PEA-15 binding to ERK1/2 MAPKs is required for its modulation of integrin activation. - Wikidata - awgldk - TriplyDB

PEA-15 binding to ERK1/2 MAPKs is required for its modulation of integrin activation.

PEA-15 binding to ERK1/2 MAPKs is required for its modulation of integrin activation.

http://www.wikidata.org/entity/Q44594112

about

Phosphorylation of PEA-15 switches its binding specificity from ERK/MAPK to FADD Structure of ERK2 bound to PEA-15 reveals a mechanism for rapid release of activated MAPK Crystal structure of human CDC7 kinase in complex with its activator DBF4 An experimentally derived database of candidate Ras-interacting proteins.PEA15 impairs cell migration and correlates with clinical features predicting good prognosis in neuroblastoma RSK2 protein suppresses integrin activation and fibronectin matrix assembly and promotes cell migration Rap1 and its effector KRIT1/CCM1 regulate beta-catenin signaling.Matrix-specific suppression of integrin activation in shear stress signaling.PEA-15 unphosphorylated at both serine 104 and serine 116 inhibits ovarian cancer cell tumorigenicity and progression through blocking β-catenin.Computational insights for the discovery of non-ATP competitive inhibitors of MAP kinases Phosphoprotein enriched in astrocytes 15 kDa (PEA-15) reprograms growth factor signaling by inhibiting threonine phosphorylation of fibroblast receptor substrate 2alpha.CD98hc (SLC3A2) mediates integrin signaling.Phosphorylation of the transcription factor Ets-1 by ERK2: rapid dissociation of ADP and phospho-Ets-1.The death effector domain protein PEA-15 negatively regulates T-cell receptor signaling.The final steps of integrin activation: the end game Solution NMR insights into docking interactions involving inactive ERK2 Akt down-regulates ERK1/2 nuclear localization and angiotensin II-induced cell proliferation through PEA-15.Phosphoprotein enriched in astrocytes-15 kDa expression inhibits astrocyte migration by a protein kinase C delta-dependent mechanism Activation of mitogen-activated protein kinase is required for migration and invasion of placental site trophoblastic tumor.High ERK protein expression levels correlate with shorter survival in triple-negative breast cancer patients Development of PEA-15 using a potent non-viral vector for therapeutic application in breast cancer.CD98hc (SLC3A2) participates in fibronectin matrix assembly by mediating integrin signaling.MEK inhibition suppresses cell invasion and migration in ovarian cancers with activation of ERK1/2.Integrin α5β1 and p53 convergent pathways in the control of anti-apoptotic proteins PEA-15 and survivin in high-grade glioma A mechanism for death receptor discrimination by death adaptors.Phosphorylation of phosphoprotein enriched in astrocytes (PEA-15) regulates extracellular signal-regulated kinase-dependent transcription and cell proliferation.Essential role of p38gamma in K-Ras transformation independent of phosphorylation.PED/PEA-15 interacts with the 67 kD laminin receptor and regulates cell adhesion, migration, proliferation and apoptosis.Talin and signaling through integrins.PEA15 binds MAPK monomers and dimers Phospholipase C epsilon suppresses integrin activation.

P2860

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P2860

PEA-15 binding to ERK1/2 MAPKs is required for its modulation of integrin activation.

http://www.wikidata.org/entity/Q44594112

description

2003 nî lūn-bûn

@nan

2003年の論文

@ja

2003年学术文章

@wuu

2003年学术文章

@zh

2003年学术文章

@zh-cn

2003年学术文章

@zh-hans

2003年学术文章

@zh-my

2003年学术文章

@zh-sg

2003年學術文章

@yue

2003年學術文章

@zh-hant

name

PEA-15 binding to ERK1/2 MAPKs is required for its modulation of integrin activation.

@en

PEA-15 binding to ERK1/2 MAPKs is required for its modulation of integrin activation.

@nl

type

label

PEA-15 binding to ERK1/2 MAPKs is required for its modulation of integrin activation.

@en

PEA-15 binding to ERK1/2 MAPKs is required for its modulation of integrin activation.

@nl

prefLabel

PEA-15 binding to ERK1/2 MAPKs is required for its modulation of integrin activation.

@en

PEA-15 binding to ERK1/2 MAPKs is required for its modulation of integrin activation.

@nl

P1433

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P1433

Journal of Biological Chemistry

P1476

PEA-15 binding to ERK1/2 MAPKs is required for its modulation of integrin activation.

@en

P2093

Anne Brunet

http://www.w3.org/2001/XMLSchema#string

Fan-Li Chou

http://www.w3.org/2001/XMLSchema#string

Florian Uberall

http://www.w3.org/2001/XMLSchema#string

Justine M Hill

http://www.w3.org/2001/XMLSchema#string

Jyh-Cheng Hsieh

http://www.w3.org/2001/XMLSchema#string

Mark H Ginsberg

http://www.w3.org/2001/XMLSchema#string

Milton H Werner

http://www.w3.org/2001/XMLSchema#string

P2860

The structure of phosphorylated p38gamma is monomeric and reveals a conserved activation-loop conformation

Phosphoprotein-protein interactions revealed by the crystal structure of kinase-associated phosphatase in complex with phosphoCDK2

Crystal structure and mutational analysis of the human CDK2 kinase complex with cell cycle-regulatory protein CksHs1

Identification of a docking groove on ERK and p38 MAP kinases that regulates the specificity of docking interactions.

The structure of phosphorylated GSK-3beta complexed with a peptide, FRATtide, that inhibits beta-catenin phosphorylation

Crystal structures of MAP kinase p38 complexed to the docking sites on its nuclear substrate MEF2A and activator MKK3b

Recognition of ERK MAP kinase by PEA-15 reveals a common docking site within the death domain and death effector domain

Atomic structure of the MAP kinase ERK2 at 2.3 A resolution

The structure of mitogen-activated protein kinase p38 at 2.1-A resolution

Activation mechanism of the MAP kinase ERK2 by dual phosphorylation

P304

52587-52597

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scholarly article

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10.1074/JBC.M309322200

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P407

P433

52

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P478

278

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P50

Jacques Pouysségur

Angela J. Glading

P577

2003-09-23T00:00:00Z

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P698

14506247

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