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| Title | Extensive targeting of chemical space at the prime side of ketoamide inhibitors of rhomboid proteases by branched substituents empowers their selectivity and potency. |
|---|---|
| Journal, issue, pages | Eur. J. Med. Chem., Vol. 275, Page 116606-116606, Year 2024 |
| Publish date | Jul 4, 2022 (structure data deposition date) |
Authors | Bach, K. / Dohnalek, J. / Skerlova, J. / Kuzmik, J. / Polachova, E. / Stanchev, S. / Majer, P. / Fanfrlik, J. / Pecina, A. / Rezac, J. ...Bach, K. / Dohnalek, J. / Skerlova, J. / Kuzmik, J. / Polachova, E. / Stanchev, S. / Majer, P. / Fanfrlik, J. / Pecina, A. / Rezac, J. / Lepsik, M. / Borshchevskiy, V. / Polovinkin, V. / Strisovsky, K. |
External links | Eur. J. Med. Chem. / PubMed:38901105 |
| Methods | X-ray diffraction |
| Resolution | 2.4 Å |
| Structure data | ![]() PDB-8ab5: |
| Chemicals | ![]() ChemComp-HOH: |
| Source |
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Keywords | HYDROLASE / rhomboid / protease / GlpG / ketoamide / inhibitor |
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