Primary structure of elongation factor 2 around the site of ADP-ribosylation is highly conserved from archaebacteria to eukaryotes
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(85)80736-5/fullpdf
Reference24 articles.
1. Diphtheria Toxin
2. Archaebacterial elongation factor is ADP-ribosylated by diphtheria toxin
3. Primary structure at the site in beef and wheat elongation factor 2 of ADP-ribosylation by diphtheria toxin
4. Selective inhibition of the reactions catalyzed by ribosome-specific transfer factors G
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1. Diphtheria toxin;The Comprehensive Sourcebook of Bacterial Protein Toxins;2015
2. The role of the diphthamide-containing loop within eukaryotic elongation factor 2 in ADP-ribosylation by Pseudomonas aeruginosa exotoxin A;Biochemical Journal;2008-06-12
3. STRUCTURE AND FUNCTION OF DIPHTHERIA TOXIN: FROM PATHOLOGY TO ENGINEERING;Journal of Toxicology: Toxin Reviews;2002-01
4. Posttranslational Modifications;Proteins;1998
5. Heterologous expression in Escherichia coli of the gene encoding an archaeal thermoacidophilic elongation factor 2. Properties of the recombinant protein;Biochimie;1997-05
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