Author

M. Kupervaser

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· 2 Cell Biology· 2

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 3 Research Focus:cell signaling & trafficking· 2 Research Focus:cell type annotation· 1 Research Focus:cell-cell communication· 1 Research Focus:chromatin & epigenetic regulation· 1 Approach:deep learning· 1 Research Focus:protein design· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

A. Boshnakovska· 2 shared M. Schuldiner· 2 shared P. Rehling· 2 shared A. Brandis· 1 shared A. Reddi· 1 shared B. Homberg· 1 shared C. Lenz· 1 shared D. Rapaport· 1 shared

Activity by Year

2018-2024 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 35 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

A. Boshnakovska

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

The molecular mechanism of on-demand sterol biosynthesis at organelle contact sites

N. Zung, N. Aravindan, A. Boshnakovska, R. Valenti, N. Preminger, F. Jonas, G. Yaakov, M. Willoughby, B. Homberg, J. Keller, M. Kupervaser, N. Dezorella, T. Dadosh, S. G. Wolf, M. Itkin, , M. Schuldiner

This study identifies Yet3 as a protein that recruits sterol biosynthesis enzymes to ER contact sites, enabling on-demand sterol production and influencing organellar structure and function.

bioRxiv · May 9, 2024 · PreprintCell Biology

Profiling the LAM family of contact site tethers provides insights into their regulation and function

E. J. Fenech, M. Kupervaser, A. Boshnakovska, S. Ravid, I. Gomes Castro, Y. Asraf, S. Callegari, C. Lenz, P. Rehling, M. Schuldiner

The paper profiles the LAM family of contact site tethers to understand their localization and function, revealing unique and shared roles through proximity labeling.

bioRxiv · Apr 18, 2024Cell Biology

Designed high-redox potential laccases exhibit high functional diversity

S. Barber-Zucker, I. Mateljak, M. Goldsmith, M. Kupervaser, M. Alcalde, S. J. Fleishman

The paper designs high-redox potential laccases with improved stability and functional diversity through stabilization and active-site engineering.

bioRxiv · Jun 22, 2022Biochemistry

CSNAP, the smallest CSN subunit, modulates proteostasis through cullin-RING ubiquitin ligases

M. G. Füzesi-Levi, R. I. Enchev, G. Ben-Nissan, Y. Levin, M. Kupervaser, G. Friedlander, T. M. Salame, R. Nevo, M. Peter, M. Sharon

This study identifies CSNAP as a key subunit of the CSN complex that modulates CRL activity through steric inhibition, affecting cell viability and DNA damage response.

bioRxiv · Oct 2, 2018Biochemistry