Clostridium difficile Toxins A and B Are Cation-dependent UDP-glucose Hydrolases with Differing Catalytic Activities

This publication has 32 references indexed in Scilit:

• Toxins A and B from Clostridium difficile differ with respect to enzymatic potencies, cellular substrate specificities, and surface binding to cultured cells.
  Journal of Clinical Investigation, 1997
• Localization of the Glucosyltransferase Activity of Clostridium difficile Toxin B to the N-terminal Part of the Holotoxin
  Journal of Biological Chemistry, 1997
• The role of the metal ion in the p21ras catalysed GTP-hydrolysis: Mn2+versus Mg2+
  Journal of Molecular Biology, 1997
• Rho: a connection between membrane receptor signalling and the cytoskeleton
  Trends in Cell Biology, 1996
• UDP-Glucose Deficiency in a Mutant Cell Line Protects against Glucosyltransferase Toxins from Clostridium difficile and Clostridium sordellii
  Published by Elsevier ,1996
• Characterization and Partial Purification of a Novel Enzymatic Activity
  Published by Elsevier ,1995
• Small GTP-Binding Proteins and the Regulation of the Actin Cytoskeleton
  Annual Review of Cell Biology, 1994
• Kinetic properties of microsomal UDP-glucuronyltransferase. Regulation by metal ions
  Biochemical and Biophysical Research Communications, 1973
• Nuclear magnetic resonance studies of the function of potassium in the mechanism of pyruvate kinase
  Biochemistry, 1972
• Enzymes Activated by Monovalent Cations
  Science, 1970