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The Journal of Biological Chemistry|March 5, 1993
Functional complementation of staphylococcal alpha-hemolysin fragments. Overlaps, nicks, and gaps in the glycine-rich loopB Walker, M Krishnasastry, H BayleyThe Journal of Biological Chemistry|October 25, 1992
Assembly of the oligomeric membrane pore formed by Staphylococcal alpha-hemolysin examined by truncation mutagenesisB Walker, M Krishnasastry, L Zorn, et al.Protein Engineering|May 1, 1994
A pore-forming protein with a metal-actuated switchB Walker, J Kasianowicz, M Krishnasastry, et al.FEBS Letters|December 12, 1994
Surface labeling of key residues during assembly of the transmembrane pore formed by staphylococcal alpha-hemolysinM Krishnasastry, B Walker, O Braha, et al.The Journal of Biological Chemistry|May 25, 1992
Functional expression of the alpha-hemolysin of Staphylococcus aureus in intact Escherichia coli and in cell lysates. Deletion of five C-terminal amino acids selectively impairs hemolytic activityB Walker, M Krishnasastry, L Zorn, et al.Pageof 1