Author

C. Davidovich

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· 2 Biochemistry· 1

Signature Assays, Organisms & Methods

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Research Focus:chromatin & epigenetic regulation· 2 Approach:experimental assay· 2 Organism:mouse· 2 Assay:ChIP-seq· 1 Assay:electronic health records· 1 Organism:human· 1 Approach:microscopy & imaging analysis· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

Q. Zhang· 2 shared V. Levina· 2 shared A. Borodavka· 1 shared A. de Marco· 1 shared A. N. Calabrese· 1 shared B. M. Owen· 1 shared C. Taveneau· 1 shared D. C. Lamb· 1 shared

Activity by Year

2020-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 18 mutual co-author links

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2 shared papersBiophysics

Q. Zhang

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Dynamic PRC1-CBX8 stabilizes a porous structure of chromatin condensates

M. Uckelmann, V. Levina, C. Taveneau, X. H. Ng, V. Pandey, J. Martinez, S. Mendiratta, J. Houx, M. Boudes, H. Venugopal, S. Trepout, Q. Zhang, S. Flanigan, M. Li, E. Sierecki, , C. Davidovich

This study uses cryo-electron tomography to reveal that PRC1-CBX8 condensates are porous and dynamic, challenging the notion of rigid chromatin compaction in gene repression.

bioRxiv · May 8, 2023Biophysics

Structural basis of rotavirus RNA chaperone displacement and RNA annealing

J. P. K. Bravo, K. Bartnik, L. Venditti, E. H. Gail, C. Davidovich, D. C. Lamb, R. Tuma, A. N. Calabrese, A. Borodavka

This study identifies how the rotavirus NSP2 protein regulates RNA chaperone activity through structural changes that promote RNA annealing and release.

bioRxiv · Oct 26, 2020Biophysics

Convergent evolution between PALI1 and JARID2 for the allosteric activation of PRC2

Q. Zhang, S. C. Agius, S. F. Flanigan, V. Levina, B. M. Owen, C. Davidovich

This study shows that PALI1, a vertebrate-specific PRC2 accessory subunit, convergently evolved to function like JARID2 by allosterically activating PRC2 through methylation and DNA binding.

bioRxiv · May 28, 2020Biochemistry