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Macrocyclic carbon-linked pyrazoles as novel inhibitors of MCL-1
Demin, S., Peschiulli, A., Velter, A. I., Vos, A., De Boeck, B., Miller, B., … Philippar, U. (2023). Macrocyclic carbon-linked pyrazoles as novel inhibitors of MCL-1. ACS Medicinal Chemistry Letters, 14(7), 955-961. https://doi.org/10.1021/acsmedchemlett.3c00141
Addressing the osimertinib resistance mutation EGFR-L858R/C797S with reversible aminopyrimidines
Grabe, T., Jeyakumar, K., Niggenaber, J., Schulz, T., Koska, S., Kleinbölting, S., … Rauh, D. (2022). Addressing the osimertinib resistance mutation EGFR-L858R/C797S with reversible aminopyrimidines. ACS Medicinal Chemistry Letters, 14, 591-598. https://doi.org/10.1021/acsmedchemlett.2c00514
Novel non-covalent LSD1 inhibitors endowed with anticancer effects in leukemia and solid tumor cellular models
Menna, M., Fiorentino, F., Marrocco, B., Lucidi, A., Tomassi, S., Cilli, D., … Mai, A. (2022). Novel non-covalent LSD1 inhibitors endowed with anticancer effects in leukemia and solid tumor cellular models. European Journal of Medicinal Chemistry, 237, 114410 (23 pp.). https://doi.org/10.1016/j.ejmech.2022.114410
The first structure of human MTHFD2L and its implications for the development of isoform-selective inhibitors
Scaletti, E. R., Gustafsson Westergren, R., Andersson, Y., Wiita, E., Henriksson, M., Homan, E. J., … Stenmark, P. (2022). The first structure of human MTHFD2L and its implications for the development of isoform-selective inhibitors. ChemMedChem, 17(18), e202200274 (10 pp.). https://doi.org/10.1002/cmdc.202200274
Complex crystal structures of EGFR with third-generation kinase inhibitors and simultaneously bound allosteric ligands
Niggenaber, J., Heyden, L., Grabe, T., Muller, M. P., Lategahn, J., & Rauh, D. (2020). Complex crystal structures of EGFR with third-generation kinase inhibitors and simultaneously bound allosteric ligands. ACS Medicinal Chemistry Letters, 11(12), 2484-2490. https://doi.org/10.1021/acsmedchemlett.0c00472
Lead optimization and biological evaluation of fragment-based cN-II inhibitors
Guillon, R., Rahimova, R., Preeti, P., Egron, D., Rouanet, S., Dumontet, C., … Peyrottes, S. (2019). Lead optimization and biological evaluation of fragment-based cN-II inhibitors. European Journal of Medicinal Chemistry, 168, 28-44. https://doi.org/10.1016/j.ejmech.2019.02.040
Structural insights into interaction mechanisms of alternative piperazine-urea YEATS domain binders in MLLT1
Ni, X., Heidenreich, D., Christott, T., Bennett, J., Moustakim, M., Brennan, P. E., … Chaikuad, A. (2019). Structural insights into interaction mechanisms of alternative piperazine-urea YEATS domain binders in MLLT1. ACS Medicinal Chemistry Letters, 10(12), 1661-1666. https://doi.org/10.1021/acsmedchemlett.9b00460
A novel biphenyl-based chemotype of retinoid X receptor ligands enables subtype and heterodimer preferences
Pollinger, J., Schierle, S., Gellrich, L., Ohrndorf, J., Kaiser, A., Heitel, P., … Merk, D. (2019). A novel biphenyl-based chemotype of retinoid X receptor ligands enables subtype and heterodimer preferences. ACS Medicinal Chemistry Letters, 10(9), 1346-1352. https://doi.org/10.1021/acsmedchemlett.9b00306
Covalent-allosteric inhibitors to achieve Akt isoform-selectivity
Quambusch, L., Landel, I., Depta, L., Weisner, J., Uhlenbrock, N., Müller, M. P., … Rauh, D. (2019). Covalent-allosteric inhibitors to achieve Akt isoform-selectivity. Angewandte Chemie International Edition, 58(52), 18823-18829. https://doi.org/10.1002/anie.201909857
Development of alkyl glycerone phosphate synthase inhibitors: structure-activity relationship and effects on ether lipids and epithelial-mesenchymal transition in cancer cells
Stazi, G., Battistelli, C., Piano, V., Mazzone, R., Marrocco, B., Marchese, S., … Valente, S. (2019). Development of alkyl glycerone phosphate synthase inhibitors: structure-activity relationship and effects on ether lipids and epithelial-mesenchymal transition in cancer cells. European Journal of Medicinal Chemistry, 163, 722-735. https://doi.org/10.1016/j.ejmech.2018.11.050
Immune-modulating enzyme indoleamine 2,3-dioxygenase is effectively inhibited by targeting its apo-form
Nelp, M. T., Kates, P. A., Hunt, J. T., Newitt, J. A., Balog, A., Maley, D., … Groves, J. T. (2018). Immune-modulating enzyme indoleamine 2,3-dioxygenase is effectively inhibited by targeting its apo-form. Proceedings of the National Academy of Sciences of the United States of America PNAS, 115(13), 3249-3254. https://doi.org/10.1073/pnas.1719190115
Binding motifs in the CBP bromodomain: an analysis of 20 crystal structures of complexes with small molecules
Zhu, J., Dong, J., Batiste, L., Unzue, A., Dolbois, A., Pascanu, V., … Caflisch, A. (2018). Binding motifs in the CBP bromodomain: an analysis of 20 crystal structures of complexes with small molecules. ACS Medicinal Chemistry Letters, 9(9), 929-934. https://doi.org/10.1021/acsmedchemlett.8b00286
Optimized 4,5-diarylimidazoles as potent/selective inhibitors of protein kinase CK1δ and their structural relation to P38<em>α</em> MAPK
Halekotte, J., Witt, L., Ianes, C., Krüger, M., Bührmann, M., Rauh, D., … Peifer, C. (2017). Optimized 4,5-diarylimidazoles as potent/selective inhibitors of protein kinase CK1δ and their structural relation to P38α MAPK. Molecules, 22(4), 522 (37 pp.). https://doi.org/10.3390/molecules22040522
Myosin-1E interacts with FAK proline-rich region 1 to induce fibronectin-type matrix
Heim, J. B., Squirewell, E. J., Neu, A., Zocher, G., Sominidi-Damodaran, S., Wyles, S. P., … Meves, A. (2017). Myosin-1E interacts with FAK proline-rich region 1 to induce fibronectin-type matrix. Proceedings of the National Academy of Sciences of the United States of America PNAS, 114(15), 3933-3938. https://doi.org/10.1073/pnas.1614894114
Catalytic competence, structure and stability of the cancer-associated R139W variant of the human NAD(P)H:quinone oxidoreductase 1 (NQO1)
Lienhart, W. D., Strandback, E., Gudipati, V., Koch, K., Binter, A., Uhl, M. K., … Macheroux, P. (2017). Catalytic competence, structure and stability of the cancer-associated R139W variant of the human NAD(P)H:quinone oxidoreductase 1 (NQO1). FEBS Journal, 284(8), 1233-1245. https://doi.org/10.1111/febs.14051
Structural basis for the inhibition of AKR1B10 by the C3 brominated TTNPB derivative UVI2008
Ruiz, F. X., Crespo, I., Álvarez, S., Porté, S., Giménez-Dejoz, J., Cousido-Siah, A., … Farrés, J. (2017). Structural basis for the inhibition of AKR1B10 by the C3 brominated TTNPB derivative UVI2008. Chemico-Biological Interactions, 276, 174-181. https://doi.org/10.1016/j.cbi.2017.01.026
Insight into the Inhibition of drug-resistant mutants of the receptor tyrosine kinase EGFR
Engel, J., Becker, C., Lategahn, J., Keul, M., Ketzer, J., Mühlenberg, T., … Rauh, D. (2016). Insight into the Inhibition of drug-resistant mutants of the receptor tyrosine kinase EGFR. Angewandte Chemie International Edition, 55(36), 10909-10912. https://doi.org/10.1002/anie.201605011
α-keto phenylamides as P1&#039;-extended proteasome inhibitors
Voss, C., Scholz, C., Knorr, S., Beck, P., Stein, M. L., Zall, A., … Schmidt, B. (2014). α-keto phenylamides as P1'-extended proteasome inhibitors. ChemMedChem, 9(11), 2557-2564. https://doi.org/10.1002/cmdc.201402244
Discovery of potent and selective spiroindolinone MDM2 inhibitor, RO8994, for cancer therapy
Zhang, Z., Ding, Q., Liu, J. J., Zhang, J., Jiang, N., Chu, X. J., … Graves, B. (2014). Discovery of potent and selective spiroindolinone MDM2 inhibitor, RO8994, for cancer therapy. Bioorganic and Medicinal Chemistry, 22(15), 4001-4009. https://doi.org/10.1016/j.bmc.2014.05.072
Discovery and optimization of 7-aminofuro[2,3-<em>c</em>]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