Author

R. Renger

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biophysics· 3 Biochemistry· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:chromatin & epigenetic regulation· 3 Assay:DNA methylation· 3 Research Focus:cell type annotation· 2 Assay:proteomics· 2 Research Focus:cell signaling & trafficking· 1 Organism:human· 1 Approach:microscopy & imaging analysis· 1

Frequent Co-Authors

F. Julicher· 2 shared S. W. Grill· 2 shared A. Hermann· 1 shared A. Mitra· 1 shared B. Huang· 1 shared C. R. Carlson· 1 shared D. Brown· 1 shared F. Ruhnow· 1 shared

Activity by Year

2019-2021 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 19 mutual co-author links

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2 shared papersBiophysics

F. Julicher

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

Co-condensation of proteins with single- and double-stranded DNA

R. Renger, J. A. Morin, R. Lemaitre, M. Ruer, F. Julicher, A. Hermann, S. W. Grill

This study uses optical tweezers to show FUS protein forms liquid-like co-condensates with DNA by adsorbing on single and double-stranded DNA, revealing phase separation mechanisms in nuclear compartments.

bioRxiv · Mar 17, 2021Biophysics

HP1 proteins compact DNA into mechanically and positionally stable phase separated domains

M. M. Keenen, D. Brown, L. D. Brennan, R. Renger, H. Khoo, C. R. Carlson, B. Huang, S. W. Grill, G. J. Narlikar, S. Redding

This study shows HP1 proteins form phase-separated DNA condensates that are mechanically stable but can be dissolved by HP1β, with differences in DNA compaction linked to their disordered regions.

bioRxiv · Oct 30, 2020Biochemistry

Force generation by protein-DNA co-condensation

T. Quail, S. Golfier, M. Elsner, K. Ishihara, R. Renger, F. Julicher, J. Brugues

The paper shows DNA condensation mediated by transcription factors generates forces that bring distant DNA regions together, suggesting a physical mechanism for chromatin organization.

bioRxiv · Sep 17, 2020 · PreprintBiophysics

The kinesin-14, Ncd, drives a right-handed, helical motion of antiparallel microtubules around each other

A. Mitra, R. Gandhimathi, F. Ruhnow, R. Renger, S. Diez

This study investigates the motion of microtubules driven by the kinesin-14 Ncd, revealing right-handed helical motion in antiparallel configurations and static behavior in parallel ones.

bioRxiv · Sep 5, 2019Biophysics