Author

S. Banchenko

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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Biochemistry· 3

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:host-pathogen & immune response· 2 Organism:non-human primate· 1 Assay:proteomics· 1 Organism:rat· 1 Assay:structural biology· 1

Frequent Co-Authors

A. Graziadei· 2 shared C. Gotthold· 2 shared C. M. T. Spahn· 2 shared D. Schwefel· 2 shared J. Rappsilber· 2 shared T. Mielke· 2 shared A. Malyshkina· 1 shared B. Sitek· 1 shared

Activity by Year

2020-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 36 mutual co-author links

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2 shared papersBiochemistry

A. Graziadei

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Author profile →

3 papers

Recent·Most cited

Structure and mechanism of a novel cytomegaloviral DCAF mediating interferon antagonism

V. T. K. Le-Trilling, S. Banchenko, D. Paydar, P. M. Leipe, L. Binting, S. Lauer, A. Graziadei, C. Gotthold, J. Burger, T. Bracht, B. Sitek, R. J. Lebbink, A. Malyshkina, T. Mielke, J. Rappsilber, , D. Schwefel

This study identifies E27 as a viral protein that targets STAT2 for degradation via CRL4 ubiquitin ligases, revealing its structural mechanism of interferon antagonism.

bioRxiv · May 5, 2022Biochemistry

Structural insights into Cullin4-RING ubiquitin ligase remodelling by Vpr from simian immunodeficiency viruses

S. Banchenko, F. Krupp, C. Gotthold, J. Buerger, A. Graziadei, F. O' Reilly, L. Sinn, O. Ruda, J. Rappsilber, C. M. T. Spahn, T. Mielke, I. A. Taylor, D. Schwefel

This paper investigates how SIVmus Vpr interacts with CRL4DCAF1 to ubiquitylate SAMHD1, revealing structural and mechanistic insights into viral counteraction of host restriction factors.

bioRxiv · Dec 31, 2020Biochemistry

The helix bundle domain of primase RepB' is required for dinucleotide formation and extension

S. Banchenko, C. Weise, E. Lanka, W. Saenger, S. Geibel

This study identifies the role of the helix bundle domain in primase RepB's ability to synthesize and extend DNA primers during replication.

bioRxiv · Feb 20, 2020Biochemistry