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  • ADP-Ribosylating Toxins
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      • Publisher's listprice EUR 106.99
      • The price is estimated because at the time of ordering we do not know what conversion rates will apply to HUF / product currency when the book arrives. In case HUF is weaker, the price increases slightly, in case HUF is stronger, the price goes lower slightly.

        44 374 Ft (42 261 Ft + 5% VAT)
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    44 374 Ft

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    Product details:

    • Edition number Softcover reprint of the original 1st ed. 1992
    • Publisher Springer Berlin Heidelberg
    • Date of Publication 10 January 2012
    • Number of Volumes 1 pieces, Book

    • ISBN 9783642769689
    • Binding Paperback
    • See also 9783540545989
    • No. of pages148 pages
    • Size 235x155 mm
    • Weight 260 g
    • Language English
    • Illustrations X, 148 p. 10 illus. Illustrations, black & white
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    Long description:

    ADP-ribosylating toxins have been the focus of intensive research for more than 30 years. Researchers from diverse fields of science have taken an interest in these bacterial toxins; they are studied, for example, by microbiologists, biochemists, cell biologists, and pharmacologists. There are two principal reasons for the broad and still growing interest in ADP­ ribosylating toxins. First, insights into the structure and functions of the toxins might be the key to prevention and treatment of diseases caused by the toxin-producing infectious micro­ organisms. Second, the ADP-ribosylating toxins provide potent and often unique pharmacological tools for the study of the physiological functions of their target proteins. The latter is especially the case with cholera and pertussis toxins, which both modify the IX-subunits of heterotrimeric G-proteins involved in signal transduction pathways. These toxins have proved invaluable in extending our basic understanding of the regulation of hormone-controlled signal transduction. This volume provides a review and an update of recent studies on the basic properties of bacterial ADP-ribosylating tbxins and/or exoenzymes. Our current knowledge of the cel­ lular entry mechanisms of ADP-ribosylating toxins is reviewed by MADSHUS and STENMARK. WILSON and COLLIER then deal with recent insights into the enzyme mechanism and active site structure of diphtheria toxin and Pseudomonas aeruginosa exotoxin A, which modify elongation factor 2. Toxins which ADP-ribosylate heterotrimeric G-proteins involved in trans­ membrane signal transduction are the subject of the next two chapters.

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    Table of Contents:

    List of Contents.- Entry of ADP-Ribosylating Toxins into Cells.- Diphtheria Toxin and Pseudomonasaeruginosa Exotoxin A: Active-Site Structure and Enzymic Mechanism.- Enhancement of Cholera Toxin-Catalyzed ADP-Ribosylation by Guanine Nucleotide-Binding Proteins.- ADP-Ribosylation of Signal-Transducing Guanine Nucleotide-Binding Proteins by Pertussis Toxin.- Clostridial Actin-ADP-Ribosylating Toxins.- Clostridium botulinum C3 ADP-Ribosyltransferase.- Pseudomonas aeruginosa Exoenzyme S.

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