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Structure based design of bicyclic Peptide inhibitors of RbAp48
Hart, P. 't., Hommen, P., Noisier, A., Krzyzanowski, A., Schüler, D., Porfetye, A. T., … Waldmann, H. (2021). Structure based design of bicyclic Peptide inhibitors of RbAp48. Angewandte Chemie International Edition, 60(4), 1813-1820. https://doi.org/10.1002/anie.202009749
Towards photochromic azobenzene-based inhibitors for tryptophan synthase
Simeth, N. A., Kinateder, T., Rajendran, C., Nazet, J., Merkl, R., Sterner, R., … Kneuttinger, A. C. (2021). Towards photochromic azobenzene-based inhibitors for tryptophan synthase. Chemistry: A European Journal, 27(7), 2439-2451. https://doi.org/10.1002/chem.202004061
Inhibition of 14-3-3/Tau by hybrid small-molecule peptides operating via two different binding modes
Andrei, S. A., Meijer, F. A., Neves, J. F., Brunsveld, L., Landrieu, I., Ottmann, C., & Milroy, L. G. (2018). Inhibition of 14-3-3/Tau by hybrid small-molecule peptides operating via two different binding modes. ACS Chemical Neuroscience, 9(11), 2639-2654. https://doi.org/10.1021/acschemneuro.8b00118
X-ray structures and feasibility assessment of CLK2 inhibitors for Phelan-McDermid syndrome
Kallen, J., Bergsdorf, C., Arnaud, B., Bernhard, M., Brichet, M., Cobos-Correa, A., … Lerchner, A. (2018). X-ray structures and feasibility assessment of CLK2 inhibitors for Phelan-McDermid syndrome. ChemMedChem, 13(18), 1997-2007. https://doi.org/10.1002/cmdc.201800344
Mono- and bivalent 14-3-3 inhibitors for characterizing supramolecular "lysine wrapping" of oligoethylene glycol (OEG) moieties in proteins
Yilmaz, E., Bier, D., Guillory, X., Briels, J., Ruiz-Blanco, Y. B., Sanchez-Garcia, E., … Kaiser, M. (2018). Mono- and bivalent 14-3-3 inhibitors for characterizing supramolecular "lysine wrapping" of oligoethylene glycol (OEG) moieties in proteins. Chemistry: A European Journal, 24(52), 13807-13814. https://doi.org/10.1002/chem.201801074
Azaindoles as zinc-binding small-molecule inhibitors of the JAMM protease CSN5
Altmann, E., Erbel, P., Renatus, M., Schaefer, M., Schlierf, A., Druet, A., … Quancard, J. (2017). Azaindoles as zinc-binding small-molecule inhibitors of the JAMM protease CSN5. Angewandte Chemie International Edition, 56(5), 1294-1297. https://doi.org/10.1002/anie.201608672
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
Chemoproteomics-Aided Medicinal Chemistry for the Discovery of EPHA2 Inhibitors
Heinzlmeir, S., Lohse, J., Treiber, T., Kudlinzki, D., Linhard, V., Gande, S. L., … Médard, G. (2017). Chemoproteomics-Aided Medicinal Chemistry for the Discovery of EPHA2 Inhibitors. ChemMedChem, 12(12), 999-1011. https://doi.org/10.1002/cmdc.201700217
Crystal structures of ERAP2 complexed with inhibitors reveal pharmacophore requirements for optimizing inhibitor potency
Mpakali, A., Giastas, P., Deprez-Poulain, R., Papakyriakou, A., Koumantou, D., Gealageas, R., … Saridakis, E. (2017). Crystal structures of ERAP2 complexed with inhibitors reveal pharmacophore requirements for optimizing inhibitor potency. ACS Medicinal Chemistry Letters, 8(3), 333-337. https://doi.org/10.1021/acsmedchemlett.6b00505
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
Tunable Probes with Direct Fluorescence Signals for the Constitutive and Immunoproteasome
Dubiella, C., Cui, H., & Groll, M. (2016). Tunable Probes with Direct Fluorescence Signals for the Constitutive and Immunoproteasome. Angewandte Chemie International Edition, 55(42), 13330-13334. https://doi.org/10.1002/anie.201605753
A Minimal β-Lactone Fragment for Selective β5c or β5i Proteasome Inhibitors
Groll, M., Korotkov, V. S., Huber, E. M., De Meijere, A., & Ludwig, A. (2015). A Minimal β-Lactone Fragment for Selective β5c or β5i Proteasome Inhibitors. Angewandte Chemie International Edition, 54(27), 7810-7814. https://doi.org/10.1002/anie.201502931
Structural, Biochemical, and Computational Studies Reveal the Mechanism of Selective Aldehyde Dehydrogenase 1A1 Inhibition by Cytotoxic Duocarmycin Analogues
Koch, M. F., Harteis, S., Blank, I. D., Pestel, G., Tietze, L. F., Ochsenfeld, C., … Sieber, S. A. (2015). Structural, Biochemical, and Computational Studies Reveal the Mechanism of Selective Aldehyde Dehydrogenase 1A1 Inhibition by Cytotoxic Duocarmycin Analogues. Angewandte Chemie International Edition, 54(46), 13550-13554. https://doi.org/10.1002/anie.201505749
Redox Modulation of PTEN Phosphatase Activity by Hydrogen Peroxide and Bisperoxidovanadium Complexes
Lee, C. U., Hahne, G., Hanske, J., Bange, T., Bier, D., Rademacher, C., … Grossmann, T. N. (2015). Redox Modulation of PTEN Phosphatase Activity by Hydrogen Peroxide and Bisperoxidovanadium Complexes. Angewandte Chemie International Edition, 54(46), 13796-13800. https://doi.org/10.1002/anie.201506338
Identification of a novel polyfluorinated compound as a lead to inhibit the human enzymes aldose reductase and AKR1B10: Structure determination of both ternary complexes and implications for drug design
Cousido-Siah, A., Ruiz, F. X., Mitschler, A., Porté, S., De Lera, Á. R., Martín, M. J., … Podjarny, A. (2014). Identification of a novel polyfluorinated compound as a lead to inhibit the human enzymes aldose reductase and AKR1B10: Structure determination of both ternary complexes and implications for drug design. Acta Crystallographica Section D: Structural Biology, 70(3), 889-903. https://doi.org/10.1107/S1399004713033452
Selective inhibition of the immunoproteasome by ligand-induced crosslinking of the active site
Dubiella, C., Cui, H., Gersch, M., Brouwer, A. J., Sieber, S. A., Krüger, A., … Groll, M. (2014). Selective inhibition of the immunoproteasome by ligand-induced crosslinking of the active site. Angewandte Chemie International Edition, 53(44), 11969-11973. https://doi.org/10.1002/anie.201406964
Discovery and optimization of 7-aminofuro[2,3-c]pyridine inhibitors of TAK1
Hornberger, K. R., Berger, D. M., Crew, A. P., Dong, H., Kleinberg, A., Li, A. H., … Tokar, B. (2013). Discovery and optimization of 7-aminofuro[2,3-c]pyridine inhibitors of TAK1. Bioorganic and Medicinal Chemistry Letters, 23(16), 4517-4522. https://doi.org/10.1016/j.bmcl.2013.06.053
Discovery of 7-aminofuro[2,3-c]pyridine inhibitors of TAK1: Optimization of kinase selectivity and pharmacokinetics
Hornberger, K. R., Chen, X., Crew, A. P., Kleinberg, A., Ma, L., Mulvihill, M. J., … Turton, R. (2013). Discovery of 7-aminofuro[2,3-c]pyridine inhibitors of TAK1: Optimization of kinase selectivity and pharmacokinetics. Bioorganic and Medicinal Chemistry Letters, 23(16), 4511-4516. https://doi.org/10.1016/j.bmcl.2013.06.054
Discovery of potent, selective and orally bioavailable imidazo[1,5-a] pyrazine derived ACK1 inhibitors
Jin, M., Wang, J., Kleinberg, A., Kadalbajoo, M., Siu, K. W., Cooke, A., … Mulvihill, M. J. (2013). Discovery of potent, selective and orally bioavailable imidazo[1,5-a] pyrazine derived ACK1 inhibitors. Bioorganic and Medicinal Chemistry Letters, 23(4), 979-984. https://doi.org/10.1016/j.bmcl.2012.12.042
Structural analysis of phenothiazine derivatives as allosteric inhibitors of the MALT1 paracaspase
Schlauderer, F., Lammens, K., Nagel, D., Vincendeau, M., Eitelhuber, A. C., Verhelst, S. H. L., … Hopfner, K. P. (2013). Structural analysis of phenothiazine derivatives as allosteric inhibitors of the MALT1 paracaspase. Angewandte Chemie International Edition, 52(39), 10384-10387. https://doi.org/10.1002/anie.201304290