AKTORIES PHARMAKOLOGIE PDF

He was Research Associate in Pharmacology at the University of Heidelberg from , received the degree Dr. His research interest is focused on cell signaling and its manipulation by bacterial protein toxins. His laboratory studies the interaction of toxins with target cells and the host receptors involved in toxin up-take and intracellular traffic. His group discovered the molecular mechanism of numerous bacterial toxins acting by ADP-ribosylation, glycosylation and deamidation of eukaryotic target proteins. Scientific aims are elucidation of the mode of actions of bacterial protein toxins as a prerequisite for development of anti-infection strategies and to use highly specific and potent toxins as pharmacological tools in cell biology and therapy. Role of membrane dynamics, intracellular trafficking and autophagosomal processes in cytotoxicity of Rho-modifying bacterial protein toxins.

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Various bacterial protein toxins and effectors target the actin cytoskeleton. Members of this group are numerous binary actin-ADP-ribosylating exotoxins e.

Clostridium botulinum C2 toxin as well as several bacterial ADP-ribosyltransferases e. Salmonella enterica SpvB which are not binary in structure. The second group includes toxins that modify actin to promote actin polymerization and the formation of actin aggregates. To this group belongs a toxin from the Photorhabdus luminescens Tc toxin complex that ADP-ribosylates actin at threonine Vibrio cholerae multifunctional, autoprocessing RTX toxin catalyses a chemical crosslinking reaction of actin thereby forming oligomers, while blocking the polymerization of actin to functional filaments.

Novel findings about members of these toxin groups are discussed in detail. This site needs JavaScript to work properly. Please enable it to take advantage of the complete set of features! Clipboard, Search History, and several other advanced features are temporarily unavailable.

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Similar articles Bidirectional attack on the actin cytoskeleton. Bacterial protein toxins causing polymerization or depolymerization of actin. Aktories K, et al. Epub Apr PMID: Review. Salmonella enterica SpvB ADP-ribosylates actin at position argininecharacterization of the catalytic domain within the SpvB protein and a comparison to binary clostridial actin-ADP-ribosylating toxins.

Hochmann H, et al. PMID: Crystal structure and novel recognition motif of rho ADP-ribosylating C3 exoenzyme from Clostridium botulinum: structural insights for recognition specificity and catalysis. Han S, et al. J Mol Biol. Characterization of the ADP-ribosylation of actin by Clostridium botulinum C2 toxin and Clostridium perfringens iota toxin. J Physiol Paris. Curr Top Microbiol Immunol. Show more similar articles See all similar articles. Cited by 50 articles Dynamic interactions within the host-associated microbiota cause tumor formation in the basal metazoan Hydra.

Rathje K, et al. PLoS Pathog. Galkina SI, et al. Int J Mol Sci. Etiology, epidemiology, pathology, and advances in diagnosis, vaccine development, and treatment of Gallibacterium anatis infection in poultry: a review. Narasinakuppe Krishnegowda D, et al. Vet Q. Diring J, et al. Nat Cell Biol. Epub Jun Show more "Cited by" articles See all "Cited by" articles. Publication types Research Support, Non-U. Gov't Actions. Review Actions. Animals Actions. Humans Actions. Models, Molecular Actions.

Polymerization Actions. Protein Conformation Actions. Substances Bacterial Toxins Actions. Adenosine Diphosphate Ribose Actions. Threonine Actions. Arginine Actions. Full-text links [x] Wiley. Copy Download.

BRAUTIGAN IN WATERMELON SUGAR PDF

Klaus Aktories

Various bacterial protein toxins and effectors target the actin cytoskeleton. Members of this group are numerous binary actin-ADP-ribosylating exotoxins e. Clostridium botulinum C2 toxin as well as several bacterial ADP-ribosyltransferases e. Salmonella enterica SpvB which are not binary in structure. The second group includes toxins that modify actin to promote actin polymerization and the formation of actin aggregates. To this group belongs a toxin from the Photorhabdus luminescens Tc toxin complex that ADP-ribosylates actin at threonine

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