Interactions between residues in staphylococcal alpha-hemolysin revealed by reversion mutagenesis.

Míreanna comhchosúla

• Assembly of the oligomeric membrane pore formed by Staphylococcal alpha-hemolysin examined by truncation mutagenesis.
  de réir: Walker, B, et al.
  Foilsithe / Cruthaithe: (1992)
• Key residues for membrane binding, oligomerization, and pore forming activity of staphylococcal alpha-hemolysin identified by cysteine scanning mutagenesis and targeted chemical modification.
  de réir: Walker, B, et al.
  Foilsithe / Cruthaithe: (1995)
• Surface labeling of key residues during assembly of the transmembrane pore formed by staphylococcal alpha-hemolysin.
  de réir: Krishnasastry, M, et al.
  Foilsithe / Cruthaithe: (1994)
• The internal cavity of the staphylococcal alpha-hemolysin pore accommodates approximately 175 exogenous amino acid residues.
  de réir: Jung, Y, et al.
  Foilsithe / Cruthaithe: (2005)
• Structure of staphylococcal alpha-hemolysin, a heptameric transmembrane pore.
  de réir: Song, L, et al.
  Foilsithe / Cruthaithe: (1996)