ADP-ribosylating toxins
著者
書誌事項
ADP-ribosylating toxins
（Current topics in microbiology and immunology, 175）
Springer, c1992
- : gw
- : us
大学図書館所蔵 件 / 全15件
-
該当する所蔵館はありません
- すべての絞り込み条件を解除する
この図書・雑誌をさがす
注記
Includes bibliographical references and index
内容説明・目次
内容説明
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.
目次
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.
「Nielsen BookData」 より