All Outputs (2)

Colicin import into E. coli cells: A model system for insights into the import mechanisms of bacteriocins (2014)
Journal Article
Kim, Y. C., Tarr, A. W., & Penfold, C. N. (2014). Colicin import into E. coli cells: A model system for insights into the import mechanisms of bacteriocins. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 1843(8), 1717-1731. https://doi.org/10.1016/j.bbamcr.2014.04.010

Bacteriocins are a diverse group of ribosomally synthesized protein antibiotics produced by most bacteria. They range from small lanthipeptides produced by lactic acid bacteria to much larger multi domain proteins of Gram negative bacteria such as th... Read More about Colicin import into E. coli cells: A model system for insights into the import mechanisms of bacteriocins.

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.