Bacterial Toxins that Covalently Modify Eukaryotic Proteins by ADP-Ribosylation
Author:
Affiliation:
1. Department of Microbiology; Medical College of Wisconsin; 8701 Watertown Plank Rd. Milwaukee WI 53226-0509
2. Food and Drug Administration; 8800 Rockville Pike Bethesda MD 20892
Publisher
ASM Press
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1128/9781555817893.ch15/fullpdf
Reference9 articles.
1. Crystal structure of nucleotide-free diphteria toxin;Bell;Biochemistry,1997
2. Photoaffinity labeling of diphtheria toxin fragment A with NAD: structure of the photoproduct at position 148;Carroll;Proc. Natl. Acad. Sci. USA,1985
3. The crystal structure of diphtheria toxin;Choe;Nature,1992
4. Three conserved consensus sequences identify the NAD-binding site of ADP-ribosylating enzymes, expressed by eukaryotes, bacteria and T-even bacteriophages;Domenighini;Mol. Microbiol,1996
5. Refined structure of Escherichia coli heat-labile enterotoxin, a close relative of cholera toxin;Sixma;J. Mol. Biol,1993
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