14-3-3 is phosphorylated by casein kinase I on residue 233. Phosphorylation at this site in vivo regulates Raf/14-3-3 interaction.
about
Protein kinase A phosphorylates and regulates dimerization of 14-3-3 epsilonThe interaction between casein kinase Ialpha and 14-3-3 is phosphorylation dependentProtein phosphatase 2A dephosphorylation of phosphoserine 112 plays the gatekeeper role for BAD-mediated apoptosis14-3-3 isotypes facilitate coupling of protein kinase C-zeta to Raf-1: negative regulation by 14-3-3 phosphorylationPhosphorylation of human keratin 18 serine 33 regulates binding to 14-3-3 proteinsProteomics-based target identification: bengamides as a new class of methionine aminopeptidase inhibitorsRegulation of Cbl molecular interactions by the co-receptor molecule CD43 in human T cellsIdentification of casein kinase Ialpha interacting protein partnersCasein kinase I associates with members of the centaurin-alpha family of phosphatidylinositol 3,4,5-trisphosphate-binding proteinsIdentification of 14-3-3zeta as a protein kinase B/Akt substrateSerine 58 of 14-3-3zeta is a molecular switch regulating ASK1 and oxidant stress-induced cell deathPhosphorylation-dependent 14-3-3 binding to LRRK2 is impaired by common mutations of familial Parkinson's diseaseIdentification of 14-3-3sigma mutation causing cutaneous abnormality in repeated-epilation mutant mouseInsight into conformational change for 14-3-3σ protein by molecular dynamics simulation.14-3-3 proteins are required for the inhibition of Ras by exoenzyme S.Proteomic identification of 14-3-3zeta as a mitogen-activated protein kinase-activated protein kinase 2 substrate: role in dimer formation and ligand bindingGene profiling of cottontail rabbit papillomavirus-induced carcinomas identifies upregulated genes directly Involved in stroma invasion as shown by small interfering RNA-mediated gene silencingA nonphosphorylated 14-3-3 binding motif on exoenzyme S that is functional in vivo.Exon B of human surfactant protein A2 mRNA, alone or within its surrounding sequences, interacts with 14-3-3; role of cis-elements and secondary structure.Function and specificity of 14-3-3 proteins in the regulation of carbohydrate and nitrogen metabolism.Proteome and phosphoproteome characterization reveals new response and defense mechanisms of Brachypodium distachyon leaves under salt stress.14-3-3 proteins in apoptosis.14-3-3 proteins as potential therapeutic targets.Increased 14-3-3 phosphorylation observed in Parkinson's disease reduces neuroprotective potential of 14-3-3 proteins.Phosphoproteomic identification of targets of the Arabidopsis sucrose nonfermenting-like kinase SnRK2.8 reveals a connection to metabolic processesDynamic interactions between 14-3-3 proteins and phosphoproteins regulate diverse cellular processes.14-3-3 proteins: a number of functions for a numbered protein.14-3-3 phosphoprotein interaction networks - does isoform diversity present functional interaction specification?Meiotic failure in cyclin A1-deficient mouse spermatocytes triggers apoptosis through intrinsic and extrinsic signaling pathways and 14-3-3 proteinsChanges in the effective gravitational field strength affect the state of phosphorylation of stress-related proteins in callus cultures of Arabidopsis thalianaSignificance of 14-3-3 self-dimerization for phosphorylation-dependent target binding.Plant 14-3-3 proteins as spiders in a web of phosphorylation.Oligomeric structure of 14-3-3 protein: what do we know about monomers?A structural basis for 14-3-3sigma functional specificity.MiR-320 inhibits the growth of glioma cells through downregulating PBX3.Isolation and characterization of casein kinase I from Dictyostelium discoideum.Regulation of casein kinase I epsilon and casein kinase I delta by an in vivo futile phosphorylation cycle.Dephosphorylation of the inhibitory phosphorylation site S287 in Xenopus Cdc25C by protein phosphatase-2A is inhibited by 14-3-3 binding.14-3-3zeta C-terminal stretch changes its conformation upon ligand binding and phosphorylation at Thr232.14-3-3 protein C-terminal stretch occupies ligand binding groove and is displaced by phosphopeptide binding.
P2860
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P2860
14-3-3 is phosphorylated by casein kinase I on residue 233. Phosphorylation at this site in vivo regulates Raf/14-3-3 interaction.
description
1997 nî lūn-bûn
@nan
1997 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
name
14-3-3 is phosphorylated by ca ...... ulates Raf/14-3-3 interaction.
@ast
14-3-3 is phosphorylated by ca ...... ulates Raf/14-3-3 interaction.
@en
14-3-3 is phosphorylated by ca ...... ulates Raf/14-3-3 interaction.
@nl
type
label
14-3-3 is phosphorylated by ca ...... ulates Raf/14-3-3 interaction.
@ast
14-3-3 is phosphorylated by ca ...... ulates Raf/14-3-3 interaction.
@en
14-3-3 is phosphorylated by ca ...... ulates Raf/14-3-3 interaction.
@nl
prefLabel
14-3-3 is phosphorylated by ca ...... ulates Raf/14-3-3 interaction.
@ast
14-3-3 is phosphorylated by ca ...... ulates Raf/14-3-3 interaction.
@en
14-3-3 is phosphorylated by ca ...... ulates Raf/14-3-3 interaction.
@nl
P2093
P2860
P356
P1476
14-3-3 is phosphorylated by ca ...... ulates Raf/14-3-3 interaction.
@en
P2093
Moelling K
Steinhussen U
P2860
P304
28882-28888
P356
10.1074/JBC.272.46.28882
P407
P577
1997-11-01T00:00:00Z