Author

S. Borgers

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· 3

Signature Assays, Organisms & Methods

Click to filter · or open tag

Research Focus:cell type annotation· 3 Approach:experimental assay· 3 Research Focus:cell signaling & trafficking· 2 Research Focus:development & morphogenesis· 2 Organism:human· 2 Organism:chicken / avian· 1 Assay:electronic health records· 1 Assay:fluorescence / live-cell microscopy· 1

Frequent Co-Authors

v. Hamel· 3 shared D. Gambarotto· 2 shared P. Guichard· 2 shared A. Giroud· 1 shared A. Paoletti· 1 shared A.-M. Tassin· 1 shared C. Zheng· 1 shared D. Fortun· 1 shared

Activity by Year

2018-2021 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 24 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

3 shared papersCell Biology

v. Hamel

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

SFI1 and centrin form a distal end complex critical for proper centriole architecture and ciliogenesis

I. Bouhlel, M. Laporte, E. Bertiaux, A. Giroud, S. Borgers, J. Azimzadeh, M. Borneans, P. Guichard, A. Paoletti, v. Hamel

This study identifies SFI1 and centrin as a distal end complex essential for centriole architecture and ciliogenesis in human cells.

bioRxiv · Oct 5, 2021 · PreprintCell Biology

WDR90 is a centriolar microtubule wall protein important for centriole architecture integrity.

E. Steib, D. Gambarotto, M. H. Laporte, N. Olieric, C. Zheng, S. Borgers, V. Olieric, M. Le Guennec, F. Koll, A.-M. Tassin, M. O. Steinmetz, P. Guichard, V. Hamel

This study identifies WDR90 as a centriolar microtubule wall protein essential for maintaining centriole structure in human and Chlamydomonas cells.

bioRxiv · Feb 15, 2020Cell Biology

Imaging beyond the super-resolution limits using ultrastructure expansion microscopy (UltraExM)

D. Gambarotto, F. U. Zwettler, M. Cernohorska, D. Fortun, S. Borgers, J. Heine, J. G. Schloetel, M. Reuss, M. Unser, E. S. Boyden, M. Sauer, V. Hamel, P. Guichard

This paper introduces UltraExM, a method that enables subdiffraction-resolution imaging of preserved ultrastructures using standard optical microscopy, revealing new insights into centriolar structures.

bioRxiv · Apr 25, 2018 · PreprintCell Biology