The host cell chaperone Hsp90 is essential for translocation of the binary Clostridium botulinum C2 toxin into the cytosol.
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Binary bacterial toxins: biochemistry, biology, and applications of common Clostridium and Bacillus proteinsHIV-1 Tat enters T cells using coated pits before translocating from acidified endosomes and eliciting biological responsesTailored ß-cyclodextrin blocks the translocation pores of binary exotoxins from C. botulinum and C. perfringens and protects cells from intoxicationA recombinant fusion toxin based on enzymatic inactive C3bot1 selectively targets macrophagesCCT chaperonin complex is required for efficient delivery of anthrax toxin into the cytosol of host cellsBinding and internalization of Clostridium botulinum C2 toxinHsp70 facilitates trans-membrane transport of bacterial ADP-ribosylating toxins into the cytosol of mammalian cells.The Hsp90 machinery facilitates the transport of diphtheria toxin into human cellsA novel Hsp70 inhibitor prevents cell intoxication with the actin ADP-ribosylating Clostridium perfringens iota toxinFGF-1 and FGF-2 require the cytosolic chaperone Hsp90 for translocation into the cytosol and the cell nucleus.Clostridium difficile binary toxin CDT: mechanism, epidemiology, and potential clinical importance.Cross-reactivity of anthrax and C2 toxin: protective antigen promotes the uptake of botulinum C2I toxin into human endothelial cellsHsp90 is required for transfer of the cholera toxin A1 subunit from the endoplasmic reticulum to the cytosol.Clostridium and bacillus binary enterotoxins: bad for the bowels, and eukaryotic being.Presynaptic enzymatic neurotoxins.Role of CypA and Hsp90 in membrane translocation mediated by anthrax protective antigen.Co- and post-translocation roles for HSP90 in cholera Intoxication.A cell-permeable fusion protein based on Clostridium botulinum C2 toxin for delivery of p53 tumorsuppressor into cancer cells.Heat shock protein 90 (HSP90) contributes to cytosolic translocation of extracellular antigen for cross-presentation by dendritic cellsMechanism of diphtheria toxin catalytic domain delivery to the eukaryotic cell cytosol and the cellular factors that directly participate in the process.Heat shock inhibits caspase-1 activity while also preventing its inflammasome-mediated activation by anthrax lethal toxin.Clostridial toxins.Exploring the role of host cell chaperones/PPIases during cellular up-take of bacterial ADP-ribosylating toxins as basis for novel pharmacological strategies to protect mammalian cells against these virulence factors.Actin as target for modification by bacterial protein toxins.Multifaceted interactions of bacterial toxins with the gastrointestinal mucosa.Into the intracellular logistics of cross-presentation.Clostridial binary toxins: iota and C2 family portraits.Impact of clostridial glucosylating toxins on the proteome of colonic cells determined by isotope-coded protein labeling and LC-MALDI.Membrane translocation of binary actin-ADP-ribosylating toxins from Clostridium difficile and Clostridium perfringens is facilitated by cyclophilin A and Hsp90.Cellular Uptake of Clostridium botulinum C2 Toxin Requires Acid Sphingomyelinase ActivityHost Cell Chaperones Hsp70/Hsp90 and Peptidyl-Prolyl Cis/Trans Isomerases Are Required for the Membrane Translocation of Bacterial ADP-Ribosylating Toxins.Clostridial Binary Toxins: Basic Understandings that Include Cell Surface Binding and an Internal "Coup de Grâce".Formation of Nanotube-Like Protrusions, Regulation of Septin Organization and Re-guidance of Vesicle Traffic by Depolymerization of the Actin Cytoskeleton Induced by Binary Bacterial Protein Toxins.Reporter assay for endo/lysosomal escape of toxin-based therapeutics.Receptor-Binding and Uptake of Binary Actin-ADP-Ribosylating Toxins.gp96 is a human colonocyte plasma membrane binding protein for Clostridium difficile toxin A.EGA Protects Mammalian Cells from Clostridium difficile CDT, Clostridium perfringens Iota Toxin and Clostridium botulinum C2 Toxin.The host cell chaperone Hsp90 is necessary for cytotoxic action of the binary iota-like toxins.Chloroquine Analog Interaction with C2- and Iota-Toxin in Vitro and in Living Cells.Toxin Transport by A-B Type of Toxins in Eukaryotic Target Cells and Its Inhibition by Positively Charged Heterocyclic Molecules.
P2860
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P2860
The host cell chaperone Hsp90 is essential for translocation of the binary Clostridium botulinum C2 toxin into the cytosol.
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
2003年论文
@zh
2003年论文
@zh-cn
name
The host cell chaperone Hsp90 ...... num C2 toxin into the cytosol.
@en
type
label
The host cell chaperone Hsp90 ...... num C2 toxin into the cytosol.
@en
prefLabel
The host cell chaperone Hsp90 ...... num C2 toxin into the cytosol.
@en
P2093
P2860
P356
P1476
The host cell chaperone Hsp90 ...... num C2 toxin into the cytosol.
@en
P2093
Dieter K Meyer
Dirk Tiemann
Holger Barth
Jost Leemhuis
P2860
P304
32266-32274
P356
10.1074/JBC.M303980200
P407
P577
2003-06-12T00:00:00Z