A Fluorescent Peptide Substrate for Measuring the ADP-Ribosylation Activity of the Cholera Toxin A-Subunit

2006 ◽  
Vol 2 (5) ◽  
pp. 195-199 ◽  
Author(s):  
Chun-Ting Yuen ◽  
Sjoerd Rijpkema
1994 ◽  
Vol 17 (5) ◽  
pp. 339-346 ◽  
Author(s):  
Kirsten L. Vadheim ◽  
Yogendra Singh ◽  
Jerry M. Keith
Keyword(s):  
Toxin A ◽  

2000 ◽  
Vol 32 (1) ◽  
pp. 69 ◽  
Author(s):  
Manju Sharma ◽  
Hemant Khanna ◽  
Naveen Arora ◽  
Yogendra Singh

2017 ◽  
Vol 659 ◽  
pp. 44-47 ◽  
Author(s):  
Mark R. Zielinski ◽  
Dmitry Gerashchenko
Keyword(s):  
Toxin A ◽  

1980 ◽  
Vol 186 (3) ◽  
pp. 749-754 ◽  
Author(s):  
C A Doberska ◽  
A J S MacPherson ◽  
B R Martin

1. Cholera toxin was shown to require the presence of GTP to activate rat liver plasma-membrane adenylate cyclase. ATP did not affect the activation process. 2. Cholera toxin catalysed the incorporation of 32P from NAD labelled in the alpha-phosphate group of the ADP moiety into a rat liver plasma-membrane protein with a subunit mol.wt. of 42 500. This is taken to demonstrate ADP-ribosylation. The ADP-ribosylation of this protein also required GTP and was unaffected by ATP. 3. Nicotinamide inhibited both the activation of adenylate cyclase by cholera toxin and the ADP-ribosylation of the protein of 42 500 subunit mol wt. Neither the activation nor the ADP-ribosylation could be reversed by treatment with nicotinamide in the presence of cholera toxin.


FEBS Letters ◽  
1997 ◽  
Vol 401 (1) ◽  
pp. 95-97 ◽  
Author(s):  
J Sanchez ◽  
R Argotte ◽  
A Buelna
Keyword(s):  
Toxin A ◽  

1998 ◽  
Vol 143 (3) ◽  
pp. 601-612 ◽  
Author(s):  
Irina Majoul ◽  
Kai Sohn ◽  
Felix Theodor Wieland ◽  
Rainer Pepperkok ◽  
Mariagrazia Pizza ◽  
...  

A cholera toxin mutant (CTX–K63) unable to raise cAMP levels was used to study in Vero cells the retrograde transport of the toxin A subunit (CTX-A–K63), which possesses a COOH-terminal KDEL retrieval signal. Microinjected GTP-γ-S inhibits the internalization as well as Golgi–ER transport of CTX-A–K63. The appearance of CTX-A–K63 in the Golgi induces a marked dispersion of Erd2p and p53 but not of the Golgi marker giantin. Erd2p is translocated under these conditions most likely to the intermediate compartment as indicated by an increased colocalization of Erd2p with mSEC13, a member of the mammalian coat protein II complex. IgGs as well as Fab fragments directed against Erd2p, β-COP, or p23, a new member of the p24 protein family, inhibit or block retrograde transport of CTX-A–K63 from the Golgi without affecting its internalization or its transport to the Golgi. Anti-Erd2p antibodies do not affect the binding of CTX-A to Erd2p, but inhibit the CTX-K63–induced translocation of Erd2p and p53.


2003 ◽  
Vol 45 (1) ◽  
pp. 25-31 ◽  
Author(s):  
Emilio A. Campos ◽  
Jun Namikoshi ◽  
Satomi Maeba ◽  
Masafumi Yamamoto ◽  
Masahiko Fukumoto ◽  
...  

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