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Three-dimensional pharmacophore design and biochemical screening identifies substituted 1,2,4-triazoles as inhibitors of the annexin A2-S100A10 protein interaction (2012)
Journal Article
Reddy, T. R., Li, C., Fischer, P. M., & Dekker, L. V. (2012). Three-dimensional pharmacophore design and biochemical screening identifies substituted 1,2,4-triazoles as inhibitors of the annexin A2-S100A10 protein interaction. ChemMedChem, 7(8), https://doi.org/10.1002/cmdc.201200107

Protein interactions are increasingly appreciated as targets in small-molecule drug discovery. The interaction between the adapter protein S100A10 and its binding partner annexin A2 is a potentially important drug target. To obtain small-molecule sta... Read More about Three-dimensional pharmacophore design and biochemical screening identifies substituted 1,2,4-triazoles as inhibitors of the annexin A2-S100A10 protein interaction.

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., …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.