Structure and function of cholera toxin and the related Escherichia coli heat-labile enterotoxin
Article Abstract:
The high morbidity of Cholera and the Escherichia coli-associated diarrheal disease is of concern among Third World countries where they are prevalent and transmissible by contaminated water supply. The cholera toxin secreted by the bacterium Vibrio cholera and the heat-labile enterotoxin of Escherichia coli exert their virulence by binding to receptors in intestinal epithelial cells and inserting an enzymatic subunit which stimulates the production of cyclic AMP as well as increase prostaglandin synthesis that lead to the excessive loss of fluids and electrolytes. Both toxins are found to be structurally and functionally related.
Publication Name: Microbiological Reviews
Subject: Biological sciences
ISSN: 0146-0749
Year: 1992
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Heat shock proteins: molecular chaperones of protein biogenesis
Article Abstract:
Heat-shock proteins (Hsps) are directly involved in protein biogenesis from the synthesis as nascent chains to the assembly of multimeric complexes. Hsps facilitate protein biogenesis by blocking nonproductive protein-protein interaction, and act as intermediaries in the folding of proteins. The two major groups of Hsps are 70-kDa, which play a critical role in the translocation of proteins from cytosol to organelles, and 60-kDa, which bind unfolded proteins and prevent their aggregation.
Publication Name: Microbiological Reviews
Subject: Biological sciences
ISSN: 0146-0749
Year: 1993
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Molecular biology of microbial ureases
Article Abstract:
Genetic and structural studies are providing a clearer view of the mechanism and regulation of urease, which has an important role in the pathogenesis of a number of bacterial infections. Synthesis of the enzyme, which hydrolyzes urea to produce ammonia and carbamate, can be regulated by nitrogen or urea. The assembly of its catalytic metallocenter requires nickel and carbon dioxide, and may also require accessory genes known to be needed for urease activation.
Publication Name: Microbiological Reviews
Subject: Biological sciences
ISSN: 0146-0749
Year: 1995
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