Titlebook: Uptake and Trafficking of Protein Toxins; Holger Barth Book 2017 The Editor(s) (if applicable) and The Author(s), under exclusive license

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Gobble

Isolate

Receptors and Binding Structures for , Toxins A and B,First, these toxins are huge single-chain but multidomain proteins that display their action intracellularly within the cytosol of host cells. And second, albeit various cell types highly differ in their sensitivity toward these toxins, no toxin-resistant cell type has been described yet. Investigat

chapel

Cell Entry of C3 Exoenzyme from , , downstream signaling pathways. It is used as pharmacological tool to study cellular Rho functions. In addition, C3bot harbors a transferase-independent activity on neurons to promote axonal and dendritic growth and branching. Many bacterial protein toxins interact specifically with proteins and/or

Offbeat

Receptor-Binding and Uptake of Binary Actin-ADP-Ribosylating Toxins,ase, which modifies actin thereby inhibiting actin polymerization, and a binding component that forms heptamers after proteolytic activation. While C2 toxin interacts with carbohydrate structures on host cells, the group of iota-like toxins binds to lipolysis-stimulated lipoprotein receptor

小木槌

,Clostridial Binary Toxins: Basic Understandings that Include Cell Surface Binding and an Internal “, . and . are one group of enteric-acting toxins that attack the actin cytoskeleton of various cell types. These enterotoxins consist of A (enzymatic) and B (cell binding/membrane translocation) components that assemble on the targeted cell surface or in solution, forming a multimeric complex. Once

Abrupt

cleaver

Multivalent Inhibitors of Channel-Forming Bacterial Toxins,ng multiple finely-tuned points of contact between multivalent ligands and their supposed multivalent targets. Here, we describe several prominent examples where the multivalent blockers were investigated for their ability to directly obstruct oligomeric channel-forming bacterial exotoxins, such as