Essential role of a GXXXG motif for membrane channel formation by Helicobacter pylori vacuolating toxin. - sprookjes - yvandenbroek - TriplyDB

Essential role of a GXXXG motif for membrane channel formation by Helicobacter pylori vacuolating toxin.

Essential role of a GXXXG motif for membrane channel formation by Helicobacter pylori vacuolating toxin.

http://www.wikidata.org/entity/Q44299992

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Protein oligomerization mediated by the transmembrane carboxyl terminal domain of Bcl-XL Dimerization of the transmembrane domain of Integrin alphaIIb subunit in cell membranes An Overview of Helicobacter pylori VacA Toxin Biology Effect of Helicobacter pylori on gastric epithelial cells Crystal structure of the Helicobacter pylori vacuolating toxin p55 domain Nutrition and Helicobacter pylori: Host Diet and Nutritional Immunity Influence Bacterial Virulence and Disease Outcome A conserved GXXXG motif in APH-1 is critical for assembly and activity of the gamma-secretase complex Helicobacter pylori VacA toxin/subunit p34: targeting of an anion channel to the inner mitochondrial membrane.Mimicry of a host anion channel by a Helicobacter pylori pore-forming toxin.Random mutagenesis of Helicobacter pylori vacA to identify amino acids essential for vacuolating cytotoxic activity.GxxxG motifs within the amyloid precursor protein transmembrane sequence are critical for the etiology of Abeta42.Analysis of a beta-helical region in the p55 domain of Helicobacter pylori vacuolating toxin.Activation of the p75 neurotrophin receptor through conformational rearrangement of disulphide-linked receptor dimers Reconstitution of Helicobacter pylori VacA toxin from purified components Transmembrane glycine zippers: physiological and pathological roles in membrane proteins.Inhibition of primary human T cell proliferation by Helicobacter pylori vacuolating toxin (VacA) is independent of VacA effects on IL-2 secretion Role of innate immunity in Helicobacter pylori-induced gastric malignancy.Molecular insights revealing interaction of Tim23 and channel subunits of presequence translocase Structural determinants of human proton-coupled folate transporter oligomerization: role of GXXXG motifs and identification of oligomeric interfaces at transmembrane domains 3 and 6 Endosome-mitochondria juxtaposition during apoptosis induced by H. pylori VacA Molecular determinants and thermodynamics of the amyloid precursor protein transmembrane domain implicated in Alzheimer's disease.Role of connexin 43 in Helicobacter pylori VacA-induced cell death.Clustering of Helicobacter pylori VacA in lipid rafts, mediated by its receptor, receptor-like protein tyrosine phosphatase beta, is required for intoxication in AZ-521 Cells.Helicobacter pylori vacuolating cytotoxin A (VacA) engages the mitochondrial fission machinery to induce host cell death.Helicobacter pylori VacA induces programmed necrosis in gastric epithelial cells.the versatility of the Helicobacter pylori vacuolating cytotoxin vacA in signal transduction and molecular crosstalk.Helicobacter pylori VacA, a paradigm for toxin multifunctionality.Critical role of the first transmembrane domain of Cx26 in regulating oligomerization and function The intermediate region of Helicobacter pylori VacA is a determinant of toxin potency in a Jurkat T cell assay.Identification of a functionally critical GXXG motif and its relationship to the folate binding site of the proton-coupled folate transporter (PCFT-SLC46A1)Structural analysis of the oligomeric states of Helicobacter pylori VacA toxin.Helicobacter pylori VacA subdomain required for intracellular toxin activity and assembly of functional oligomeric complexes Helicobacter pylori in health and disease.The Pathogenic A116V Mutation Enhances Ion-Selective Channel Formation by Prion Protein in Membranes.The impact of autophagic processes on the intracellular fate of Helicobacter pylori: more tricks from an enigmatic pathogen?Clustering and redistribution of late endocytic compartments in response to Helicobacter pylori vacuolating toxin.Dominant-negative inhibitors of the Clostridium perfringens epsilon-toxin.Diet, microbial virulence, and Helicobacter pylori-induced gastric cancer.Fine mapping of the N-terminal cytotoxicity region of Clostridium perfringens enterotoxin by site-directed mutagenesis Membrane channel structure of Helicobacter pylori vacuolating toxin: role of multiple GXXXG motifs in cylindrical channels.

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P2860

Essential role of a GXXXG motif for membrane channel formation by Helicobacter pylori vacuolating toxin.

http://www.wikidata.org/entity/Q44299992

description

2003 nî lūn-bûn

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2003年の論文

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2003年学术文章

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2003年学术文章

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2003年学术文章

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2003年学术文章

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2003年學術文章

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2003年學術文章

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2003年學術文章

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name

Essential role of a GXXXG moti ...... cter pylori vacuolating toxin.

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Essential role of a GXXXG moti ...... cter pylori vacuolating toxin.

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type

label

Essential role of a GXXXG moti ...... cter pylori vacuolating toxin.

@en

Essential role of a GXXXG moti ...... cter pylori vacuolating toxin.

@nl

prefLabel

Essential role of a GXXXG moti ...... cter pylori vacuolating toxin.

@en

Essential role of a GXXXG moti ...... cter pylori vacuolating toxin.

@nl

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P1433

Journal of Biological Chemistry

P1476

Essential role of a GXXXG moti ...... cter pylori vacuolating toxin.

@en

P2093

Arlene D Vinion-Dubiel

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Gabor Szabo

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Hideki Iwamoto

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

Mark S McClain

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

Ping Cao

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

Yi Li

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

Zhifeng Shao

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P2860

The Structure of the Potassium Channel: Molecular Basis of K+ Conduction and Selectivity

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A simple method for displaying the hydropathic character of a protein

Bacillus thuringiensis CryIA(a) insecticidal toxin: crystal structure and channel formation

Structure of staphylococcal alpha-hemolysin, a heptameric transmembrane pore

A transmembrane helix dimer: structure and implications

Unidentified curved bacilli on gastric epithelium in active chronic gastritis

Self-association of N-syndecan (syndecan-3) core protein is mediated by a novel structural motif in the transmembrane domain and ectodomain flanking region

Molecular dynamics simulations of water within models of ion channels.

The vacuolating toxin from Helicobacter pylori forms hexameric pores in lipid bilayers at low pH.

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12101-12108

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10.1074/JBC.M212595200

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14

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278

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Timothy L. Cover

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2003-01-30T00:00:00Z

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10920940

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12562777

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P921

Helicobacter pylori