Author

T. Schoneberg

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· 2 Cell Biology· 1 Physiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:cell signaling & trafficking· 3 Organism:human· 3 Research Focus:protein folding & dynamics· 2 Assay:structural biology· 2 Approach:biophysical modeling· 1 Organism:C. elegans· 1 Research Focus:cell type annotation· 1

Frequent Co-Authors

B. Kieslich· 2 shared N. Strater· 2 shared A. B. Knierim· 1 shared A. Ricken· 1 shared C. Wilde· 1 shared D. Bready· 1 shared D. Fenyö· 1 shared D. G. Placantonakis· 1 shared

Activity by Year

2022-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 15 mutual co-author links

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2 shared papersBiochemistry

B. Kieslich

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

Structural basis of GAIN domain autoproteolysis and cleavage-resistance in the adhesion G-protein coupled receptors

F. Pohl, F. Seufert, Y. K. Chung, D. Volke, R. Hoffmann, T. Schoneberg, T. Langenhan, P. W. Hildebrand, N. Strater

This study identifies structural determinants that confer resistance to autoproteolysis in adhesion GPCRs despite the presence of a canonical GPS motif.

bioRxiv · Mar 12, 2023Biochemistry

The N terminus-only (trans) function of the Adhesion GPCR Latrophilin-1 controls multiple processes in reproduction of C. elegans

D. Matus, V. E. Gross, F. Fiedler, W. B. Post, A. B. Knierim, J. L. Schon, T. Schoneberg, S. Promel

This study identifies three 7TM-independent functions of the aGPCR Latrophilin-1 in C. elegans reproduction, mediated through N terminus-only signaling from adjacent somatic cells.

bioRxiv · Feb 18, 2023Physiology

The dimerized pentraxin-like domain of the adhesion G protein-coupled receptor 112 (ADGRG4) suggests function in sensing mechanical forces

B. Kieslich, J. Brendler, A. Ricken, T. Schoneberg, N. Strater

The paper determines the structure of the PTX-like domain of ADGRG4 and shows it forms a Ca2+-independent homodimer, suggesting a role in sensing mechanical forces in intestinal cells.

bioRxiv · Sep 20, 2022Biochemistry

PTK7 is a positive allosteric modulator of GPR133 (ADGRD1) signaling in GBM

J. D. Frenster, H. Erdjument-Bromage, W. Liu, G. Stephan, N. Ravn-Boess, D. Bready, J. Wilcox, B. Kieslich, M. Jankovic, C. Wilde, S. Horn, N. Straeter, I. Liebscher, T. Schoneberg, D. Fenyö, , D. G. Placantonakis

This study identifies PTK7 as a positive allosteric modulator of GPR133 signaling in glioblastoma, showing that their interaction enhances receptor activation and is relevant to tumor pathogenesis.

bioRxiv · Jun 15, 2022 · PreprintCell Biology