Thapsigargin-induced transport of cholera toxin to the endoplasmic reticulum. - Wikidata - wikimedia - TriplyDB

Thapsigargin-induced transport of cholera toxin to the endoplasmic reticulum.

Thapsigargin-induced transport of cholera toxin to the endoplasmic reticulum.

http://www.wikidata.org/entity/Q37236024

about

Entry of ricin and Shiga toxin into cells: molecular mechanisms and medical perspectives A dipeptide metalloendoprotease substrate completely blocks the response of cells in culture to cholera toxin.Endocytosis and intracellular transport of ricin: recent discoveries.Toxin entry: how bacterial proteins get into mammalian cells.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 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 cytosol Dynamin-mediated internalization of caveolae.Filipin-dependent inhibition of cholera toxin: evidence for toxin internalization and activation through caveolae-like domains.Protein toxins from plants and bacteria: probes for intracellular transport and tools in medicine.Retrograde transport of protein toxins through the Golgi apparatus.Cholera toxin up-regulates endoplasmic reticulum proteins that correlate with sensitivity to the toxin.Structural basis for the differential toxicity of cholera toxin and Escherichia coli heat-labile enterotoxin. Construction of hybrid toxins identifies the A2-domain as the determinant of differential toxicity.Toxin entry: retrograde transport through the secretory pathway.KDEL receptor (Erd2p)-mediated retrograde transport of the cholera toxin A subunit from the Golgi involves COPI, p23, and the COOH terminus of Erd2p.Differences in Caveolae Dynamics in Vascular Smooth Muscle Cells of Different Phenotypes

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Thapsigargin-induced transport of cholera toxin to the endoplasmic reticulum.

http://www.wikidata.org/entity/Q37236024

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on October 1996

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Thapsigargin-induced transport of cholera toxin to the endoplasmic reticulum.

@en

Thapsigargin-induced transport of cholera toxin to the endoplasmic reticulum.

@nl

type

label

Thapsigargin-induced transport of cholera toxin to the endoplasmic reticulum.

@en

Thapsigargin-induced transport of cholera toxin to the endoplasmic reticulum.

@nl

prefLabel

Thapsigargin-induced transport of cholera toxin to the endoplasmic reticulum.

@en

Thapsigargin-induced transport of cholera toxin to the endoplasmic reticulum.

@nl

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PNAS.93.22.12339

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Proceedings of the National Academy of Sciences of the United States of America

P1476

Thapsigargin-induced transport of cholera toxin to the endoplasmic reticulum.

@en

P2093

Garred O

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van Deurs B

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P2860

The three-dimensional crystal structure of cholera toxin

Rapid redistribution of Golgi proteins into the ER in cells treated with brefeldin A: evidence for membrane cycling from Golgi to ER

Protein and cell membrane iodinations with a sparingly soluble chloroamide, 1,3,4,6-tetrachloro-3a,6a-diphrenylglycoluril

A C-terminal signal prevents secretion of luminal ER proteins

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

Targeting of cholera toxin and Escherichia coli heat labile toxin in polarized epithelia: role of COOH-terminal KDEL

Structure and function of cholera toxin and the related Escherichia coli heat-labile enterotoxin

Routing of internalized ricin and ricin conjugates to the Golgi complex.

Brefeldin A redistributes resident and itinerant Golgi proteins to the endoplasmic reticulum

Localization of the Lys, Asp, Glu, Leu tetrapeptide receptor to the Golgi complex and the intermediate compartment in mammalian cells.

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12339-12343

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scholarly article

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10.1073/PNAS.93.22.12339

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22

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Kirsten Sandvig

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1996-10-01T00:00:00Z

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14304612

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8901582

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endoplasmic reticulum

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37992

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