The Role of the Amino Terminus in the Kinetics and Assembly of α-Hemolysin of Staphylococcus aureus

This publication has 19 references indexed in Scilit:

• Crossing the Hydrophobic Barrier--Insertion of Membrane Proteins
  Science, 1996
• Structure of Staphylococcal α-Hemolysin, a Heptameric Transmembrane Pore
  Science, 1996
• The 2.0 Å crystal structure of a heterotrimeric G protein
  Nature, 1996
• Releasing the calcium trigger
  Nature Structural & Molecular Biology, 1995
• Surface labeling of key residues during assembly of the transmembrane pore formed by staphylococcal α‐hemolysin
  FEBS Letters, 1994
• A general method for the extraction of DNA from bacteria
  Journal of Microbiological Methods, 1994
• Structure of the Aeromonas toxin proaerolysin in its water-soluble and membrane-channel states
  Nature, 1994
• A pore-forming protein with a metal-actuated switch
  Protein Engineering, Design and Selection, 1994
• Rendering a membrane protein soluble in water: a common packing motif in bacterial protein toxins
  Trends in Biochemical Sciences, 1993
• Extent of N-terminal methionine excision from Escherichia coli proteins is governed by the side-chain length of the penultimate amino acid.
  Proceedings of the National Academy of Sciences, 1989