Author

B. Zagrovic

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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Biochemistry· 3 Biophysics· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Assay:structural biology· 3 Organism:human· 2 Research Focus:protein folding & dynamics· 2 Research Focus:chromatin & epigenetic regulation· 1 Organism:mouse· 1 Assay:protein structure· 1 Research Focus:protein structure prediction· 1

Frequent Co-Authors

A. Stadler· 2 shared G. Dong· 2 shared J. Sunter· 2 shared S. Alonso-Gil· 2 shared S. Vaughan· 2 shared A. A. Polyansky· 1 shared A. Akalin· 1 shared A. Koehler· 1 shared

Activity by Year

2022-2023 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 14 mutual co-author links

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2 shared papersBiochemistry

A. Stadler

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

The C-terminus of CFAP410 forms a tetrameric helical bundle that is essential for its localization to the basal body

A. Stadler, S. Alonso-Gil, B. Zagrovic, S. Vaughan, J. Sunter, G. Dong

This study determines the structure of CFAP410's C-terminal domain and shows that its tetrameric helical bundle is essential for basal body localization, explaining how the L224P mutation causes ciliopathies.

bioRxiv · Nov 30, 2023Biochemistry

CFAP410 has a bimodular architecture with a conserved surface patch on its N-terminal LRR motif for binding interaction partners

A. Stadler, H. B. Gabriel, L. V. De Liz, S. Alonso-Gil, X. Deng, R. Crickley, K. Korbula, K. Huang, B. Zagrovic, S. Vaughan, J. Sunter, G. Dong

This study reports the crystal structure of the N-terminal domain of CFAP410 and shows how mutations in this domain disrupt its structural stability and interaction with partners, leading to disease.

bioRxiv · Sep 21, 2022 · PreprintBiochemistry

The SPOC domain is a phosphoserine binding module that bridges transcription machinery with co- and post-transcriptional regulators

L.-M. Appel, I. Grishkovskaya, J. Benedum, V. Franke, A. Polyansky, A. Neudolt, A. Wunder, B. Zagrovic, A. Akalin, K. Djinovic-Carugo, D. Slade

bioRxiv · Feb 26, 2022 · PreprintBiochemistry

Protein compactness and interaction valency define the architecture of a biomolecular condensate across scales

A. A. Polyansky, L. D. Gallego, R. G. Efremov, A. Koehler, B. Zagrovic

This study connects molecular dynamics simulations of Lge11-80 with in vitro condensate behavior to derive a framework describing condensate architecture based on protein valency and compactness.

bioRxiv · Feb 18, 2022Biophysics