The Rho-ADP-ribosylating C3 exoenzyme from Clostridium botulinum and related C3-like transferases
- 28 August 2001
- Vol. 39 (11) , 1647-1660
- https://doi.org/10.1016/s0041-0101(01)00152-0
Abstract
No abstract availableThis publication has 139 references indexed in Scilit:
- Crystal structure and novel recognition motif of Rho ADP-ribosylating C3 exoenzyme from Clostridium botulinum: structural insights for recognition specificity and catalysisJournal of Molecular Biology, 2001
- Evidence that Arg‐295, Glu‐378, and Glu‐380 are active‐site residues of the ADP‐ribosyltransferase activity of iota toxinFEBS Letters, 1996
- Evidence for Rho-mediated Agonist Stimulation of Phospholipase D in Rat1 FibroblastsJournal of Biological Chemistry, 1996
- The Rho's progress: a potential role during neuritogenesis for the Rho family of GTPasesTrends in Neurosciences, 1995
- Synergistic Activation of Rat Brain Phospholipase D by ADP-ribosylation Factor and rhoA p21, and Its Inhibition by Clostridium botulinum C3 ExoenzymePublished by Elsevier ,1995
- ADP-ribosylation of a small size GTP-binding protein in bovine neutrophils by the C3 exoenzyme of Clostridium botulinum and effect on the cell motilityBiochemical and Biophysical Research Communications, 1991
- Molecular cloning and sequencing of the epidermal cell differentiation inhibitor gene from Staphylococcus aureusBiochemical and Biophysical Research Communications, 1991
- A novel epidermal cell differentiation inhibitor (EDIN): Purification and characterization from StaphylococcusaureusBiochemical and Biophysical Research Communications, 1990
- Purification of the 22 kDa protein substrate of botulinum ADP‐ribosyltransferase C3 from porcine brain cytosol and its characterization as a GTP‐binding protein highly homologous to the rho gene productFEBS Letters, 1989
- The rho gene product expressed in E. Coli is a substrate of botulinum ADP-ribosyltransferase C3Biochemical and Biophysical Research Communications, 1989