Author

M. Galchenkova

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· 3 Biochemistry· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 5 Research Focus:protein structure prediction· 3 Assay:structural biology· 3 Research Focus:drug response / drug discovery· 2 Research Focus:host-pathogen & immune response· 2 Organism:virus· 2 Assay:protein structure· 1

Frequent Co-Authors

O. Yefanov· 5 shared K. Lorenzen· 4 shared L. Gelisio· 4 shared D. Oberthuer· 3 shared F. TrostiD· 3 shared H. Andaleeb· 3 shared H. Ginn· 3 shared J. Lieske· 3 shared

Activity by Year

2020-2022 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 45 mutual co-author links

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5 shared papersBiophysics

O. Yefanov

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Author profile →

5 papers

Recent·Most cited

JINXED: Just in time crystallization for easy structure determination of biological macromolecules

A. Henkel, M. Galchenkova, J. Maracke, O. Yefanov, J. Hakanpaeae, J. R. Mesters, H. N. Chapman, D. Oberthuer

The paper introduces JINXED, a method that combines protein crystallization and data collection in one step to improve data quality and enable time-resolved experiments.

bioRxiv · Oct 26, 2022Biophysics

SARS-CoV-2 papain-like protease PLpro in complex with natural compounds reveal allosteric sites for antiviral drug design

V. Srinivasan, H. Brognaro, P. R. Prabhu, E. E. de Souza, S. Guenther, P. Y. A. Reinke, T. J. Lane, H. Ginn, H. Han, W. Ewert, J. Sprenger, F. H. M. Koua, S. Falke, N. Werner, H. Andaleeb, , P

This study identifies three natural compounds that inhibit SARS-CoV-2 PLpro by binding to the ISG15/Ub-S2 allosteric site, showing antiviral activity and potential for drug design.

Communications Biology · Aug 11, 2022Peer-reviewedBiochemistry

Structure of the Lysinibacillus sphaericus Tpp49Aa1 pesticidal protein elucidated from natural crystals using MHz-SFX

L. J. Williamson, M. Galchenkova, H. L. Best, R. J. Bean, A. Munke, S. Awel, G. Pena, J. Knoska, R. Schubert, K. Doerner, H.-W. Park, D. K. Bideshi, A. Henkel, V. Kremling, B. Klopprogge, , D. Oberthur

This paper determines the structure of Tpp49Aa1 using MHz-SFX and investigates its interaction with Cry48Aa1, expanding its known target range to include additional mosquito species.

bioRxiv · Jan 14, 2022 · 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