Author

R. I. Enchev

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 Biophysics· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 3 Research Focus:cell signaling & trafficking· 2 Assay:cryo-EM· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

M. Peter· 2 shared A. Kaczmarczyk· 1 shared A. Nans· 1 shared B. Lee· 1 shared C. Barroso· 1 shared C.-S. Lee· 1 shared D. J. Smith· 1 shared D. S. Rueda· 1 shared

Activity by Year

2018-2020 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 20 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 papersBiochemistry

M. Peter

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Single-molecule analysis reveals cooperative stimulation of Rad51 filament nucleation and growth by mediator proteins

O. Belan, C. Barroso, A. Kaczmarczyk, R. Anand, S. Federico, N. O'Reilly, M. D. Newton, E. Maeots, R. I. Enchev, E. Martinez-Perez, D. S. Rueda, S. J. Boulton

The paper uses single-molecule imaging to show how BRC-2 and RFS-1/RIP-1 mediate RAD-51 filament nucleation and growth during homologous recombination.

bioRxiv · Nov 5, 2020Biophysics

Visual Biochemistry: modular microfluidics enables kinetic insight from time-resolved cryo-EM

M.-E. Maeots, B. Lee, A. Nans, S.-G. Jeong, M. M. N. Esfahani, D. J. Smith, C.-S. Lee, S. S. Lee, M. Peter, R. I. Enchev

This paper introduces a time-resolved cryo-EM method using modular microfluidics to visualize biochemical reactions at near-atomic resolution and millisecond timescales, demonstrating its application to RecA filament formation.

Nature Communications · Jul 10, 2020Peer-reviewedBiochemistry

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