Inactivation of the Elongation Factor Tu by Mosquitocidal Toxin-Catalyzed Mono-ADP-Ribosylation
Author:
Affiliation:
1. Institut für Experimentelle und Klinische Pharmakologie und Toxikologie, Albert-Ludwigs-Universität Freiburg, D-79104 Freiburg
2. Institute of Physical Biochemistry, University of Witten/Herdecke, D-58448 Witten, Germany
Abstract
Publisher
American Society for Microbiology
Subject
Ecology,Applied Microbiology and Biotechnology,Food Science,Biotechnology
Link
https://journals.asm.org/doi/pdf/10.1128/AEM.68.10.4894-4899.2002
Reference30 articles.
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2. Braun, U., B. Habermann, I. Just, K. Aktories, and J. Vandekerckhove. 1989. 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 product. FEBS Lett.243:70-76.
3. Bredehorst, R., K. Wielckens, A. Gartemann, H. Lengyel, and K. Klapproth. 1978. Two different types of bonds linking single ADP-ribose residues covalently to proteins. Eur. J. Biochem.92:129-135.
4. Cassel, D., and T. Pfeuffer. 1978. Mechanism of cholera toxin action: covalent modification of the guanyl nucleotide-binding protein of the adenylate cyclase system. Proc. Natl. Acad. Sci. USA75:2669-2673.
5. Cervantes-Laurean, D., P. T. Loflin, D. E. Minter, E. L. Jacobson, and M. K. Jacobson. 1995. Protein modification by ADP-ribose via acid-labile linkages. J. Biol. Chem.270:7929-7936.
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