The dimeric versus monomeric status of 14-3-3zeta is controlled by phosphorylation of Ser58 at the dimer interface. - Wikidata - awgldk - TriplyDB

The dimeric versus monomeric status of 14-3-3zeta is controlled by phosphorylation of Ser58 at the dimer interface.

The dimeric versus monomeric status of 14-3-3zeta is controlled by phosphorylation of Ser58 at the dimer interface.

http://www.wikidata.org/entity/Q42799340

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Identification of 14-3-3zeta as an EGF receptor interacting protein 14-3-3zeta/tau heterodimers regulate Slingshot activity in migrating keratinocytes Modulation of 14-3-3 interaction with phosphorylated histone H3 by combinatorial modification patterns Proteomic and biochemical analysis of 14-3-3-binding proteins during C2-ceramide-induced apoptosis Caught in self-interaction: evolutionary and functional mechanisms of protein homooligomerization CpG island promoter methylation and silencing of 14-3-3sigma gene expression in LNCaP and Tramp-C1 prostate cancer cell lines is associated with methyl-CpG-binding protein MBD2 Sphingolipid signaling in metabolic disorders Characterization of 14-3-3-ζ Interactions with Integrin Tails Binding and transcriptional regulation by 14-3-3 (Bmh) proteins requires residues outside of the canonical motif.Regulation of yeast Yak1 kinase by PKA and autophosphorylation-dependent 14-3-3 binding.Serine 58 of 14-3-3zeta is a molecular switch regulating ASK1 and oxidant stress-induced cell death The application of an emerging technique for protein-protein interaction interface mapping: the combination of photo-initiated cross-linking protein nanoprobes with mass spectrometry.A computational framework for boosting confidence in high-throughput protein-protein interaction datasets Functional states of homooligomers: insights from the evolution of glycosyltransferases.14-3-3 protein masks the DNA binding interface of forkhead transcription factor FOXO4.Dimerization is essential for 14-3-3zeta stability and function in vivo 14-3-3 and its binding partners are regulators of protein-protein interactions during spermatogenesis Polarity proteins and cell-cell interactions in the testis.Mechanisms of protein oligomerization, the critical role of insertions and deletions in maintaining different oligomeric states Regulating survival and development in the retina: key roles for simple sphingolipids.Evolutionary, physicochemical, and functional mechanisms of protein homooligomerization.Transcriptional regulation of YWHAZ, the gene encoding 14-3-3ζ.Increased 14-3-3 phosphorylation observed in Parkinson's disease reduces neuroprotective potential of 14-3-3 proteins.Structural basis for protein-protein interactions in the 14-3-3 protein family Dynamic interactions between 14-3-3 proteins and phosphoproteins regulate diverse cellular processes.Klotho Regulates 14-3-3ζ Monomerization and Binding to the ASK1 Signaling Complex in Response to Oxidative Stress.14-3-3 proteins: a number of functions for a numbered protein.Destabilisation of dimeric 14-3-3 proteins as a novel approach to anti-cancer therapeutics.14-3-3 phosphoprotein interaction networks - does isoform diversity present functional interaction specification?Regulation of the subcellular localization of the G-protein subunit regulator GPSM3 through direct association with 14-3-3 protein.Bacterial co-expression of human Tau protein with protein kinase A and 14-3-3 for studies of 14-3-3/phospho-Tau interaction.14-3-3-regulated Ca(2+)-dependent protein kinase CPK3 is required for sphingolipid-induced cell death in Arabidopsis.A functional 14-3-3zeta-independent association of PI3-kinase with glycoprotein Ib alpha, the major ligand-binding subunit of the platelet glycoprotein Ib-IX-V complex Phosphorylation-dependent interaction with 14-3-3 in the regulation of bad trafficking in retinal ganglion cells.Built-in loops allow versatility in domain-domain interactions: lessons from self-interacting domains.Interaction of hookworm 14-3-3 with the forkhead transcription factor DAF-16 requires intact Akt phosphorylation sites Determinants of 14-3-3σ protein dimerization and function in drug and radiation resistance.Identification of chaperones in a MPP+-induced and ATRA/TPA-differentiated SH-SY5Y cell PD model.Sphingosine-dependent apoptosis: a unified concept based on multiple mechanisms operating in concert.Oligomeric structure of 14-3-3 protein: what do we know about monomers?

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P2860

The dimeric versus monomeric status of 14-3-3zeta is controlled by phosphorylation of Ser58 at the dimer interface.

http://www.wikidata.org/entity/Q42799340

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2003 nî lūn-bûn

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2003年の論文

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2003年論文

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2003年論文

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2003年論文

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2003年论文

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2003年论文

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2003年论文

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name

The dimeric versus monomeric s ...... Ser58 at the dimer interface.

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The dimeric versus monomeric s ...... Ser58 at the dimer interface.

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type

label

The dimeric versus monomeric s ...... Ser58 at the dimer interface.

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The dimeric versus monomeric s ...... Ser58 at the dimer interface.

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prefLabel

The dimeric versus monomeric s ...... Ser58 at the dimer interface.

@en

The dimeric versus monomeric s ...... Ser58 at the dimer interface.

@nl

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Journal of Biological Chemistry

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The dimeric versus monomeric s ...... Ser58 at the dimer interface.

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Frank C Stomski

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Jane Murphy

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Joanna M Woodcock

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Michael C Berndt

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P2860

Crystal structure of the 14-3-3zeta:serotonin N-acetyltransferase complex. a role for scaffolding in enzyme regulation

Suppression of apoptosis signal-regulating kinase 1-induced cell death by 14-3-3 proteins

Structure of a 14-3-3 protein and implications for coordination of multiple signalling pathways

Crystal structure of the zeta isoform of the 14-3-3 protein

Identification of 14-3-3zeta as a protein kinase B/Akt substrate

A dimeric 14-3-3 protein is an essential cofactor for Raf kinase activity

Isoforms of 14-3-3 protein can form homo- and heterodimers in vivo and in vitro: implications for function as adapter proteins

Phosphatidylinositol 3-kinase signaling inhibits DAF-16 DNA binding and function via 14-3-3-dependent and 14-3-3-independent pathways

Site-specific serine phosphorylation of the IL-3 receptor is required for hemopoietic cell survival

14-3-3 proteins: structure, function, and regulation

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36323-36327

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10.1074/JBC.M304689200

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38

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278

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phosphorylation