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Dr Andrew McEwan

Dr Andrew McEwan
Dr Andrew McEwan
Dr Andrew McEwan

Advanced Research Fellow

About
School/Department
School of Medicine, Medical Sciences and Nutrition
Publications

Page 2 of 2 Results 11 to 17 of 17

  • An Efficient Method for the In Vitro Production of Azol(in)e-Based Cyclic Peptides

    Houssen, W. E., Bent, A. F., McEwan, A. R., Pieiller, N., Tabudravu, J., Koehnke, J., Mann, G., Adaba, R. I., Thomas, L., Hawas, U. W., Liu, H., Schwarz-Linek, U., Smith, M. C. M., Naismith, J. H., Jaspars, M.
    Angewandte Chemie International Edition, vol. 53, no. 51, pp. 14171-14174
    Contributions to Journals: Articles

  • Gated rotation mechanism of site-specific recombination by ΦC31 integrase

    Olorunniji, F. J., Buck, D. E., Colloms, S. D., McEwan, A. R., Smith, M. C., Stark, W. M., Rosser, S. J.
    Proceedings of the National Academy of Sciences of the United States of America, vol. 109, no. 48, pp. 19661-19666
    Contributions to Journals: Articles

  • Zinc is essential for high-affinity DNA binding and recombinase activity of phi C31 integrase

    McEwan, A. R., Raab, A., Kelly, S. M., Feldmann, J., Smith, M. C. M.
    Nucleic Acids Research, vol. 39, no. 14, pp. 6137-6147
    Contributions to Journals: Articles

  • Site-specific recombination by fC31 integrase and other large serine recombinases

    Smith, M. C. M., Brown, W. R. A., McEwan, A., Rowley, P. A.
    Biochemical Society Transactions, vol. 38, no. 2, pp. 388-394
    Contributions to Journals: Articles

  • DNA binding and synapsis by the large C-terminal domain of ϕC31 integrase

    McEwan, A., Rowley, P. A., Smith, M. C.
    Nucleic Acids Research, vol. 37, no. 14, pp. 4764-4773
    Contributions to Journals: Articles

  • The fluorinase from Streptomyces cattleya is also a chlorinase

    Deng, H., Cobb, S. L., McEwan, A. R., McGlinchey, R. P., Naismith, J. H., O'hagan, D., Robinson, D. A., Spencer, J. B.
    Angewandte Chemie International Edition, vol. 45, no. 5, pp. 759-762
    Contributions to Journals: Articles

  • Substrate specificity in enzymatic fluorination. The fluorinase from Streptomyces cattleya accepts 2'-deoxyadenosine substrates

    Cobb, S. L., Deng, H., McEwan, A. R., Naismith, J. H., O'hagan, D., Robinson, D. A.
    Organic & Biomolecular Chemistry, no. 8, pp. 1458-1460
    Contributions to Journals: Articles
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