Phosphorylation of PEA-15 switches its binding specificity from ERK/MAPK to FADD
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The PEA-15 protein regulates autophagy via activation of JNKOn the Quest of Cellular Functions of PEA-15 and the Therapeutic OpportunitiesFLIP and the death effector domain familyCorrelation of rat cortical Fas-associated death domain (FADD) protein phosphorylation with the severity of spontaneous morphine abstinence syndrome: role of α(2)-adrenoceptors and extracellular signal-regulated kinasesERK MAP kinase is targeted to RSK2 by the phosphoprotein PEA-15.PEA-15 unphosphorylated at both serine 104 and serine 116 inhibits ovarian cancer cell tumorigenicity and progression through blocking β-catenin.Phosphoprotein enriched in astrocytes 15 kDa (PEA-15) reprograms growth factor signaling by inhibiting threonine phosphorylation of fibroblast receptor substrate 2alpha.Effects of environmental tobacco smoke on adult rat brain biochemistry.The death effector domain protein PEA-15 negatively regulates T-cell receptor signaling.Phosphoprotein enriched in astrocytes (PEA)-15: a potential therapeutic target in multiple disease states.Species-specific microRNA roles elucidated following astrocyte activation.Bioactives from Artemisia dracunculus L. enhance insulin sensitivity via modulation of skeletal muscle protein phosphorylationGenomic analysis of the HER2/TOP2A amplicon in breast cancer and breast cancer cell lines.P45 forms a complex with FADD and promotes neuronal cell survival following spinal cord injury.A phospholipase Cγ1-activated pathway regulates transcription in human vascular smooth muscle cells.Death pathways triggered by activated Ras in cancer cellsIdentification of a novel AMPK-PEA15 axis in the anoikis-resistant growth of mammary cells.Characterization of a MAPK scaffolding protein logic gate in gonadotropes.Phosphoprotein enriched in astrocytes-15 kDa expression inhibits astrocyte migration by a protein kinase C delta-dependent mechanismEstradiol attenuates down-regulation of PEA-15 and its two phosphorylated forms in ischemic brain injuryRegulating TRAIL receptor-induced cell death at the membrane : a deadly discussionPEA-15 potentiates H-Ras-mediated epithelial cell transformation through phospholipase DMEK1/2 inhibitor selumetinib (AZD6244) inhibits growth of ovarian clear cell carcinoma in a PEA-15-dependent manner in a mouse xenograft modelHsp27 silencing coordinately inhibits proliferation and promotes Fas-induced apoptosis by regulating the PEA-15 molecular switch.Development of PEA-15 using a potent non-viral vector for therapeutic application in breast cancer.Phosphorylation is the switch that turns PEA-15 from tumor suppressor to tumor promoterRegulations of Reversal of Senescence by PKC Isozymes in Response to 12-O-Tetradecanoylphorbol-13-Acetate via Nuclear Translocation of pErk1/2.Ras and rheb signaling in survival and cell deathPTEN loss promotes mitochondrially dependent type II Fas-induced apoptosis via PEA-15.PEA-15 induces autophagy in human ovarian cancer cells and is associated with prolonged overall survival.ERK and cell death: mechanisms of ERK-induced cell death--apoptosis, autophagy and senescence.Targetting PED/PEA-15 for diabetes treatment.Melatonin prevents down-regulation of astrocytic phosphoprotein PEA-15 in ischemic brain injury.Protein phosphatase 4 regulates apoptosis in leukemic and primary human T-cells.Chaperone-mediated autophagy substrate proteins in cancer.PED/PEA-15 interacts with the 67 kD laminin receptor and regulates cell adhesion, migration, proliferation and apoptosis.PEA-15 (Phosphoprotein Enriched in Astrocytes 15) Is a Protective Mediator in the Vasculature and Is Regulated During Neointimal Hyperplasia.NMR backbone dynamics studies of human PED/PEA-15 outline protein functional sites.Effects of anti-depressant treatments on FADD and p-FADD protein in rat brain cortex: enhanced anti-apoptotic p-FADD/FADD ratio after chronic desipramine and fluoxetine administration.Nonapoptotic functions of Fas/CD95 in the immune response.
P2860
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P2860
Phosphorylation of PEA-15 switches its binding specificity from ERK/MAPK to FADD
description
2005 nî lūn-bûn
@nan
2005 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Phosphorylation of PEA-15 switches its binding specificity from ERK/MAPK to FADD
@ast
Phosphorylation of PEA-15 switches its binding specificity from ERK/MAPK to FADD
@en
Phosphorylation of PEA-15 switches its binding specificity from ERK/MAPK to FADD
@en-gb
Phosphorylation of PEA-15 switches its binding specificity from ERK/MAPK to FADD
@nl
type
label
Phosphorylation of PEA-15 switches its binding specificity from ERK/MAPK to FADD
@ast
Phosphorylation of PEA-15 switches its binding specificity from ERK/MAPK to FADD
@en
Phosphorylation of PEA-15 switches its binding specificity from ERK/MAPK to FADD
@en-gb
Phosphorylation of PEA-15 switches its binding specificity from ERK/MAPK to FADD
@nl
prefLabel
Phosphorylation of PEA-15 switches its binding specificity from ERK/MAPK to FADD
@ast
Phosphorylation of PEA-15 switches its binding specificity from ERK/MAPK to FADD
@en
Phosphorylation of PEA-15 switches its binding specificity from ERK/MAPK to FADD
@en-gb
Phosphorylation of PEA-15 switches its binding specificity from ERK/MAPK to FADD
@nl
P2093
P2860
P356
P1433
P1476
Phosphorylation of PEA-15 switches its binding specificity from ERK/MAPK to FADD
@en
P2093
Anna Knapinska
Hema Vaidyanathan
Hemamalini Renganathan
P2860
P304
P356
10.1042/BJ20050378
P407
P50
P577
2005-09-15T00:00:00Z