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Crystal structure of FAD-independent methylene-tetrahydrofolate reductase from <em>Mycobacterium hassiacum</em>
Gehl, M., Demmer, U., Ermler, U., & Shima, S. (2023). Crystal structure of FAD-independent methylene-tetrahydrofolate reductase from Mycobacterium hassiacum. Proteins, 91(9), 1329-1340. https://doi.org/10.1002/prot.26504
Novel potent and highly selective DDR1 inhibitors from integrated lead finding
Kuhn, B., Ritter, M., Benz, J., Kocer, B., Sarie, J. C., Hochstrasser, R., … Prunotto, M. (2023). Novel potent and highly selective DDR1 inhibitors from integrated lead finding. Medicinal Chemistry Research, 32(7), 1400-1425. https://doi.org/10.1007/s00044-023-03066-2
A novel pan-selective bromodomain inhibitor for epigenetic drug design
Warstat, R., Pervaiz, M., Regenass, P., Amann, M., Schmidtkunz, K., Einsle, O., … Günther, S. (2023). A novel pan-selective bromodomain inhibitor for epigenetic drug design. European Journal of Medicinal Chemistry, 249, 115139 (12 pp.). https://doi.org/10.1016/j.ejmech.2023.115139
Elucidation of a nutlin-derivative-HDM2 complex structure at the interaction site by NMR molecular replacement: a straightforward derivation
Mertens, V., Abi Saad, M. J., Coudevylle, N., Wälti, M. A., Finke, A., Marsh, M., & Orts, J. (2022). Elucidation of a nutlin-derivative-HDM2 complex structure at the interaction site by NMR molecular replacement: a straightforward derivation. Journal of Magnetic Resonance Open, 10-11, 100032 (5 pp.). https://doi.org/10.1016/j.jmro.2022.100032
A high quality, industrial data set for binding affinity prediction: performance comparison in different early drug discovery scenarios
Tosstorff, A., Rudolph, M. G., Cole, J. C., Reutlinger, M., Kramer, C., Schaffhauser, H., … Kuhn, B. (2022). A high quality, industrial data set for binding affinity prediction: performance comparison in different early drug discovery scenarios. Journal of Computer-Aided Molecular Design, 36(10), 753-765. https://doi.org/10.1007/s10822-022-00478-x
Activation, structure, biosynthesis and bioactivity of glidobactin-like proteasome inhibitors from <em>Photorhabdus laumondii</em>
Zhao, L., Le Chapelain, C., Brachmann, A. O., Kaiser, M., Groll, M., & Bode, H. B. (2021). Activation, structure, biosynthesis and bioactivity of glidobactin-like proteasome inhibitors from Photorhabdus laumondii. ChemBioChem, 22(9), 1582-1588. https://doi.org/10.1002/cbic.202100014
Structure-based macrocyclization of substrate analogue NS2B-NS3 protease inhibitors of Zika, West Nile and dengue viruses
Braun, N. J., Quek, J. P., Huber, S., Kouretova, J., Rogge, D., Lang-Henkel, H., … Steinmetzer, T. (2020). Structure-based macrocyclization of substrate analogue NS2B-NS3 protease inhibitors of Zika, West Nile and dengue viruses. ChemMedChem, 15(15), 1439-1452. https://doi.org/10.1002/cmdc.202000237
Drug design inspired by nature: crystallographic detection of an auto-tailored protease inhibitor template
Gall, F. M., Hohl, D., Frasson, D., Wermelinger, T., Mittl, P. R. E., Sievers, M., & Riedl, R. (2019). Drug design inspired by nature: crystallographic detection of an auto-tailored protease inhibitor template. Angewandte Chemie International Edition, 58(12), 4051-4055. https://doi.org/10.1002/anie.201812348
Improvement of aglycone π-stacking yields nanomolar to sub-nanomolar FimH antagonists
Schönemann, W., Cramer, J., Mühlethaler, T., Fiege, B., Silbermann, M., Rabbani, S., … Ernst, B. (2019). Improvement of aglycone π-stacking yields nanomolar to sub-nanomolar FimH antagonists. ChemMedChem, 14(7), 749-757. https://doi.org/10.1002/cmdc.201900051
A comprehensive analysis of the protein-ligand interactions in crystal structures of <em>Mycobacterium tuberculosis</em> EthR
Tanina, A., Wohlkönig, A., Soror, S. H., Flipo, M., Villemagne, B., Prevet, H., … Wintjens, R. (2019). A comprehensive analysis of the protein-ligand interactions in crystal structures of Mycobacterium tuberculosis EthR. Biochimica et Biophysica Acta: Proteins and Proteomics, 1867(3), 248-258. https://doi.org/10.1016/j.bbapap.2018.12.003
Crystal structure of the essential biotin-dependent carboxylase AccA3 from <em>Mycobacterium tuberculosis</em>
Bennett, M., & Högbom, M. (2017). Crystal structure of the essential biotin-dependent carboxylase AccA3 from Mycobacterium tuberculosis. FEBS Open Bio, 7(5), 620-626. https://doi.org/10.1002/2211-5463.12212
Structural elucidation of a nonpeptidic inhibitor specific for the human immunoproteasome
Cui, H., Baur, R., Le Chapelain, C., Dubiella, C., Heinemeyer, W., Huber, E. M., & Groll, M. (2017). Structural elucidation of a nonpeptidic inhibitor specific for the human immunoproteasome. ChemBioChem, 18(6), 523-526. https://doi.org/10.1002/cbic.201700021
A PDE6δ-KRas inhibitor chemotype with up to seven H-bonds and picomolar affinity that prevents efficient inhibitor release by Arl2
Martín-Gago, P., Fansa, E. K., Klein, C. H., Murarka, S., Janning, P., Schürmann, M., … Waldmann, H. (2017). A PDE6δ-KRas inhibitor chemotype with up to seven H-bonds and picomolar affinity that prevents efficient inhibitor release by Arl2. Angewandte Chemie International Edition, 56(9), 2423-2428. https://doi.org/10.1002/anie.201610957
Structural basis of microtubule stabilization by discodermolide
Prota, A. E., Bargsten, K., Redondo-Horcajo, M., Smith, A. B., Yang, C. P. H., McDaid, H. M., … Steinmetz, M. O. (2017). Structural basis of microtubule stabilization by discodermolide. ChemBioChem, 18(10), 905-909. https://doi.org/10.1002/cbic.201600696
Optimized target residence time: Type I½ inhibitors for p38α MAP kinase with improved binding kinetics through direct interaction with the R-spine
Wentsch, H. K., Walter, N. M., Bührmann, M., Mayer-Wrangowski, S., Rauh, D., Zaman, G. J. R., … Laufer, S. (2017). Optimized target residence time: Type I½ inhibitors for p38α MAP kinase with improved binding kinetics through direct interaction with the R-spine. Angewandte Chemie International Edition, 56(19), 5363-5367. https://doi.org/10.1002/anie.201701185
Optimization of inhibitors of <em>Mycobacterium tuberculosis</em> pantothenate synthetase based on group efficiency analysis
Hung, A. W., Silvestre, H. L., Wen, S., George, G. P. C., Boland, J., Blundell, T. L., … Abell, C. (2016). Optimization of inhibitors of Mycobacterium tuberculosis pantothenate synthetase based on group efficiency analysis. ChemMedChem, 11(1), 38-42. https://doi.org/10.1002/cmdc.201500414
Structure-based development of an affinity probe for sirtuin 2
Schiedel, M., Rumpf, T., Karaman, B., Lehotzky, A., Gerhardt, S., Ovádi, J., … Jung, M. (2016). Structure-based development of an affinity probe for sirtuin 2. Angewandte Chemie International Edition, 55(6), 2252-2256. https://doi.org/10.1002/anie.201509843
Targeted delivery of proteasome inhibitors to somatostatin-receptor-expressing cancer cells by octreotide conjugation
Beck, P., Cui, H., Hegemann, J. D., Marahiel, M. A., Krüger, A., & Groll, M. (2015). Targeted delivery of proteasome inhibitors to somatostatin-receptor-expressing cancer cells by octreotide conjugation. ChemMedChem, 10(12), 1969-1973. https://doi.org/10.1002/cmdc.201500449
Selective nhibition of the immunoproteasome by structure-based targeting of a non-catalytic cysteine
Dubiella, C., Baur, R., Cui, H., Huber, E. M., & Groll, M. (2015). Selective nhibition of the immunoproteasome by structure-based targeting of a non-catalytic cysteine. Angewandte Chemie International Edition, 54(52), 15888-15891. https://doi.org/10.1002/anie.201506631
Tracing binding modes in hit-to-lead optimization: chameleon-like poses of aspartic protease inhibitors
Kuhnert, M., Köster, H., Bartholomäus, R., Park, A. Y., Shahim, A., Heine, A., … Diederich, W. E. (2015). Tracing binding modes in hit-to-lead optimization: chameleon-like poses of aspartic protease inhibitors. Angewandte Chemie International Edition, 54(9), 2849-2853. https://doi.org/10.1002/anie.201411206