Author

J. Fedry

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

Cell Biology· 2 Immunology· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Organism:human· 3 Research Focus:cell signaling & trafficking· 2 Approach:experimental assay· 2 Research Focus:cell type annotation· 1 Research Focus:chromatin & epigenetic regulation· 1 Assay:cryo-EM· 1 Research Focus:host-pathogen & immune response· 1 Approach:microscopy & imaging analysis· 1

Frequent Co-Authors

F. Förster· 2 shared A. des Georges· 1 shared A. Raimondi· 1 shared B. J. Bosch· 1 shared C. Galli· 1 shared C. Wang· 1 shared D. L. Hurdiss· 1 shared D. Morone· 1 shared

Activity by Year

2020-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 15 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

F. Förster

Mutual co-authors in cluster

Author profile →

3 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

SEC62 and TMX4 control asymmetric autophagy of the nuclear envelope upon LINC complex disassembly

M. Kucinska, J. Fedry, C. Galli, D. Morone, A. Raimondi, T. Solda, F. Foerster, M. Molinari

The paper identifies SEC62 and TMX4 as regulators of asymmetric autophagy of the nuclear envelope during LINC complex disassembly in response to ER homeostatic changes.

bioRxiv · Oct 5, 2022 · PreprintCell Biology

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