A nonphosphorylated 14-3-3 binding motif on exoenzyme S that is functional in vivo. - Wikidata - awgldk - TriplyDB

A nonphosphorylated 14-3-3 binding motif on exoenzyme S that is functional in vivo.

A nonphosphorylated 14-3-3 binding motif on exoenzyme S that is functional in vivo.

http://www.wikidata.org/entity/Q33292512

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The interaction between casein kinase Ialpha and 14-3-3 is phosphorylation dependent Recognition of an intra-chain tandem 14-3-3 binding site within PKCepsilon Proteomic and biochemical analysis of 14-3-3-binding proteins during C2-ceramide-induced apoptosis Phosphorylation-independent interaction between 14-3-3 and exoenzyme S: from structure to pathogenesis Mdm38 is a 14-3-3-like receptor and associates with the protein synthesis machinery at the inner mitochondrial membrane Binding and transcriptional regulation by 14-3-3 (Bmh) proteins requires residues outside of the canonical motif.14-3-3σ Gene Loss Leads to Activation of the Epithelial to Mesenchymal Transition Due to the Stabilization of c-Jun Protein Tomato TFT1 is required for PAMP-triggered immunity and mutations that prevent T3S effector XopN from binding to TFT1 attenuate Xanthomonas virulence 14-3-3 proteins play a role in the cell cycle by shielding cdt2 from ubiquitin-mediated degradation Pseudomonas aeruginosa ExoS ADP-ribosyltransferase inhibits ERM phosphorylation.14-3-3zeta escorts CCTalpha for calcium-activated nuclear import in lung epithelia.Interaction of a 14-3-3 protein with the plant microtubule-associated protein EDE1 Electrostatic interactions play a minor role in the binding of ExoS to 14-3-3 proteins Protein modifications regulate the role of 14-3-3γ adaptor protein in cAMP-induced steroidogenesis in MA-10 Leydig cells.Platelet-derived growth factor (PDGF) regulates Slingshot phosphatase activity via Nox1-dependent auto-dephosphorylation of serine 834 in vascular smooth muscle cells.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.Phosphoregulatory protein 14-3-3 facilitates SAC1 transport from the endoplasmic reticulum.The type III secretion system of Pseudomonas aeruginosa: infection by injection.Functional domains and motifs of bacterial type III effector proteins and their roles in infection.The Reg1-interacting proteins, Bmh1, Bmh2, Ssb1, and Ssb2, have roles in maintaining glucose repression in Saccharomyces cerevisiae.MudPIT analysis of released proteins in Pseudomonas aeruginosa laboratory and clinical strains in relation to pro-inflammatory effects.Climbing fiber activity reduces 14-3-3-θ regulated GABA(A) receptor phosphorylation in cerebellar Purkinje cells.Translocation of Pseudomonas aeruginosa from the intestinal tract is mediated by the binding of ExoS to an Na,K-ATPase regulator, FXYD3.IDENTIFICATION AND EXPRESSION ANALYSIS OF TWO 14-3-3 PROTEINS IN THE MOSQUITO Aedes aegypti, AN IMPORTANT ARBOVIRUSES VECTOR.The 14-3-3 protein forms a molecular complex with heat shock protein Hsp60 and cellular prion protein.Caged phosphopeptides reveal a temporal role for 14-3-3 in G1 arrest and S-phase checkpoint function.The YopD translocator of Yersinia pseudotuberculosis is a multifunctional protein comprised of discrete domains.Identification of a host 14-3-3 Protein that Interacts with Xanthomonas effector AvrRxv.Exoenzyme S of Pseudomonas aeruginosa is not able to induce apoptosis when cells express activated proteins, such as Ras or protein kinase B/Akt.Chimeric 14-3-3 proteins for unraveling interactions with intrinsically disordered partners.Presence and distribution of 14-3-3 proteins in human ocular surface tissues.The Pseudomonas syringae effector HopQ1 promotes bacterial virulence and interacts with tomato 14-3-3 proteins in a phosphorylation-dependent manner.The binding site for regulatory 14-3-3 protein in plant plasma membrane H+-ATPase: involvement of a region promoting phosphorylation-independent interaction in addition to the phosphorylation-dependent C-terminal end.Xanthomonas T3S Effector XopN Suppresses PAMP-Triggered Immunity and Interacts with a Tomato Atypical Receptor-Like Kinase and TFT1.Host protein interactions with enteropathogenic Escherichia coli (EPEC): 14-3-3tau binds Tir and has a role in EPEC-induced actin polymerization.Delineation of exoenzyme S residues that mediate the interaction with 14-3-3 and its biological activity.Identification of Inhibitors of Pseudomonas aeruginosa Exotoxin-S ADP-Ribosyltransferase Activity.Identification and molecular characterization of a novel signaling molecule 14-3-3 epsilon in Clonorchis sinensis excretory/secretory products.Intracellular Localization of Type III-deliveredPseudomonasExoS with Endosome Vesicles

P2860

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P2860

A nonphosphorylated 14-3-3 binding motif on exoenzyme S that is functional in vivo.

http://www.wikidata.org/entity/Q33292512

description

2002 nî lūn-bûn

@nan

2002 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2002 թվականի հոտեմբերին 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

A nonphosphorylated 14-3-3 binding motif on exoenzyme S that is functional in vivo.

@ast

A nonphosphorylated 14-3-3 binding motif on exoenzyme S that is functional in vivo.

@en

type

label

A nonphosphorylated 14-3-3 binding motif on exoenzyme S that is functional in vivo.

@ast

A nonphosphorylated 14-3-3 binding motif on exoenzyme S that is functional in vivo.

@en

prefLabel

A nonphosphorylated 14-3-3 binding motif on exoenzyme S that is functional in vivo.

@ast

A nonphosphorylated 14-3-3 binding motif on exoenzyme S that is functional in vivo.

@en

P1433

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P356

J.1432-1033.2002.03191.X

P1433

P1476

A nonphosphorylated 14-3-3 binding motif on exoenzyme S that is functional in vivo.

@en

P2093

Alastair Aitken

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

Alex Peden

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

Bengt Hallberg

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

Kristina Stefansson

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

Margareta Aili

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

Maria L Henriksson

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

P2860

Akt promotes cell survival by phosphorylating and inhibiting a Forkhead transcription factor

Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine

Activation of Raf-1 by 14-3-3 proteins

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

Involvement of 14-3-3 proteins in nuclear localization of telomerase

Structural analysis of 14-3-3 phosphopeptide complexes identifies a dual role for the nuclear export signal of 14-3-3 in ligand binding

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

14-3-3zeta binds a phosphorylated Raf peptide and an unphosphorylated peptide via its conserved amphipathic groove

14-3-3 is involved in p75 neurotrophin receptor-mediated signal transduction.

P304

4921-4929

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P31

scholarly article

P356

10.1046/J.1432-1033.2002.03191.X

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P407

P433

20

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P478

269

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P50

Matthew S. Francis

P577

2002-10-01T00:00:00Z

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P5875

8422289

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P698

12383250

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