Immunochemical Analysis of the Structure of Diphtheria Toxin Shows All Three Domains Undergo Structural Changes at Low pH

This publication has 25 references indexed in Scilit:

• Simple centrifugation method for efficient pelleting of both small and large unilamellar vesicles that allows convenient measurement of protein binding
  Biochemistry, 1993
• Targeting of specific domains of diphtheria toxin by site-directed antibodies
  Journal of General Microbiology, 1992
• The crystal structure of diphtheria toxin
  Nature, 1992
• Diphtheria toxin: membrane interaction and membrane translocation
  Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes, 1992
• Folding changes in membrane-inserted diphtheria toxin that may play important roles in its translocation
  Biochemistry, 1991
• Localization of the active site of diphtheria toxin
  Biochemistry, 1988
• Similarity of the conformation of diphtheria toxin at high temperature to that in the membrane-penetrating low-pH state.
  Proceedings of the National Academy of Sciences, 1986
• pH-dependence of the phospholipid interaction of diphtheria-toxin fragments
  Biochemical Journal, 1985
• Effect of pH on the conformation of diphtheria toxin and its implications for membrane penetration
  Biochemistry, 1985
• An immunological study of the diphtheria toxin molecule
  Immunochemistry, 1972