Botulinum ADP-ribosyltransferase C3: a new tool to study low molecular weight GTP-binding proteins
Authors:
- Klaus AktoriesKlaus Aktories
- Alan HallAHAlan Hall
- 1 October 1989
- journal article
- review article
- Published by Elsevier in Trends in Pharmacological Sciences
- Vol. 10 (10) , 415-418
Abstract
No abstract availableKeywords
This publication has 32 references indexed in Scilit:
- 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
- Botulinum toxin‐induced ADP‐ribosylation and inhibition of exocytosis are unrelated eventsFEBS Letters, 1988
- A 22 kDa ras‐related G‐protein is the substrate for an ADP‐ribosyltransferase from Clostridium botulinumFEBS Letters, 1988
- Clostridium spiroforme toxin is a binary toxin which ADP-ribosylates cellular actinBiochemical and Biophysical Research Communications, 1988
- Separation of the 24 kDa substrate for botulinum C3 ADP-ribosyltransferase and the cholera toxin ADP-ribosylation factorBiochemical and Biophysical Research Communications, 1988
- Subcellular distribution and isoelectric heterogeneity of the substrate for ADP-ribosyl transferase fromBiochemical and Biophysical Research Communications, 1988
- Botulinum ADP‐ribosyltransferase C3 but not botulinum neurotoxins C1 and D ADP‐ribosylates low molecular mass GTP‐binding proteinsFEBS Letters, 1987
- ADP‐ribosylation of specific membrane proteins in pheochromocytoma and primary‐cultured brain cells by botulinum neurotoxins type C and DFEBS Letters, 1987
- Clostridium botulinum type C produces a novel ADP‐ribosyltransferase distinct from botulinum C2 toxinFEBS Letters, 1987