Author

C. Ehrt

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biophysics· 2 Biochemistry· 1

Signature Assays, Organisms & Methods

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Research Focus:drug response / drug discovery· 3 Approach:experimental assay· 3 Assay:structural biology· 2 Organism:virus· 2 Research Focus:host-pathogen & immune response· 1 Research Focus:protein structure prediction· 1

Frequent Co-Authors

D. Oberthuer· 3 shared S. Falke· 3 shared A. Peck· 2 shared A. Tolstikova· 2 shared B. Norton-Baker· 2 shared B. Seychell· 2 shared C. Li· 2 shared F. KouaiD· 2 shared

Activity by Year

2020-2024 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 45 mutual co-author links

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3 shared papersBiophysics

D. Oberthuer

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

SARS-CoV-2 methyltransferase nsp10-16 in complex with natural and drug-like purine analogs for guiding structure-based drug discovery

V. Kremling, S. Falke, Y. Fernandez-Garcia, C. Ehrt, A. Kiene, B. Klopprogge, T. E. S. Scheer, F. Barthels, P. Middendorf, S. Kuehn, S. Guenther, M. Rarey, H. N. Chapman, D. Oberthuer, J. Sprenger

The paper identifies ligands binding to the SARS-CoV-2 nsp10-16 complex using X-ray crystallography and reports their structures, providing insights for drug discovery.

bioRxiv · Mar 13, 2024 · PreprintBiochemistry

Inhibition of SARS-CoV-2 main protease by allosteric drug-binding

S. Guenther, P. Y. A. Reinke, Y. Fernandez-Garcia, J. Lieske, T. J. Lane, H. Ginn, F. Koua, C. Ehrt, W. Ewert, D. Oberthuer, O. Yefanov, S. Meier, K. Lorenzen, B. Krichel, J. Kopicki, , Schwi

The paper identifies 37 compounds binding to SARS-CoV-2 main protease through X-ray crystallography, with five non-peptidic compounds showing antiviral activity in cell-based assays.

bioRxiv · Nov 12, 2020Biophysics

Catalytic cleavage of HEAT and subsequent covalent binding of the tetralone moiety by the SARS-CoV-2 main protease

S. Günther, P. Y. A. Reinke, D. Oberthuer, O. Yefanov, H. Ginn, S. Meier, T. J. Lane, K. Lorenzen, L. Gelisio, W. Brehm, I. Dunkel, M. Domaracky, S. Saouane, J. Lieske, C. Ehrt, , G

The paper presents the crystal structure of SARS-CoV-2 main protease covalently bound to a metabolite of HEAT, revealing a pro-drug mechanism and potential for non-peptidic inhibitors.

bioRxiv · May 2, 2020 · PreprintBiophysics