Author

T. Pauly

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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Biophysics· 2 Biochemistry· 1

Signature Assays, Organisms & Methods

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Research Focus:cell type annotation· 2 Organism:human· 2 Approach:biophysical modeling· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:chromatin & epigenetic regulation· 1 Research Focus:drug response / drug discovery· 1 Approach:experimental assay· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

L. Nagel-Steger· 3 shared A. Boquoi· 1 shared A. Cabrera-Orefice· 1 shared A. K. Buell· 1 shared A. Macha· 1 shared A. Viegas· 1 shared B. Frieg· 1 shared C. Toelzer· 1 shared

Activity by Year

2021-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 18 mutual co-author links

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3 shared papersBiophysics

L. Nagel-Steger

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Author profile →

3 papers

Recent·Most cited

Pentameric assembly of glycine receptor intracellular domains provides insights into gephyrin clustering

A. Macha, N. Gruenewald, N. Havarushka, N. Burdina, C. Toelzer, Y. Merkler, A. Cabrera-Orefice, T. Pauly, U. Brandt, L. Nagel-Steger, K. Niefind, G. Schwarz

The paper studies glycine receptor intracellular domains using a pentameric scaffold, revealing structural flexibility and a mechanism for gephyrin clustering at inhibitory synapses.

bioRxiv · Nov 10, 2022 · PreprintBiochemistry

Biophysical and pharmacokinetic characterization of a small-molecule inhibitor of RUNX1/ETO tetramerization with anti-leukemic effects

M. Gopalswamy, T. Kroeger, D. Bickel, B. Frieg, S. Akter, S. Schott-Verdugo, A. Viegas, T. Pauly, M. Mayer, J. Przibilla, J. Reiners, L. Nagel-Steger, S. H. J. Smits, G. Groth, M. Etzkorn, H. Gohlke

This paper characterizes a small-molecule inhibitor of RUNX1/ETO tetramerization, showing it disrupts tetramer stability and has favorable pharmacokinetic properties for potential anti-leukemic therapy.

bioRxiv · Dec 22, 2021Biophysics

Universal amyloidogenicity of patient-derivedimmunoglobulin light chains

R. Sternke-Hoffmann, T. Pauly, R. K. Norrild, J. Hansen, M. Dupre, F. Tucholski, M. Duchateau, M. Rey, S. Metzger, A. Boquoi, F. Platten, S. U. Egelhaaf, J. Chamot-Rooke, R. Fenk, L. Nagel-Steger, , A. K. Buell

This study shows that all tested patient-derived immunoglobulin light chains have comparable amyloidogenic potential, with proteolytic cleavage being a key determinant of in vivo aggregation.

bioRxiv · May 12, 2021 · PreprintBiophysics