Author

D. Boehringer

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· 3 Cell Biology· 1 Immunology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 6 Organism:human· 5 Research Focus:cell signaling & trafficking· 4 Assay:imaging· 2 Assay:protein structure· 2 Assay:proteomics· 2 Research Focus:benchmarking· 1 Approach:biophysical modeling· 1

Frequent Co-Authors

B. Fabry· 3 shared A. Bauer· 2 shared C. Mark· 2 shared D. Kah· 2 shared J. Rabl· 2 shared L. Bischof· 2 shared M. Peter· 2 shared P. Afanasyev· 2 shared

Activity by Year

2020-2024 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 23 mutual co-author links

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3 shared papersBiophysics

B. Fabry

Mutual co-authors in cluster

Author profile →

8 papers

Recent·Most cited

SP110 sequestration of SP100 protects against toxic filaments during innate immune signaling

E. J. Aird, J. Rabl, T. Knuesel, L. Scherpe, D. Boehringer, J. E. Corn

The paper identifies SP110 as a negative regulator of type 1 interferon-driven cell death by counteracting SP100's toxic filament formation through CARD domain interactions.

bioRxiv · Apr 3, 2024Immunology

Contractility of cardiac and skeletal muscle tissue increases with environmental stiffness

D. Kah, J. Lell, T. Wach, M. Spoerrer, C. A. Dessalles, J. Kraxner, S. Wiedenmann, R. C. Gerum, S. Vergarajauregui, T. U. Esser, D. Boehringer, F. B. Engel, I. Thievessen, B. Fabry

This study shows that contractile force in cardiac and skeletal muscle tissues increases with environmental stiffness following a power-law relationship.

bioRxiv · Feb 23, 2024 · PreprintBiophysics

Fiber alignment in 3D collagen networks as a biophysical marker for cell contractility

D. Boehringer, A. Bauer, I. Moravec, L. Bischof, D. Kah, C. Mark, T. J. Grundy, E. Goerlach, G. M. O'Neill, S. Budday, P. Strissel, R. Strick, A. Malandrino, R. Gerum, M. Mak, , B. Fabry

This study uses fiber alignment and density in 3D collagen networks as a proxy for cell traction forces, validated in hepatic stellate cells and glioblastoma cell lines, and provides an open-source tool for drug screening.

bioRxiv · Jun 28, 2023Biophysics

A solid beta-sheet structure is formed at the surface of FUS liquid droplets during aging

L. Emmanouilidis, E. Bartalucci, Y. Kan, M. Ijavi, M. E. Perez, P. Afanasyev, D. Boehringer, J. Zehnder, S. H. Parekh, M. Bonn, T. C. T. Michaels, T. Wiegand, F. H.- T. Allain

This study investigates FUS liquid droplet maturation, revealing a solid beta-sheet surface layer that forms during aging, with RNA inhibiting this process.

bioRxiv · Jun 2, 2023Biochemistry

Dynamic traction force measurements of migrating immune cells in 3D matrices

D. Boehringer, M. Condor, L. Bischof, T. Czerwinski, N. Gampl, P. A. Ngo, A. Bauer, R. Lopez-Posadas, K. Franze, C. Voskens, S. Budday, C. Mark, B. Fabry, R. Gerum

This study measures dynamic traction forces of migrating NK cells in 3D matrices and finds that force bursts increase with matrix stiffness to aid migration through constrictions.

bioRxiv · Nov 16, 2022Biophysics

A conserved mechanism regulates reversible amyloids via pH-sensing regions

G. Cereghetti, V. M. Kissling, L. M. Koch, A. Arm, P. Afanasyev, M. Linsenmeier, C. Eichmann, J. Zhou, Y. Cao, D. M. Pfizenmaier, S. Kroschwald, T. Wiegand, R. Cadalbert, D. Boehringer, R. Mezzenga, , M. Peter

This study identifies a conserved mechanism by which pH-sensing regions regulate reversible amyloid formation in pyruvate kinase across yeast and human cells.

bioRxiv · Mar 21, 2022 · PreprintCell Biology

The human GID complex engages two independent modules for substrate recruitment

M. Peter, W. I. Mohamed, S. L. Park, J. Rabl, A. Leitner, D. Boehringer

This study identifies two distinct modules in the human GID complex for substrate recruitment, revealing different roles for WDR26 and GID4 in ubiquitination and substrate recognition.

The EMBO Reports · Oct 14, 2021Peer-reviewedBiochemistry

The 3.2A resolution structure of human mTORC2

A. Scaiola, F. Mangia, S. Imseng, D. Boehringer, K. Berneiser, M. Shimobayashi, E. Stuttfeld, M. N. Hall, N. Ban, T. Maier

This study presents a 3.2 Å resolution cryo-EM structure of human mTORC2, revealing structural features and regulatory mechanisms.

bioRxiv · Apr 10, 2020 · PreprintBiochemistry