Dr CHRISTOPHER PENFOLD's Outputs (4)

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.

Immunity protein release from a cell-bound nuclease colicin complex requires global conformational rearrangement (2013)
Journal Article
Vankemmelbeke, M., Housden, N. G., James, R., Kleanthous, C., & Penfold, C. N. (2013). Immunity protein release from a cell-bound nuclease colicin complex requires global conformational rearrangement. Microbiology Open, 2(5), https://doi.org/10.1002/mbo3.122

Nuclease colicins bind their target receptor BtuB in the outer membrane of sensitive Escherichia coli cells in the form of a high-affinity complex with their cognate immunity proteins. The release of the immunity protein from the colicin complex is a... Read More about Immunity protein release from a cell-bound nuclease colicin complex requires global conformational rearrangement.

Structural evidence that colicin a protein binds to a novel binding site of TolA protein in Escherichia coli periplasm (2012)
Journal Article
Li, C., Zhang, Y., Vankemmelbeke, M., Hecht, O., Aleanizy, F. S., Macdonald, C., Moore, G. R., James, R., & Penfold, C. N. (2012). Structural evidence that colicin a protein binds to a novel binding site of TolA protein in Escherichia coli periplasm. Journal of Biological Chemistry, 287(23), https://doi.org/10.1074/jbc.M112.342246

The Tol assembly of proteins is an interacting network of proteins located in the Escherichia coli cell envelope that transduces energy and contributes to cell integrity. TolA is central to this network linking the inner and outer membranes by intera... Read More about Structural evidence that colicin a protein binds to a novel binding site of TolA protein in Escherichia coli periplasm.

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.