Author

F. Paulsen

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

Click to filter author papers

Bioengineering· 1 Biophysics· 1 Cell Biology· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 2 Organism:human· 2 Assay:bulk RNA-seq· 1 Research Focus:cell type annotation· 1 Research Focus:host-pathogen & immune response· 1 Approach:mechanistic / dynamical model· 1 Organism:virus· 1

Frequent Co-Authors

E. Socher· 2 shared P. Arnold· 2 shared A. Drobny· 1 shared A.-O. Gostian· 1 shared C. Gunther· 1 shared F. Zunke· 1 shared G. Schulze-Tanzil· 1 shared H. Sicht· 1 shared

Activity by Year

2021-2024 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 33 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

2 shared papersCell Biology

E. Socher

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Characterization of a new lacrimal gland cell line in 2D and 3D cell culture models

S. Gleixner, I. Zahn, J. Dietrich, S. Singh, A. Drobny, Y. Schneider, R. Schwendner, E. Socher, N. Blavet, L. Brauer, A.-O. Gostian, M. Balk, G. Schulze-Tanzil, C. Gunther, F. Paulsen, P. Arnold

This paper develops an immortalized human lacrimal gland epithelial cell line for studying dry eye disease mechanisms and potential treatments.

bioRxiv · Feb 13, 2024 · PreprintCell Biology

Inverse identification of region-specific hyperelastic material parameters for human brain tissue

J. Hinrichsen, N. Reiter, L. Bräuer, F. Paulsen, S. Kaessmair, S. Budday

The paper identifies region-specific hyperelastic material parameters for human brain tissue using an inverse scheme and experimental data, revealing distinct mechanical properties across anatomical regions.

bioRxiv · Dec 19, 2022 · PreprintBioengineering

Mutations in the B.1.1.7 SARS-CoV-2 spike protein reduce receptor-binding affinity and induce a flexible link to the fusion peptide

E. Socher, M. Conrad, L. Heger, F. Paulsen, H. Sicht, F. Zunke, P. Arnold

This paper uses molecular dynamics simulations to show that B.1.1.7 SARS-CoV-2 mutations reduce ACE2 binding affinity and increase flexibility near the fusion peptide, potentially contributing to higher infectivity.

bioRxiv · Apr 6, 2021Biophysics