Protein engineering studies of A-chain loop 47-56 of Escherichia coli heat-labile enterotoxin point to a prominent role of this loop for cytotoxicity
Author:
Publisher
Wiley
Subject
Molecular Biology,Microbiology
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1365-2958.1996.tb02520.x/fullpdf
Reference46 articles.
1. The Arg7Lys Mutant of Heat-Labile Enterotoxin Exhibits Great Flexibility of Active Site Loop 47-56 of the A Subunit
2. Purification of the B-Subunit Oligomer of Escherichia coli Heat-Labile Enterotoxin by Heterologous Expression and Secretion in a Marine Vibrio
3. Site-specific mutagenesis of the catalytic subunit of cholera toxin: substituting lysine for arginine 7 causes loss of activity
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3. Comparative Study on Characterization of Recombinant B Subunit of E. coli Heat-Labile Enterotoxin (rLTB) Prepared from E. coli and P. pastoris;J MICROBIOL BIOTECHN;2010
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5. Crystal structure of heat-labile enterotoxin from Escherichia coli with increased thermostability introduced by an engineered disulfide bond in the A subunit;Protein Science;2008-12-31
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