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Results: 7
Number of items: 7
  • Open Access
    Schmidt, M., Huang, Y.-H., Texeira de Oliveira, E. F., Toplak, A., Wijma, H. J., Janssen, D. B., van Maarseveen, J. H., Craik, D. J., & Nuijens, T. (2019). Efficient Enzymatic Cyclization of Disulfide-Rich Peptides by Using Peptide Ligases. ChemBioChem, 20(12), 1524-1529. https://doi.org/10.1002/cbic.201900033
  • Open Access
    Streefkerk, D. E., Schmidt, M., Ippel, J. H., Hackeng, T. M., Nuijens, T., Timmerman, P., & van Maarseveen, J. H. (2019). Synthesis of Constrained Tetracyclic Peptides by Consecutive CEPS, CLIPS, and Oxime Ligation. Organic Letters, 21(7), 2095-2100. https://doi.org/10.1021/acs.orglett.9b00378
  • Open Access
    Schmidt, M. (2019). Enzymatic tools for peptide ligation and cyclization: Development and applications. [Thesis, fully internal, Universiteit van Amsterdam].
  • Richelle, G., Schmidt, M., Hiemstra, H., Nuijens, T., van Maarseveen, J., & Timmerman, P. (2018). Multicyclic Peptides via Templated Tandem CLIPS/CuAAC Cyclizations. Journal of Peptide Science, 24(S2), S160. Article P225. https://doi.org/10.1002/psc.3127
  • Schmidt, M., Toplak, A., Rozeboom, H. J., Wijma, H. J., Quaedflieg, P. J. L. M., Van Maarseveen, J. H., Janssen, D. B., & Nuijens, T. (2018, January 10). Crystal structure of thymoligase, a substrate-tailored peptiligase variant [Data set]. Protein Data Bank (PDB). https://doi.org/10.2210/pdb5ox2/pdb
  • Open Access
    Schmidt, M., Toplak, A., Rozeboom, H. J., Wijma, H. J., Quaedflieg, P. J. L. M., van Maarseveen, J. H., Janssen, D. B., & Nuijens, T. (2018). Design of a substrate-tailored peptiligase variant for the efficient synthesis of thymosin-α1. Organic & Biomolecular Chemistry, 16(4), 609-618. https://doi.org/10.1039/c7ob02812a
  • Open Access
    Schmidt, M., Toplak, A., Quaedflieg, P. J. L. M., Ippel, H., Richelle, G. J. J., Hackeng, T. M., van Maarseveen, J. H., & Nuijens, T. (2017). Omniligase-1: A Powerful Tool for Peptide Head-to-Tail Cyclization. Advanced Synthesis & Catalysis, 359(12), 2050-2055. https://doi.org/10.1002/adsc.201700314
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