c-Jun can recruit JNK to phosphorylate dimerization partners via specific docking interactions
about
JNKK1 organizes a MAP kinase module through specific and sequential interactions with upstream and downstream components mediated by its amino-terminal extensionTargeting of p38 mitogen-activated protein kinases to MEF2 transcription factorsRole of the ATFa/JNK2 complex in Jun activationJSAP1, a novel jun N-terminal protein kinase (JNK)-binding protein that functions as a Scaffold factor in the JNK signaling pathwayMenin uncouples Elk-1, JunD and c-Jun phosphorylation from MAP kinase activationHomologous regions of the alpha subunit of eukaryotic translational initiation factor 2 (eIF2alpha) and the vaccinia virus K3L gene product interact with the same domain within the dsRNA-activated protein kinase (PKR)Human eukaryotic translation initiation factor 4G (eIF4G) recruits mnk1 to phosphorylate eIF4ERegulation of IL-4 expression by the transcription factor JunB during T helper cell differentiationA new c-Jun N-terminal kinase (JNK)-interacting protein, Sab (SH3BP5), associates with mitochondriaDifferential targeting of the stress mitogen-activated protein kinases to the c-Jun dimerization protein 2Identification of a docking groove on ERK and p38 MAP kinases that regulates the specificity of docking interactions.p38 and extracellular signal-regulated kinases regulate the myogenic program at multiple stepsExtracellular signal-regulated kinase binds to TFII-I and regulates its activation of the c-fos promoterRole for the pleckstrin homology domain-containing protein CKIP-1 in AP-1 regulation and apoptosisExpression of NPAT, a novel substrate of cyclin E-CDK2, promotes S-phase entrySubstrate discrimination among mitogen-activated protein kinases through distinct docking sequence motifsSelectivity of docking sites in MAPK kinasesAdaptable molecular interactions guide phosphorylation of the SR protein ASF/SF2 by SRPK1Smads bind directly to the Jun family of AP-1 transcription factorsIdentification of mitogen-activated protein kinase docking sites in enzymes that metabolize phosphatidylinositols and inositol phosphates.JNK Signaling: Regulation and Functions Based on Complex Protein-Protein Partnershipsp38α MAP Kinase C-Terminal Domain Binding Pocket Characterized by Crystallographic and Computational AnalysesCrystal structure of inhibitor of κB kinase βRepression of yeast Ste12 transcription factor by direct binding of unphosphorylated Kss1 MAPK and its regulation by the Ste7 MEKRegulation of c-Myc through phosphorylation at Ser-62 and Ser-71 by c-Jun N-terminal kinaseA docking site in MKK4 mediates high affinity binding to JNK MAPKs and competes with similar docking sites in JNK substratesThe AP-1 repressor, JDP2, is a bona fide substrate for the c-Jun N-terminal kinaseRegulation of two JunD isoforms by Jun N-terminal kinasesAP-1 repressor protein JDP-2: inhibition of UV-mediated apoptosis through p53 down-regulationc-Jun NH2-terminal kinases target the ubiquitination of their associated transcription factorsExtracellular signal-regulated kinase 1/2-mediated phosphorylation of JunD and FosB is required for okadaic acid-induced activator protein 1 activationA conserved docking site in MEKs mediates high-affinity binding to MAP kinases and cooperates with a scaffold protein to enhance signal transmissionA liver full of JNK: signaling in regulation of cell function and disease pathogenesis, and clinical approachesComputational prediction and experimental verification of new MAP kinase docking sites and substrates including Gli transcription factorsCell fate determination factor DACH1 inhibits c-Jun-induced contact-independent growthActivation of the cytochrome c gene by electrical stimulation in neonatal rat cardiac myocytes. Role of NRF-1 and c-JunThe Ras/Rac1/Cdc42/SEK/JNK/c-Jun cascade is a key pathway by which agonists stimulate DNA synthesis in primary cultures of rat hepatocytesp75-Ras-GRF1 is a c-Jun/AP-1 target protein: its up regulation results in increased Ras activity and is necessary for c-Jun-induced nonadherent growth of Rat1a cellsJNK phosphorylates synaptotagmin-4 and enhances Ca2+-evoked releasec-Jun amino-terminal kinase-1 mediates glucose-responsive upregulation of the RNA editing enzyme ADAR2 in pancreatic beta-cells
P2860
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P2860
c-Jun can recruit JNK to phosphorylate dimerization partners via specific docking interactions
description
1996 nî lūn-bûn
@nan
1996 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի նոյեմբերին 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
c-Jun can recruit JNK to phosp ...... specific docking interactions
@ast
c-Jun can recruit JNK to phosp ...... specific docking interactions
@en
c-Jun can recruit JNK to phosp ...... specific docking interactions
@nl
type
label
c-Jun can recruit JNK to phosp ...... specific docking interactions
@ast
c-Jun can recruit JNK to phosp ...... specific docking interactions
@en
c-Jun can recruit JNK to phosp ...... specific docking interactions
@nl
prefLabel
c-Jun can recruit JNK to phosp ...... specific docking interactions
@ast
c-Jun can recruit JNK to phosp ...... specific docking interactions
@en
c-Jun can recruit JNK to phosp ...... specific docking interactions
@nl
P2093
P3181
P1433
P1476
c-Jun can recruit JNK to phosp ...... specific docking interactions
@en
P2093
P304
P3181
P356
10.1016/S0092-8674(00)81999-6
P407
P577
1996-11-29T00:00:00Z