Order-disorder-order transitions mediate the activation of cholera toxin.
about
Modulation of toxin stability by 4-phenylbutyric acid and negatively charged phospholipidsA therapeutic chemical chaperone inhibits cholera intoxication and unfolding/translocation of the cholera toxin A1 subunitStabilization of the tertiary structure of the cholera toxin A1 subunit inhibits toxin dislocation and cellular intoxicationHsp90 is required for transfer of the cholera toxin A1 subunit from the endoplasmic reticulum to the cytosol.Contribution of subdomain structure to the thermal stability of the cholera toxin A1 subunit.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.Protein-disulfide isomerase displaces the cholera toxin A1 subunit from the holotoxin without unfolding the A1 subunitSubstrate-induced unfolding of protein disulfide isomerase displaces the cholera toxin A1 subunit from its holotoxin.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.Cholera toxin: an intracellular journey into the cytosol by way of the endoplasmic reticulum.Insights on the trafficking and retro-translocation of glycosphingolipid-binding bacterial toxins.There is Diversity in Disorder-"In all Chaos there is a Cosmos, in all Disorder a Secret Order".Host Cell Chaperones Hsp70/Hsp90 and Peptidyl-Prolyl Cis/Trans Isomerases Are Required for the Membrane Translocation of Bacterial ADP-Ribosylating Toxins.Carbohydrate inhibitors of cholera toxin.Cell Propagation of Cholera Toxin CTA ADP-Ribosylating Factor by Exosome Mediated Transfer.Protein disulfide isomerase does not act as an unfoldase in the disassembly of cholera toxin
P2860
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P2860
Order-disorder-order transitions mediate the activation of cholera toxin.
description
2008 nî lūn-bûn
@nan
2008年の論文
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2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
2008年论文
@zh
2008年论文
@zh-cn
name
Order-disorder-order transitions mediate the activation of cholera toxin.
@ast
Order-disorder-order transitions mediate the activation of cholera toxin.
@en
type
label
Order-disorder-order transitions mediate the activation of cholera toxin.
@ast
Order-disorder-order transitions mediate the activation of cholera toxin.
@en
prefLabel
Order-disorder-order transitions mediate the activation of cholera toxin.
@ast
Order-disorder-order transitions mediate the activation of cholera toxin.
@en
P2093
P2860
P1476
Order-disorder-order transitions mediate the activation of cholera toxin
@en
P2093
Andrea L Creath
Dianne I Lou
Glen B Legge
Ravi S Ampapathi
Steven R Blanke
P2860
P304
P356
10.1016/J.JMB.2007.12.075
P407
P50
P577
2008-01-05T00:00:00Z