Author

P. Arnold

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· 1 Cell Biology· 1 Pathology· 1

Signature Assays, Organisms & Methods

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

Frequent Co-Authors

E. Socher· 2 shared F. Paulsen· 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 2/yr

Co-Author Collaboration Network

10 top collaborators · 33 mutual co-author links

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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

Obsessive Compulsive Disorder and Response Inhibition: Meta-analysis of the Stop-Signal Task

K. Mar, P. Townes, P. Pechlivanoglou, P. Arnold, R. J. Schachar

This meta-analysis finds that OCD patients show longer stop-signal reaction times, indicating impaired response inhibition, with greater deficits in older individuals.

bioRxiv · Jul 16, 2021Pathology

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