Publications

Mechanism and spectrum of inhibition of a 4′-cyano modified nucleotide analog against diverse RNA polymerases of prototypic respiratory RNA viruses

Gordon, C. J., Walker, S. M., Tchesnokov, E. P., Kocincova, D., Pitts, J., Siegel, D. S., Perry, J. K., Feng, J. Y., Bilello, J. P., Götte, M. (2024). Journal of Biological Chemistry. https://doi.org/10.1016/j.jbc.2024.107514

Structures, functions and adaptations of the human LINE-1 ORF2 protein

Baldwin, E. T., van Eeuwen, T., Hoyos, D., Zalevsky, A., Tchesnokov, E. P., Sánchez, R., Miller, B. D., Di Stefano, L. H., Ruiz, F. X., Hancock, M., Işik, E., Mendez-Dorantes, C., Walpole, T., Nichols, C., Wan, P., Riento, K., Halls-Kass, R., Augustin, M., Lammens, A., Jestel, A., Upla, P., Xibinaku, K., Congreve, S., Hennink, M., Rogala, K. B., Schneider, A. M., Fairman, J. E., Christensen, S. M., Desrosiers, Brian., Bisacchi, G. S., Saunders, O.L, Hafeez, N., Miao, W., Kapeller, R., Zaller, D. M., Sali, A., Weichenrieder, O., Burns, K. H., Götte, M., Rout, M. P., Arnold, E., Greenbaum, G. D., Romero, D. L. LaCava J., & Taylor, M. S. (2024). Nature, 626(7997), 194–206. https://doi.org/10.1038/s41586-023-06947-z

Structural basis for substrate selection by the SARS-CoV-2 replicase

Malone, B. F., Perry, J. K., Olinares, P. D. B., Lee, H. W., Chen, J., Appleby, T. C., Feng, J. Y., Bilello, J. P., Ng, H., Sotiris, J., Ebrahim, M., Chua, E. Y. D., Mendez, J. H., Eng, E. T., Landick, R., Götte, M., Chait, B. T., Campbell, E. A., & Darst, S. A. (2023). Nature, 614(7949), 781–787. https://doi.org/10.1038/s41586-022-05664-3

Human endogenous retrovirus-K (HERV-K) reverse transcriptase (RT) structure and biochemistry reveals remarkable similarities to HIV-1 RT and opportunities for HERV-K-specific inhibition

Baldwin, E. T., Götte, M., Tchesnokov, E. P., Arnold, E., Hagel, M., Nichols, C., Dossang, P., Lamers, M., Wan, P., Steinbacher, S., & Romero, D. L. (2022). Proceedings of the National Academy of Sciences, 119(27), e2200260119. https://doi.org/10.1073/pnas.2200260119

Mutations in the SARS-CoV-2 RNA-dependent RNA polymerase confer resistance to remdesivir by distinct mechanisms

Stevens, L. J., Pruijssers, A. J., Lee, H. W., Gordon, C. J., Tchesnokov, E. P., Gribble, J., George, A. S., Hughes, T. M., Lu, X., Li, J., Perry, J. K., Porter, D. P., Cihlar, T., Sheahan, T. P., Baric, R. S., Götte, M., & Denison, M. R. (n.d.). Science Translational Medicine, 14(656), eabo0718. https://doi.org/10.1126/scitranslmed.abo0718

Efficient incorporation and template-dependent polymerase inhibition are major determinants for the broad-spectrum antiviral activity of remdesivir

Gordon, C. J., Lee, H. W., Tchesnokov, E. P., Perry, J. K., Feng, J. Y., Bilello, J. P., Porter, D. P., & Götte, M. (2022). Journal of Biological Chemistry, 298(2), 101529. https://doi.org/10.1016/j.jbc.2021.101529

Knowledge Gaps in the Understanding of Antimicrobial Resistance in Canada

McCubbin, K. D., Anholt, R. M., de Jong, E., Ida, J. A., Nóbrega, D. B., Kastelic, J. P., Conly, J. M., Götte, M., McAllister, T. A., Orsel, K., Lewis, I., Jackson, L., Plastow, G., Wieden, H.-J., McCoy, K., Leslie, M., Robinson, J. L., Hardcastle, L., Hollis, A., Ashbolt, N. J., Checkley, S., Tyrrell, G. J., Buret, A. G., Rennert-May, E., Goddard, E., Otto, S. J. G., Barkema, H. W. (2021). Frontiers in Public Health, 9, 726484. https://doi.org/10.3389/fpubh.2021.726484

Remdesivir for the treatment of Covid-19: The value of biochemical studies.

Götte, M. (2021). Current Opinion in Virology, 49, 81–85. https://doi.org/10.1016/j.coviro.2021.04.014

Report of the National Institutes of Health SARS-CoV-2 Antiviral Therapeutics Summit

Hall, M. D., Anderson, J. M., Anderson, A., Baker, D., Bradner, J., Brimacombe, K. R., Campbell, E. A., Corbett, K. S., Carter, K., Cherry, S., Chiang, L., Cihlar, T., de Wit, E., Denison, M., Disney, M., Fletcher, C. V., Ford-Scheimer, S. L., Götte, M., Grossman, A. C., Hayden, F. G., Hazuda, D. J., Lanteri, C. A., Marston, H., Mesecar, A. D., Moore, S., Nwankwo, J. O., O'Rear, J., Painter, G., Singh Saikatendu, K., Schiffer, C. A., Sheahan, T. P., Shi, P-Y., Smyth, H. D., Sofia, M. J., Weetall, M., Weller, S. K., Whitley, R., Fauci, A. S., Austin, C. P., Collins, F. S., Conley, A. J., Davis, M. I. (2021). The Journal of Infectious Diseases, 224(Supplement_1), S1–S21. https://doi.org/10.1093/infdis/jiab305

Molnupiravir promotes SARS-CoV-2 mutagenesis via the RNA template

Gordon, C. J., Tchesnokov, E. P., Schinazi, R. F., & Götte, M. (2021). Journal of Biological Chemistry, 297(1). https://doi.org/10.1016/j.jbc.2021.100770

The active form of the influenza cap-snatching endonuclease inhibitor baloxavir marboxil is a tight binding inhibitor

Todd, B., Tchesnokov, E. P., & Götte, M. (2021). Journal of Biological Chemistry, 296. https://doi.org/10.1016/j.jbc.2021.100486

Template-dependent inhibition of coronavirus RNA-dependent RNA polymerase by remdesivir reveals a second mechanism of action

Tchesnokov, E. P., Gordon, C. J., Woolner, E., Kocinkova, D., Perry, J. K., Feng, J. Y., Porter, D. P., & Götte, M. (2020). Journal of Biological Chemistry, 295(47), 16156–16165. https://doi.org/10.1074/jbc.AC120.015720

Remdesivir targets a structurally analogous region of the Ebola virus and SARS-CoV-2 polymerases

Lo, M. K., Albariño, C. G., Perry, J. K., Chang, S., Tchesnokov, E. P., Guerrero, L., Chakrabarti, A., Shrivastava-Ranjan, P., Chatterjee, P., McMullan, L. K., Martin, R., Jordan, R., Götte, M., Montgomery, J. M., Nichol, S. T., Flint, M., Porter, D., & Spiropoulou, C. F. (2020). Remdesivir targets a structurally analogous region of the Ebola virus and SARS-CoV-2 polymerases. Proceedings of the National Academy of Sciences, 117(43), 26946–26954. https://doi.org/10.1073/pnas.2012294117

Independent inhibition of the polymerase and deubiquitinase activities of the Crimean-Congo Hemorrhagic Fever Virus full-length L-protein

Tchesnokov, E. P., Bailey-Elkin, B. A., Mark, B. L., & Götte, M. (2020). PLOS Neglected Tropical Diseases, 14(6), e0008283. https://doi.org/10.1371/journal.pntd.0008283

Remdesivir is a direct-acting antiviral that inhibits RNA-dependent RNA polymerase from severe acute respiratory syndrome coronavirus 2 with high potency

Gordon, C. J., Tchesnokov, E. P., Woolner, E., Perry, J. K., Feng, J. Y., Porter, D. P., & Götte, M. (2020). Journal of Biological Chemistry, 295(20), 6785–6797. https://doi.org/10.1074/jbc.RA120.013679

The antiviral compound remdesivir potently inhibits RNA-dependent RNA polymerase from Middle East respiratory syndrome coronavirus

Gordon, C. J., Tchesnokov, E. P., Feng, J. Y., Porter, D. P., & Götte, M. (2020). Journal of Biological Chemistry, 295(15), 4773–4779. https://doi.org/10.1074/jbc.AC120.013056

NRTIs tenofovir, TAF, TDF, and FTC are inactive against SARS-CoV-2

Feng, J. Y., Bilello, J. P., Babusis, D., Gordon, C. J., Tchesnokov, E. P., Perry, J. K., Du Pont, V., Vijjapurapu, A., Zhao, X., Götte, M., & Cihlar, T. (2021, October 30). Gilead Sciences Inc. https://www.hivandmore.de/kongresse/eacs2021/downloads/Feng_NRTI-TAF-TDF-FTC-and-SARS-CoV-2_EACS-2021_PE1-2.pdf

 Hepatitis C Virus Helicase Binding Activity Monitored through Site-Specific Labeling Using an Expanded Genetic Code

Ablenas, C. J., Gidi, Y., Powdrill, M. H., Ahmed, N., Shaw, T. A., Mesko, M., Götte, M., Cosa, G., & Pezacki, J. P. (2019). ACS Infectious Diseases, 5(12), 2118–2126. https://doi.org/10.1021/acsinfecdis.9b00220

Mechanism of Inhibition of Ebola Virus RNA-Dependent RNA Polymerase by Remdesivir

Tchesnokov, E. P., Feng, J. Y., Porter, D. P., & Götte, M. (2019). Mechanism of Inhibition of Ebola Virus RNA-Dependent RNA Polymerase by Remdesivir. Viruses, 11(4). https://doi.org/10.3390/v11040326

Pharmacophore requirements for HIV-1 reverse transcriptase inhibitors that selectively “Freeze” the pre-translocated complex during the polymerization catalytic cycle.

Lacbay, C. M., Menni, M., Bernatchez, J. A., Götte, M., & Tsantrizos, Y. S. (2018). Bioorganic & Medicinal Chemistry, 26(8), 1713–1726. https://doi.org/10.1016/j.bmc.2018.02.017

Recombinant RNA-Dependent RNA Polymerase Complex of Ebola Virus

Tchesnokov, E. P., Raeisimakiani, P., Ngure, M., Marchant, D., & Götte, M. (2018). Scientific Reports, 8(1), 3970. https://doi.org/10.1038/s41598-018-22328-3