The Host Cell Chaperone Hsp90 Is Essential for Translocation of the Binary Clostridium botulinum C2 Toxin into the Cytosol
Open Access
- 1 August 2003
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 278 (34) , 32266-32274
- https://doi.org/10.1074/jbc.m303980200
Abstract
No abstract availableKeywords
This publication has 38 references indexed in Scilit:
- Translocation of botulinum neurotoxin light chain protease through the heavy chain channelNature Structural & Molecular Biology, 2002
- Hsp90The Journal of cell biology, 2001
- Cellular Uptake of the Clostridium perfringens Binary Iota-ToxinInfection and Immunity, 2001
- Low pH-induced Formation of Ion Channels by Clostridium difficile Toxin B in Target CellsJournal of Biological Chemistry, 2001
- Proteolytic Inactivation of MAP-Kinase-Kinase by Anthrax Lethal FactorScience, 1998
- pH‐dependent permeabilization of the plasma membrane of mammalian cells by anthrax protective antigenMolecular Microbiology, 1993
- Mechanisms of the cytopathic action of actin‐ADP‐ribosylating toxinsMolecular Microbiology, 1992
- The rho gene product expressed in E. Coli is a substrate of botulinum ADP-ribosyltransferase C3Biochemical and Biophysical Research Communications, 1989
- Clostridium spiroforme toxin is a binary toxin which ADP-ribosylates cellular actinBiochemical and Biophysical Research Communications, 1988
- Botulinum C2 toxin ADP-ribosylates actinNature, 1986