Outputs (2)

Internally quenched peptides for the study of lysostaphin: An antimicrobial protease that kills Staphylococcus aureus (2006)
Journal Article
Warfield, R., Bardelang, P., Saunders, H., Chan, W. C., Penfold, C., James, R., & Thomas, N. R. (2006). Internally quenched peptides for the study of lysostaphin: An antimicrobial protease that kills Staphylococcus aureus. Organic and Biomolecular Chemistry, 4(19), 3626-3638. https://doi.org/10.1039/b607999g

Lysostaphin (EC. 3.4.24.75) is a protein secreted by Staphylococcus simulans biovar staphylolyticus and has been shown to be active against methicillin resistant S. aureus (MRSA). The design and synthesis of three internally quenched substrates for l... Read More about Internally quenched peptides for the study of lysostaphin: An antimicrobial protease that kills Staphylococcus aureus.

Discovery of antagonist peptides against bacterial helicase-primase interaction in B. stearothermophilus by reverse yeast three-hybrid (2005)
Journal Article
Gardiner, L., Coyle, B. J., Chan, W. C., & Soultanas, P. (2005). Discovery of antagonist peptides against bacterial helicase-primase interaction in B. stearothermophilus by reverse yeast three-hybrid. Cell Chemistry Biology, 12(5), 595-604. https://doi.org/10.1016/j.chembiol.2005.04.007

Developing small-molecule antagonists against protein-protein interactions will provide powerful tools for mechanistic/functional studies and the discovery of new antibacterials. We have developed a reverse yeast three-hybrid approach that allows hig... Read More about Discovery of antagonist peptides against bacterial helicase-primase interaction in B. stearothermophilus by reverse yeast three-hybrid.