B57DC79Q24598333-905F5317-BA55-4687-8DA2-321CED2E13DAQ24627125-23B8523D-79BD-497D-84B7-B2BDB9991E1BQ26823704-B8B8E1A5-C6E4-4326-8F5A-88C63A1B88F7Q26995817-E30FF593-9783-4EFE-8302-13EEBEAF0BD6Q27315944-B7B5A9B8-7AEB-4F27-A5E6-087C1B466905Q27327234-8C30117E-F6A6-4DDF-B5CE-24EF85A958BAQ27347311-8575AEDE-E24B-4F54-86A2-0965F10813FEQ27677410-B2E8CEB3-C3CD-4503-AA8B-0E5A56A26709Q27938705-90A6DF7D-7546-4EFF-B703-6DBD7D83FCB4Q28344875-225BD642-5023-4B59-9D77-A21068D56D1BQ30308300-C49A00F6-20FB-436B-9F19-CCC2304671A7Q30455386-9FFEF2EE-B4AD-4BFF-BCF8-3EB3B546231DQ33348585-73C7DCB9-B905-4C81-98B1-D93FEA7C7481Q33807200-55663E0C-A5F0-450C-A9E4-4933FC47F3B0Q33861397-96EF425E-4FAA-4CB2-A47A-8326383E551DQ34077890-582E5221-264E-4225-B538-E0AE1061E031Q34467856-89B02551-11C8-4520-9265-7A2BB2ABEF66Q34517696-ACC55700-E13A-4635-B470-5C61600099D9Q34675213-DB13E0CF-A518-4F73-96B0-B7559AF641B3Q35095669-E86E286D-4DFD-4E93-9E49-DA4B49956177Q35129344-0EE1FE22-09B8-4627-982B-11F70B0F997FQ36172723-110DCD76-D96D-4321-9BD7-413F90F32CB4Q36561763-6830E281-0E56-4D27-B836-50D7F7202905Q36621450-D44BB418-212B-40F4-BF66-E5827380C7E7Q36742759-F39A4503-ED24-4095-B08D-9A059890E0F0Q36869603-54228FEF-CED8-4CE8-A29D-A25DD9016F6BQ37186184-CA434A9E-DBCC-4379-BDEF-DE82B8D8C661Q37289669-1CCBB6A7-71BD-4C5D-9043-EAC811DF3B0BQ37307494-0EBDE3E4-619E-454D-AC65-CF63488ACC54Q37412348-A367C470-18EF-4FEF-8BF1-D43F205A5448Q37595524-1ACB3018-1EF9-4DE1-AAC3-36B5E48B552DQ37667933-5E793763-CC76-41A3-A5E6-C585FB80F2FDQ38175453-CAF1DB6A-4D7B-4BD2-B9A7-FAAEA7CED8F5
P2860
A specific protein carboxyl methylesterase that demethylates phosphoprotein phosphatase 2A in bovine brain
description
1996 nî lūn-bûn
@nan
1996 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի հունիսին հրատարակված գիտական հոդված
@hy
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
name
A specific protein carboxyl me ...... phosphatase 2A in bovine brain
@ast
A specific protein carboxyl me ...... phosphatase 2A in bovine brain
@en
A specific protein carboxyl me ...... phosphatase 2A in bovine brain
@nl
type
label
A specific protein carboxyl me ...... phosphatase 2A in bovine brain
@ast
A specific protein carboxyl me ...... phosphatase 2A in bovine brain
@en
A specific protein carboxyl me ...... phosphatase 2A in bovine brain
@nl
prefLabel
A specific protein carboxyl me ...... phosphatase 2A in bovine brain
@ast
A specific protein carboxyl me ...... phosphatase 2A in bovine brain
@en
A specific protein carboxyl me ...... phosphatase 2A in bovine brain
@nl
P2093
P2860
P3181
P356
P1476
A specific protein carboxyl me ...... phosphatase 2A in bovine brain
@en
P2093
P2860
P304
P3181
P356
10.1073/PNAS.93.12.6043
P407
P577
1996-06-11T00:00:00Z