Author

F. Förster

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

Biochemistry· 1 Cell Biology· 1 Immunology· 1 Microbiology· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 3 Assay:structural biology· 3 Organism:human· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:chromatin & epigenetic regulation· 1 Assay:cryo-EM· 1 Research Focus:drug response / drug discovery· 1 Research Focus:host-pathogen & immune response· 1

Frequent Co-Authors

D. L. Hurdiss· 2 shared F. J. M. van Kuppeveld· 2 shared J. Fedry· 2 shared A. Brancale· 1 shared A. des Georges· 1 shared A. J. R. Heck· 1 shared A. Konijnenberg· 1 shared A. L. W. van Vliet· 1 shared

Activity by Year

2020-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 16 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 papersMicrobiology

D. L. Hurdiss

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

Visualization of translation reorganization upon persistent collision stress in mammalian cells

J. Fedry, J. Silva, M. Vanevic, S. Fronik, Y. Mechulam, E. Schmitt, A. des Georges, W. Faller, F. Förster

The paper visualizes how translation reorganizes in mammalian cells under persistent collision stress, revealing changes in ribosome complexes and quality control mechanisms.

bioRxiv · Mar 23, 2023 · PreprintCell Biology

Thriving in the heat - Lysine acetylation stabilizes the quaternary structure of a Mega-Dalton hyperthermoactive PEP-synthase

P. Albanese, W. Song, S. v. Keulen, J. Koendjbiharie, F. Koh, B. Steigenberger, T. Vincent, A. Konijnenberg, A. J. R. Heck, S. Kengen, A. M. J. J. Bonvin, F. Förster, R. A. Scheltema

The paper investigates how lysine acetylation stabilizes the structure of a hyperthermoactive PEP-synthase from Pyrococcus furious, revealing its role in maintaining function under extreme temperatures.

bioRxiv · Aug 11, 2022 · PreprintBiochemistry

Fluoxetine targets an allosteric site in the enterovirus 2C AAA+ ATPase and stabilizes the hexameric complex

D. L. Hurdiss, P. El Kazzi, L. Bauer, N. Papageorgiou, F. P. Ferron, T. Donselaar, A. L. W. van Vliet, B. Canard, E. Decroly, A. Brancale, T. Zeev-Ben-Mordehai, F. Förster, F. J. M. van Kuppeveld, B. Coutard

This study identifies fluoxetine as an inhibitor of the enterovirus 2C AAA+ ATPase, revealing its mechanism of action through structural and functional analyses.

bioRxiv · Apr 26, 2021Microbiology

A human monoclonal antibody targeting a conserved pocket in the SARS-CoV-2 receptor-binding domain core

J. Fedry, D. L. Hurdiss, C. Wang, W. Li, G. Obal, I. Drulyte, S. C. Howes, F. J. M. van Kuppeveld, F. Förster, B. J. Bosch

This paper identifies a human monoclonal antibody, 47D11, that targets a conserved hydrophobic pocket in the SARS-CoV-2 RBD, revealing its structural basis for neutralization and potential therapeutic use.

bioRxiv · Sep 30, 2020Immunology