Cholera toxin is exported from microsomes by the Sec61p complex.
about
Retrograde transport pathways utilised by viruses and protein toxinsEDEM is involved in retrotranslocation of ricin from the endoplasmic reticulum to the cytosolOne step at a time: endoplasmic reticulum-associated degradationUnfolded cholera toxin is transferred to the ER membrane and released from protein disulfide isomerase upon oxidation by Ero1A molecular portrait of the response to unfolded proteinsRecent technical developments in the study of ER-associated degradationThe delicate balance between secreted protein folding and endoplasmic reticulum-associated degradation in human physiologyThe protein translocation channel binds proteasomes to the endoplasmic reticulum membraneA bacterial toxin and a nonenveloped virus hijack ER-to-cytosol membrane translocation pathways to cause diseaseStabilization of the tertiary structure of the cholera toxin A1 subunit inhibits toxin dislocation and cellular intoxicationDetection of toxin translocation into the host cytosol by surface plasmon resonance.Identification of host cell factors required for intoxication through use of modified cholera toxinIntoxication of zebrafish and mammalian cells by cholera toxin depends on the flotillin/reggie proteins but not Derlin-1 or -2Cholera toxin toxicity does not require functional Arf6- and dynamin-dependent endocytic pathways.Identification and characterization of small molecules that inhibit intracellular toxin transportN-terminal extension of the cholera toxin A1-chain causes rapid degradation after retrotranslocation from endoplasmic reticulum to cytosolInhibitors of COP-mediated transport and cholera toxin action inhibit simian virus 40 infection.Conditionally and transiently disordered proteins: awakening cryptic disorder to regulate protein function.HEDJ, an Hsp40 co-chaperone localized to the endoplasmic reticulum of human cells.Endocytotic uptake and retrograde transport of a virally encoded killer toxin in yeast.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 pathwayInhibition of endoplasmic reticulum-associated degradation in CHO cells resistant to cholera toxin, Pseudomonas aeruginosa exotoxin A, and ricin.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.The cholera toxin A1(3) subdomain is essential for interaction with ADP-ribosylation factor 6 and full toxic activity but is not required for translocation from the endoplasmic reticulum to the cytosolCo- 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 subunitCharacterization of a mutant Escherichia coli heat-labile toxin, LT(R192G/L211A), as a safe and effective oral adjuvant.Low resolution structure and dynamics of a colicin-receptor complex determined by neutron scatteringStructural 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.Cross-presentation: dendritic cells and macrophages bite off more than they can chew!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.Endoplasmic Reticulum-Targeted Subunit Toxins Provide a New Approach to Rescue Misfolded Mutant Proteins and Revert Cell Models of Genetic Diseases.The VCP/p97 and YOD1 Proteins Have Different Substrate-dependent Activities in Endoplasmic Reticulum-associated Degradation (ERAD)A single native ganglioside GM1-binding site is sufficient for cholera toxin to bind to cells and complete the intoxication pathway.Derlin-1 facilitates the retro-translocation of cholera toxin.Journey to the Center of the Cell: Current Nanocarrier Design Strategies Targeting Biopharmaceuticals to the Cytoplasm and Nucleus
P2860
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P2860
Cholera toxin is exported from microsomes by the Sec61p complex.
description
2000 nî lūn-bûn
@nan
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
2000年论文
@zh
2000年论文
@zh-cn
name
Cholera toxin is exported from microsomes by the Sec61p complex.
@en
type
label
Cholera toxin is exported from microsomes by the Sec61p complex.
@en
prefLabel
Cholera toxin is exported from microsomes by the Sec61p complex.
@en
P2093
P2860
P356
P1476
Cholera toxin is exported from microsomes by the Sec61p complex.
@en
P2093
P2860
P304
P356
10.1083/JCB.148.6.1203
P407
P577
2000-03-01T00:00:00Z