Showing results (1-10 of 1,057) with videos related to
Sort By:
Pageof 106
Protein Engineering|May 1, 1994
A pore-forming protein with a metal-actuated switchB Walker, J Kasianowicz, M Krishnasastry, 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.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.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.Chemistry & Biology|July 1, 1997
Designed protein pores as components for biosensorsO Braha, B Walker, S Cheley, et al.The Journal of Biological Chemistry|September 29, 1995
Key residues for membrane binding, oligomerization, and pore forming activity of staphylococcal alpha-hemolysin identified by cysteine scanning mutagenesis and targeted chemical modificationB Walker, H BayleyProtein Engineering|May 1, 1995
Restoration of pore-forming activity in staphylococcal alpha-hemolysin by targeted covalent modificationB Walker, H BayleyProtein Engineering|January 1, 1994
A pore-forming protein with a protease-activated triggerB Walker, H BayleyBiophysical Journal|February 4, 1999
Genetically engineered metal ion binding sites on the outside of a Channel's transmembrane beta-barrelJ J Kasianowicz, D L Burden, L C Han, et al.Pageof 106