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1.
Falke, S.* et al.: Structural elucidation and antiviral activity of covalent cathepsin L inhibitors. J. Med. Chem. 67, 7048-7067 (2024)
2.
Grygier, P.* et al.: Silmitasertib (CX-4945), a clinically used CK2-kinase inhibitor with additional effects on GSK3β and DYRK1A kinases: A structural perspective. J. Med. Chem. 66, 4009-4024 (2023)
3.
Kitel, R.* et al.: Discovery of inhibitory fragments that selectively target spire2-FMN2 interaction. J. Med. Chem. 66, 15715-15727 (2023)
4.
Narayanan, D.* et al.: Development of noncovalent small-molecule Keap1-Nrf2 inhibitors by fragment-based drug discovery. J. Med. Chem. 65, 14481-14526 (2022)
5.
Hofmeister, A.* et al.: Syntheses of morpholine-based nucleotide analogs for hepatic siRNA targeting and stabilization. J. Med. Chem. 64, 6838–6855 (2021)
6.
Pallesen, J.S.* et al.: Deconstructing noncovalent kelch-like ECH-associated protein 1 (Keap1) inhibitors into fragments to reconstruct new potent compounds. J. Med. Chem. 64, 4623-4661 (2021)
7.
Dawidowski, M. et al.: Structure-activity relationship in pyrazolo[4,3-c]pyridines, first inhibitors of PEX14-PEX5 Protein-Protein Interaction (PPI) with trypanocidal activity. J. Med. Chem. 63, 847-879 (2020)
8.
Hanke, S.* et al.: Structural studies on the inhibitory binding mode of aromatic coumarinic esters to human kallikrein-related peptidase 7. J. Med. Chem. 63, 5723-5733 (2020)
9.
Solbak, S.M.* et al.: Developing inhibitors of the p47phox-p22phox protein-protein interaction by fragment-based drug discovery. J. Med. Chem. 63, 1156-1177 (2020)
10.
van de Plassche, M.A.T.* et al.: Use of non-natural amino acids for the design and synthesis of a selective, cell-permeable MALT1 activity-based probe. J. Med. Chem. 63, 3996-4004 (2020)
11.
Li, C.* et al.: Novel allosteric activators for ferroptosis regulator glutathione peroxidase 4. J. Med. Chem. 62, 266-275 (2019)
12.
Guarino, C.* et al.: Exploiting the S4-S5 Specificity of Human Neutrophil Proteinase 3 to Improve the Potency of Peptidyl Di(chlorophenyl)-phosphonate Ester Inhibitors: A Kinetic and Molecular Modeling Analysis. J. Med. Chem. 61, 1858-1870 (2018)
13.
Kyriakou, E. et al.: Celastrol promotes weight loss in diet-induced obesity by inhibiting the protein tyrosine phosphatases PTP1B and TCPTP in the hypothalamus. J. Med. Chem. 61, 11144-11157 (2018)
14.
Bertoletti, N.* et al.: New insights into human 17β-hydroxysteroid dehydrogenase type 14: First crystal structures in complex with a steroidal ligand and with a potent non-steroidal inhibitor. J. Med. Chem. 59, 6961-6967 (2016)
15.
Braun, F.* et al.: First structure-activity relationship of 17β-hydroxysteroid dehydrogenase type 14 nonsteroidal inhibitors and crystal structures in complex with the enzyme. J. Med. Chem. 59, 10719-10737 (2016)
16.
Jagtap, P.K. et al.: Rational design of cyclic peptide inhibitors of U2AF homology motif (UHM) domains to modulate pre-mRNA splicing. J. Med. Chem. 59, 10190-10197 (2016)
17.
Gilsbach, B.K.* et al.: Structural characterization of LRRK2 inhibitors. J. Med. Chem. 58, 3751-3756 (2015)
18.
Marchais-Oberwinkler, S.* et al.: Structural optimization of 2,5-tiophene amides as highly potent and selective 17β-hydroxysteroid dehydrogenase type 2 inhibitors for the treatment of osteoporosis. J. Med. Chem. 56, 167-181 (2013)
19.
Wetzel, M.* et al.: Introduction of an electron withdrawing group on the hydroxyphenylnaphthol scaffold improves the potency of 17β-hydroxysteroid dehydrogenase type 2 (17β-HSD2) inhibitors. J. Med. Chem. 54, 7547-7557 (2011)
20.
Garg, D. et al.: Novel approaches for targeting thymidylate synthase to overcome the resistance and toxicity of anticancer drugs. J. Med. Chem. 53, 6539-6549 (2010)
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