Author

N. Schneberger

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 Biophysics· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:protein folding & dynamics· 3 Organism:bacteria (other)· 1 Research Focus:benchmarking· 1 Research Focus:cell signaling & trafficking· 1 Assay:cryo-EM· 1 Approach:deep learning· 1 Assay:protein structure· 1

Frequent Co-Authors

G. Hagelueken· 4 shared M. F. Peter· 3 shared M. Geyer· 3 shared C. Rouillon· 2 shared G. H. Thomas· 2 shared A. Durand· 1 shared C. Gebhardt· 1 shared C. Ziegler· 1 shared

Activity by Year

2020-2024 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 31 mutual co-author links

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4 shared papersBiochemistry

G. Hagelueken

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4 papers

Recent·Most cited

The SAVED domain of the type III CRISPR protease CalpL is a ring nuclease

S. C. Binder, N. Schneberger, M. Engeser, M. Geyer, C. Rouillon, G. Hagelueken

This study identifies the SAVED domain of CalpL as a ring nuclease that cleaves cA4, revealing its role in regulating the CRISPR defense system.

bioRxiv · May 8, 2024Biochemistry

SAVED by a toxin: Structure and function of the CRISPR Lon protease.

C. Rouillon, N. Schneberger, H. Chi, M. F. Peter, M. Geyer, W. Boenigk, R. Seifert, M. F. White, G. Hagelueken

The paper reports the crystal structure of CRISPR-Lon, a protein that activates by binding cA4 and cleaves CRISPR-T to release a nuclease-like fragment.

bioRxiv · Dec 6, 2021Biochemistry

The structure of HiSiaQM defines the architecture of tripartite ATP-independent periplasmic (TRAP) transporters

M. F. Peter, P. Depping, N. Schneberger, E. Severi, K. Gatterdam, S. Tindall, A. Durand, V. Heinz, P. A. Koenig, M. Geyer, C. Ziegler, G. H. Thomas, G. Hagelueken

This paper presents the first cryo-EM structure of TRAP transporter membrane domains and identifies structural features that enable monomeric elevator architecture.

bioRxiv · Dec 3, 2021Biochemistry

Triggering closure of a sialic acid TRAP transporter substrate binding protein through binding of natural or artificial substrates

M. F. Peter, C. Gebhardt, J. Glaenzer, N. Schneberger, M. de Boer, G. H. Thomas, T. Cordes, G. Hagelueken

This study investigates the conformational changes in the sialic acid TRAP transporter SBP VcSiaP upon substrate binding, showing that substrate induces closure and provides structural insights for inhibitor development.

bioRxiv · Dec 2, 2020Biophysics