Hsp90 is required for transfer of the cholera toxin A1 subunit from the endoplasmic reticulum to the cytosol. - Wikidata - wikimedia - TriplyDB

Hsp90 is required for transfer of the cholera toxin A1 subunit from the endoplasmic reticulum to the cytosol.

Hsp90 is required for transfer of the cholera toxin A1 subunit from the endoplasmic reticulum to the cytosol.

http://www.wikidata.org/entity/Q34181280

about

A deubiquitinase negatively regulates retro-translocation of nonubiquitinated substrates The delicate balance between secreted protein folding and endoplasmic reticulum-associated degradation in human physiology A bacterial toxin and a nonenveloped virus hijack ER-to-cytosol membrane translocation pathways to cause disease A therapeutic chemical chaperone inhibits cholera intoxication and unfolding/translocation of the cholera toxin A1 subunit Cytosolic entry of Shiga-like toxin a chain from the yeast endoplasmic reticulum requires catalytically active Hrd1p Hsp70 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 cells A novel Hsp70 inhibitor prevents cell intoxication with the actin ADP-ribosylating Clostridium perfringens iota toxin Detection of toxin translocation into the host cytosol by surface plasmon resonance.Alteration of the proteostasis network of plant cells promotes the post-endoplasmic reticulum trafficking of recombinant mutant (L444P) human β-glucocerebrosidase.Toxin instability and its role in toxin translocation from the endoplasmic reticulum to the cytosol.Ricin trafficking in cells Co- and post-translocation roles for HSP90 in cholera Intoxication.Establishment of an in vitro transport assay that reveals mechanistic differences in cytosolic events controlling cholera toxin and T-cell receptor α retro-translocation Protein-disulfide isomerase displaces the cholera toxin A1 subunit from the holotoxin without unfolding the A1 subunit Bacterial virulence in the moonlight: multitasking bacterial moonlighting proteins are virulence determinants in infectious disease Heat shock protein 90 (HSP90) contributes to cytosolic translocation of extracellular antigen for cross-presentation by dendritic cells Mechanism of diphtheria toxin catalytic domain delivery to the eukaryotic cell cytosol and the cellular factors that directly participate in the process.Geldanamycin Enhances Retrograde Transport of Shiga Toxin in HEp-2 Cells.Structural and functional interactions between the cholera toxin A1 subunit and ERdj3/HEDJ, a chaperone of the endoplasmic reticulum.The nucleotide exchange factors Grp170 and Sil1 induce cholera toxin release from BiP to enable retrotranslocation.Inhibition of Cholera Toxin and Other AB Toxins by Polyphenolic Compounds.An essential role for chloroplast heat shock protein 90 (Hsp90C) in protein import into chloroplasts.The ERdj5-Sel1L complex facilitates cholera toxin retrotranslocation The Lhs1/GRP170 chaperones facilitate the endoplasmic reticulum-associated degradation of the epithelial sodium channel Mouse Mammary Tumor Virus Signal Peptide Uses a Novel p97-Dependent and Derlin-Independent Retrotranslocation Mechanism To Escape Proteasomal Degradation.Into the intracellular logistics of cross-presentation.Clostridial binary toxins: iota and C2 family portraits.Insights on the trafficking and retro-translocation of glycosphingolipid-binding bacterial toxins.Cholera: pathophysiology and emerging therapeutic targets.Membrane translocation of binary actin-ADP-ribosylating toxins from Clostridium difficile and Clostridium perfringens is facilitated by cyclophilin A and Hsp90.Host Cell Chaperones Hsp70/Hsp90 and Peptidyl-Prolyl Cis/Trans Isomerases Are Required for the Membrane Translocation of Bacterial ADP-Ribosylating Toxins.Reporter assay for endo/lysosomal escape of toxin-based therapeutics.Intracellular events regulating cross-presentation.Hsp90 is involved in the entry of clostridial neurotoxins into the cytosol of nerve terminals.Cell Propagation of Cholera Toxin CTA ADP-Ribosylating Factor by Exosome Mediated Transfer.

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P2860

Hsp90 is required for transfer of the cholera toxin A1 subunit from the endoplasmic reticulum to the cytosol.

http://www.wikidata.org/entity/Q34181280

description

2010 nî lūn-bûn

@nan

2010 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի հուլիսին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

name

Hsp90 is required for transfer ...... smic reticulum to the cytosol.

@ast

Hsp90 is required for transfer ...... smic reticulum to the cytosol.

@en

Hsp90 is required for transfer ...... smic reticulum to the cytosol.

@nl

type

label

Hsp90 is required for transfer ...... smic reticulum to the cytosol.

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Hsp90 is required for transfer ...... smic reticulum to the cytosol.

@en

Hsp90 is required for transfer ...... smic reticulum to the cytosol.

@nl

prefLabel

Hsp90 is required for transfer ...... smic reticulum to the cytosol.

@ast

Hsp90 is required for transfer ...... smic reticulum to the cytosol.

@en

Hsp90 is required for transfer ...... smic reticulum to the cytosol.

@nl

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JBC.M110.148981

P1433

Journal of Biological Chemistry

P1476

Hsp90 is required for transfer ...... smic reticulum to the cytosol.

@en

P2093

Fernando Navarro-Garcia

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

Helen Burress

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

Jazmin Huerta

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

Keith Ireton

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

Ken Teter

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

Michael Taylor

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

Shane Massey

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

P2860

Hsp90 cochaperone Aha1 downregulation rescues misfolding of CFTR in cystic fibrosis

Cytosolic chaperones influence the fate of a toxin dislocated from the endoplasmic reticulum

Distinct roles for the Hsp40 and Hsp90 molecular chaperones during cystic fibrosis transmembrane conductance regulator degradation in yeast.

Cholera toxin: a paradigm for multi-functional engagement of cellular mechanisms (Review)

Stabilization of the tertiary structure of the cholera toxin A1 subunit inhibits toxin dislocation and cellular intoxication

Expression, activity and cytotoxicity of pertussis toxin S1 subunit in transfected mammalian cells.

Hsp90 and co-chaperones twist the functions of diverse client proteins.

N-terminal extension of the cholera toxin A1-chain causes rapid degradation after retrotranslocation from endoplasmic reticulum to cytosol

Entry of cholera toxin into polarized human intestinal epithelial cells. Identification of an early brefeldin A sensitive event required for A1-peptide generation.

Hsp-90-associated oncoproteins: multiple targets of geldanamycin and its analogs.

P304

31261-31267

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scholarly article

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10.1074/JBC.M110.148981

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P407

P433

41

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P478

285

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P577

2010-07-28T00:00:00Z

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20667832

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P921

endoplasmic reticulum

P932

2951200

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