Author

I. Liebscher

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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Cell Biology· 3

Signature Assays, Organisms & Methods

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Research Focus:cell signaling & trafficking· 3 Approach:experimental assay· 3 Organism:human· 3 Assay:proteomics· 3

Frequent Co-Authors

D. G. Placantonakis· 3 shared G. Stephan· 3 shared J. D. Frenster· 3 shared B. Kieslich· 2 shared C. Wilde· 2 shared D. Bready· 2 shared J. Wilcox· 2 shared N. Ravn-Boess· 2 shared

Activity by Year

2020-2022 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 44 mutual co-author links

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3 shared papersCell Biology

D. G. Placantonakis

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3 papers

Recent·Most cited

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

Activation of the adhesion GPCR GPR133 (ADGRD1) by antibodies targeting the N-terminus

G. Stephan, J. D. Frenster, I. Liebscher, D. G. Placantonakis

This study shows that antibodies targeting the N-terminus of GPR133 promote receptor activation by inducing NTF-CTF dissociation, increasing cAMP levels in GBM cells.

bioRxiv · Sep 13, 2021 · PreprintCell Biology

Dissociation of the intramolecularly cleaved N- and C-terminal fragments of the adhesion G protein-coupled receptor GPR133 (ADGRD1) increases canonical signaling

J. D. Frenster, G. Stephan, N. Ravn-Boess, D. Bready, J. Wilcox, B. Kieslich, C. Wilde, N. Sträter, G. R. Wiggin, I. Liebscher, T. Schöneberg, D. G. Placantonakis

This study shows that cleavage of GPR133 into NTF and CTF fragments at the plasma membrane enhances canonical signaling in GBM and HEK293T cells compared to an uncleavable mutant.

bioRxiv · Dec 8, 2020 · PreprintCell Biology