Diphtheria toxin can simultaneously bind to its receptor and adenylyl-(3',5')-uridine 3'-monophosphate
- 1 October 1986
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 25 (21) , 6608-6611
- https://doi.org/10.1021/bi00369a041
Abstract
Note: In lieu of an abstract, this is the article's first page.This publication has 15 references indexed in Scilit:
- Diphtheria toxin-receptor interaction: A polyphosphate-insensitive diphtheria toxin-binding domainBiochemical and Biophysical Research Communications, 1982
- Studies on the Role of a Nucleoside‐Phosphate‐Binding Site of Diphtheria Toxin in the Binding of Toxin to Vero Cells or LiposomesEuropean Journal of Biochemistry, 1981
- An endogenous dinucleotide bound to diphtheria toxin. Adenylyl-(3',5')-uridine 3'-monophosphate.Journal of Biological Chemistry, 1981
- Diphtheria toxin fragment forms large pores in phospholipid bilayer membranes.Proceedings of the National Academy of Sciences, 1981
- Diphtheria toxin:receptor interaction. Characterization of the receptor interaction with the nucleotide-free toxin, the nucleotide-bound toxin, and the B-fragment of the toxin.Journal of Biological Chemistry, 1981
- Diphtheria toxin forms transmembrane channels in planar lipid bilayers.Proceedings of the National Academy of Sciences, 1981
- The entry of diphtheria toxin into the mammalian cell cytoplasm: evidence for lysosomal involvement.The Journal of cell biology, 1980
- Ligand interactions of diphtheria toxin. II. Relationships between the NAD site and the P site.Journal of Biological Chemistry, 1980
- Diphtheria toxin entry into cells is facilitated by low pH.The Journal of cell biology, 1980
- Protection of mammalian cells from diphtheria toxin by exogenous nucleotidesCanadian Journal of Microbiology, 1979