Author

S. Schenck

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 Organism:bacteria (other)· 2 Research Focus:protein structure prediction· 2 Assay:structural biology· 2 Assay:cryo-EM· 1 Research Focus:host-pathogen & immune response· 1 Organism:human· 1

Frequent Co-Authors

J. D. Brunner· 3 shared A. Moroni· 1 shared D. Bucher· 1 shared D. Ni· 1 shared G. Thiel· 1 shared H. Stahlberg· 1 shared I. Zimmermann· 1 shared J. Steyaert· 1 shared

Activity by Year

2018-2024 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 25 mutual co-author links

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3 shared papersBiochemistry

J. D. Brunner

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3 papers

Recent·Most cited

Structures of native SV2A reveal the binding mode for tetanus neurotoxin and anti-epileptic racetams

S. Schenck, T. Laeremans, J. Steyaert, J. D. Brunner

This study determines the structures of native SV2A, revealing its binding modes for tetanus neurotoxin and anti-epileptic drugs, and provides insights into toxin-receptor interactions and drug specificity.

bioRxiv · May 7, 2024Biochemistry

Insight into Lipopolysaccharide Translocation by Cryo-EM structures of a LptDE Transporter in Complex with Pro-Macrobodies

M. Botte, D. Ni, S. Schenck, I. Zimmermann, M. Chami, N. Bocquet, P. Egloff, D. Bucher, M. Trabuco, R. K. Y. Cheng, J. D. Brunner, M. A. Seeger, H. Stahlberg, M. Hennig

The paper uses cryo-EM to determine structures of the LptDE transporter complex with Pro-Macrobodies, revealing partially and fully opened states of the transporter during LPS translocation.

bioRxiv · Mar 23, 2021 · PreprintBiochemistry

Structural basis for ion selectivity in TMEM175 K+ channels

J. D. Brunner, R. P. Jakob, T. Schulze, Y. Neldner, A. Moroni, G. Thiel, T. Maier, S. Schenck

This study determines the X-ray structure of a bacterial TMEM175 K+ channel, revealing a unique cation-selective mechanism involving a conserved threonine residue and conformational changes.

bioRxiv · Dec 4, 2018Biochemistry