Jan Konvalinka
Affiliations: | Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences |
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| Novotný P, Humpolíčková J, Nováková V, et al. (2024) The zymogenic form of SARS-CoV-2 main protease: A discrete target for drug discovery. The Journal of Biological Chemistry. 108079 |
| Kryštůfek R, Šácha P, Starková J, et al. (2021) Re-emerging Aspartic Protease Targets: Examining Major Aspartyl Peptidase 1 as a Target for Antifungal Drug Discovery. Journal of Medicinal Chemistry. 64: 6706-6719 |
| Majerová T, Novotný P, Krýsová E, et al. (2019) Exploiting the unique features of Zika and Dengue proteases for inhibitor design. Biochimie. 166: 132-141 |
| Vorlova B, Knedlik T, Tykvart J, et al. (2019) GCPII and its close homolog GCPIII: from a neuropeptidase to a cancer marker and beyond. Frontiers in Bioscience (Landmark Edition). 24: 648-687 |
| Humpolíčková J, Weber J, Starková J, et al. (2018) Inhibition of the precursor and mature forms of HIV-1 protease as a tool for drug evaluation. Scientific Reports. 8: 10438 |
| Tretyachenko V, Vymětal J, Bednárová L, et al. (2017) Random protein sequences can form defined secondary structures and are well-tolerated in vivo. Scientific Reports. 7: 15449 |
| Knedlík T, Vorlová B, Navrátil V, et al. (2017) Mouse glutamate carboxypeptidase II (GCPII) has a similar enzyme activity and inhibition profile but a different tissue distribution to human GCPII. Febs Open Bio. 7: 1362-1378 |
| Hanne J, Göttfert F, Schimer J, et al. (2016) Stimulated Emission Depletion Nanoscopy Reveals Time-Course of Human Immunodeficiency Virus Proteolytic Maturation. Acs Nano |
| Navrátil M, Tykvart J, Schimer J, et al. (2016) Comparison of human glutamate carboxypeptidases II and III reveals their divergent substrate specificities. The Febs Journal |
| Tykvart J, Schimer J, Jančařík A, et al. (2015) Design of highly potent urea-based, exosite-binding inhibitors selective for glutamate carboxypeptidase II. Journal of Medicinal Chemistry. 58: 4357-63 |