Author

Y. Turgay

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 Biophysics· 1 Cell Biology· 1 Microbiology· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Assay:cryo-EM· 2 Approach:experimental assay· 2 Approach:microscopy & imaging analysis· 2 Research Focus:protein structure prediction· 2 Organism:bacteria (other)· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:development & morphogenesis· 1 Research Focus:host-pathogen & immune response· 1

Frequent Co-Authors

E. Slack· 2 shared M. Eibauer· 2 shared M. Radiom· 2 shared M. S. Weber· 2 shared O. Medalia· 2 shared R. D. Goldman· 2 shared R. Mezzenga· 2 shared S. Sivagurunathan· 2 shared

Activity by Year

2021-2023 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 19 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 papersBiophysics

E. Slack

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

BiophysicsbioRxivPreprintJul 29, 2023

Surface crosslinking of virus-like particles increases resistance to proteases, low pH and mechanical stress for mucosal applications

A. Ali, S. Ganguillet, Y. Turgay…·M. Radiom

This study enhances the stability of virus-like particles (VLPs) against environmental stressors by surface crosslinking, without affecting their vaccine function.

DOI 10.1101/2023.07.29.550271

experimental assay

𝕏 PostBluesky

MicrobiologybioRxivPreprintJul 13, 2023

Nanoscale clustering by O-antigen-Secretory Immunoglobulin-A binding limits outer membrane diffusion by encaging individual Salmonella cells

A. Hockenberry, M. Radiom, M. Arnoldini…·E. Slack

The paper shows SIgA binding to Salmonella O-antigen nanoscale crosslinks the outer membrane, leading to biased inheritance and accelerated IgA escape through phase-variation.

DOI 10.1101/2023.07.13.548943

bacteria (other)proteomics

𝕏 PostBluesky

BiochemistrybioRxivMay 22, 2023

Vimentin filaments integrate low complexity domains in a highly complex helical structure

M. Eibauer, M. S. Weber, R. Kronenberg-Tenga…·O. Medalia

This study determines the 3D structure of vimentin intermediate filaments, revealing how disordered domains contribute to their mechanical properties.

DOI 10.1038/s41594-024-01261-2

cryo-EMmicroscopy & imaging analysis

𝕏 PostBluesky

Cell BiologybioRxivPreprintJul 15, 2021

The molecular architecture of vimentin filaments

M. Eibauer, M. S. Weber, Y. Turgay…·O. Medalia

This study reveals the subnanometer structure of vimentin filaments in mouse cells, showing their helical symmetry and molecular composition.

DOI 10.1101/2021.07.15.452584

mousecryo-EM

𝕏 PostBluesky