An ERK2 docking site in the Pointed domain distinguishes a subset of ETS transcription factors.
about
The biology of the Ets1 proto-oncogeneNovel role for PDEF in epithelial cell migration and invasionThe ePHD protein SPBP interacts with TopBP1 and together they co-operate to stimulate Ets1-mediated transcriptionDevelopment of ERK Activity Sensor, an in vitro, FRET-based sensor of Extracellular Regulated Kinase activity.Identification of mitogen-activated protein kinase docking sites in enzymes that metabolize phosphatidylinositols and inositol phosphates.Regulation of endothelial homeostasis, vascular development and angiogenesis by the transcription factor ERGMolecular mechanisms of ETS transcription factor-mediated tumorigenesisRas signaling requires dynamic properties of Ets1 for phosphorylation-enhanced binding to coactivator CBPConstitutive activation of the ETS-1-miR-222 circuitry in metastatic melanomaEAPII interacts with ETS1 and modulates its transcriptional functionThe many faces of SAMExtracellular signal-regulated kinase activated by epidermal growth factor and cell adhesion interacts with and phosphorylates vinexinRole of MAP kinases in the 1,25-dihydroxyvitamin D3-induced transactivation of the rat cytochrome P450C24 (CYP24) promoter. Specific functions for ERK1/ERK2 and ERK5The transcription factor ETS-1 regulates angiotensin II-stimulated fibronectin production in mesangial cellsER residency of the ceramide phosphoethanolamine synthase SMSr relies on homotypic oligomerization mediated by its SAM domainEts1 is an effector of protein kinase Calpha in cancer cells.ELF5 isoform expression is tissue-specific and significantly altered in cancer.The structural and dynamic basis of Ets-1 DNA binding autoinhibition.Differential regulation of NAB corepressor genes in Schwann cells.Deletion of ETS-1, a gene in the Jacobsen syndrome critical region, causes ventricular septal defects and abnormal ventricular morphology in mice.Phosphorylation of the transcription factor Ets-1 by ERK2: rapid dissociation of ADP and phospho-Ets-1.A model of a MAPK•substrate complex in an active conformation: a computational and experimental approachDNA binding by the ETS protein TEL (ETV6) is regulated by autoinhibition and self-association.Expanding the repertoire of an ERK2 recruitment site: cysteine footprinting identifies the D-recruitment site as a mediator of Ets-1 binding.Activation and mitogen-activated protein kinase regulation of transcription factors Ets and NF-kappaB in Mycobacterium-infected macrophages and role of these factors in tumor necrosis factor alpha and nitric oxide synthase 2 promoter function.Cyclin H binding to the RARalpha activation function (AF)-2 domain directs phosphorylation of the AF-1 domain by cyclin-dependent kinase 7.Docking sites on mitogen-activated protein kinase (MAPK) kinases, MAPK phosphatases and the Elk-1 transcription factor compete for MAPK binding and are crucial for enzymic activity.EBV-encoded LMP1 upregulates Igκ 3'enhancer activity and Igκ expression in nasopharyngeal cancer cells by activating the Ets-1 through ERKs signaling.Characterization of an ERK-binding domain in microphthalmia-associated transcription factor and differential inhibition of ERK2-mediated substrate phosphorylation.Analysis of mitogen-activated protein kinase activation and interactions with regulators and substratesMitogen-activated protein kinase (MAPK)-docking sites in MAPK kinases function as tethers that are crucial for MAPK regulation in vivo.Ancestral state reconstruction by comparative analysis of a GRN kernel operating in echinoderms.A genome-wide RNAi screen reveals MAP kinase phosphatases as key ERK pathway regulators during embryonic stem cell differentiation.GA-binding protein and p300 are essential components of a retinoic acid-induced enhanceosome in myeloid cellsThe novel SAM domain protein Aveugle is required for Raf activation in the Drosophila EGF receptor signaling pathwaySolution NMR insights into docking interactions involving inactive ERK2Signalling specificity of Ser/Thr protein kinases through docking-site-mediated interactions.E74-like factor 3 (ELF3) impacts on matrix metalloproteinase 13 (MMP13) transcriptional control in articular chondrocytes under proinflammatory stress.PAX3 and ETS1 synergistically activate MET expression in melanoma cells.Reverse genetic screening reveals poor correlation between morpholino-induced and mutant phenotypes in zebrafish.
P2860
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P2860
An ERK2 docking site in the Pointed domain distinguishes a subset of ETS transcription factors.
description
2002 nî lūn-bûn
@nan
2002 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
An ERK2 docking site in the Po ...... of ETS transcription factors.
@ast
An ERK2 docking site in the Po ...... of ETS transcription factors.
@en
type
label
An ERK2 docking site in the Po ...... of ETS transcription factors.
@ast
An ERK2 docking site in the Po ...... of ETS transcription factors.
@en
prefLabel
An ERK2 docking site in the Po ...... of ETS transcription factors.
@ast
An ERK2 docking site in the Po ...... of ETS transcription factors.
@en
P2860
P356
P1433
P1476
An ERK2 docking site in the Po ...... of ETS transcription factors.
@en
P2093
Barbara J Graves
Jeffrey J Seidel
P2860
P304
P356
10.1101/GAD.950902
P577
2002-01-01T00:00:00Z