A therapeutic chemical chaperone inhibits cholera intoxication and unfolding/translocation of the cholera toxin A1 subunit - Wikidata - awgldk - TriplyDB

A therapeutic chemical chaperone inhibits cholera intoxication and unfolding/translocation of the cholera toxin A1 subunit

A therapeutic chemical chaperone inhibits cholera intoxication and unfolding/translocation of the cholera toxin A1 subunit

http://www.wikidata.org/entity/Q28477818

about

Emerging novel concept of chaperone therapies for protein misfolding diseases The delicate balance between secreted protein folding and endoplasmic reticulum-associated degradation in human physiology Modulation of toxin stability by 4-phenylbutyric acid and negatively charged phospholipids Detection of toxin translocation into the host cytosol by surface plasmon resonance.Grape extracts inhibit multiple events in the cell biology of cholera intoxication.Toxin instability and its role in toxin translocation from the endoplasmic reticulum to the cytosol.ADP-ribosylation factor 6 acts as an allosteric activator for the folded but not disordered cholera toxin A1 polypeptide.Co- and post-translocation roles for HSP90 in cholera Intoxication.Substrate-induced unfolding of protein disulfide isomerase displaces the cholera toxin A1 subunit from its holotoxin.On the role of protein disulfide isomerase in the retrograde cell transport of secreted phospholipases A2 Structural and functional interactions between the cholera toxin A1 subunit and ERdj3/HEDJ, a chaperone of the endoplasmic reticulum.A Conformational Shift in the Dissociated Cholera Toxin A1 Subunit Prevents Reassembly of the Cholera Holotoxin.Lipid rafts alter the stability and activity of the cholera toxin A1 subunit.Thermal Unfolding of the Pertussis Toxin S1 Subunit Facilitates Toxin Translocation to the Cytosol by the Mechanism of Endoplasmic Reticulum-Associated Degradation.Targeting bacterial toxins.Cholera: pathophysiology and emerging therapeutic targets.Host Cell Chaperones Hsp70/Hsp90 and Peptidyl-Prolyl Cis/Trans Isomerases Are Required for the Membrane Translocation of Bacterial ADP-Ribosylating Toxins.Cell Propagation of Cholera Toxin CTA ADP-Ribosylating Factor by Exosome Mediated Transfer.

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P2860

A therapeutic chemical chaperone inhibits cholera intoxication and unfolding/translocation of the cholera toxin A1 subunit

http://www.wikidata.org/entity/Q28477818

description

2011 nî lūn-bûn

@nan

2011 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի ապրիլին հրատարակված գիտական հոդված

@hy

2011年の論文

@ja

2011年論文

@yue

2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

@wuu

name

A therapeutic chemical chapero ...... f the cholera toxin A1 subunit

@ast

A therapeutic chemical chapero ...... f the cholera toxin A1 subunit

@en

A therapeutic chemical chapero ...... f the cholera toxin A1 subunit

@nl

type

label

A therapeutic chemical chapero ...... f the cholera toxin A1 subunit

@ast

A therapeutic chemical chapero ...... f the cholera toxin A1 subunit

@en

A therapeutic chemical chapero ...... f the cholera toxin A1 subunit

@nl

prefLabel

A therapeutic chemical chapero ...... f the cholera toxin A1 subunit

@ast

A therapeutic chemical chapero ...... f the cholera toxin A1 subunit

@en

A therapeutic chemical chapero ...... f the cholera toxin A1 subunit

@nl

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JOURNAL.PONE.0018825

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A therapeutic chemical chapero ...... f the cholera toxin A1 subunit

@en

P2093

Abhay H Pande

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

Fernando Navarro-Garcia

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

Jazmin Huerta

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

Ken Teter

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

Mansfield Burlingame

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

Suren A Tatulian

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

Tuhina Banerjee

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

P2860

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

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.

Inhibition of retrograde transport protects mice from lethal ricin challenge.

The low lysine content of ricin A chain reduces the risk of proteolytic degradation after translocation 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.

Transfer of the cholera toxin A1 polypeptide from the endoplasmic reticulum to the cytosol is a rapid process facilitated by the endoplasmic reticulum-associated degradation pathway

Inhibition of endoplasmic reticulum-associated degradation in CHO cells resistant to cholera toxin, Pseudomonas aeruginosa exotoxin A, and ricin.

Contribution of subdomain structure to the thermal stability of the cholera toxin A1 subunit.

P304

e18825

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scholarly article

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10.1371/JOURNAL.PONE.0018825

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4

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2011-04-19T00:00:00Z

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51082756

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21526142

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

P921

molecular chaperones

P932

3079739

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