Author

K. Belacic

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· 2 Biophysics· 1

Signature Assays, Organisms & Methods

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Assay:cryo-EM· 2 Approach:experimental assay· 2 Approach:microscopy & imaging analysis· 2 Research Focus:protein folding & dynamics· 2 Assay:proteomics· 2 Research Focus:cell type annotation· 1 Research Focus:chromatin & epigenetic regulation· 1 Organism:human· 1

Frequent Co-Authors

D. Haselbach· 3 shared I. Grishkovskaya· 2 shared N. G. Brown· 2 shared A. Meinhart· 1 shared A. Pauli· 1 shared A. Schleiffer· 1 shared A. Sonn Segev· 1 shared B. Bauer· 1 shared

Activity by Year

2019-2022 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 24 mutual co-author links

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3 shared papersBiochemistry

D. Haselbach

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Author profile →

3 papers

Recent·Most cited

Cryo-EM structure of the chain-elongating E3 ligase UBR5

Z. Hodakova, I. Grishkovskaya, H. L. Brunner, D. L. Bolhuis, K. Belacic, A. Schleiffer, H. Kotisch, N. G. Brown, D. Haselbach

The paper presents the cryo-EM structure of UBR5, revealing its dimeric architecture and dynamic domain movements, and identifies AKIRIN2 as an interacting protein.

bioRxiv · Nov 3, 2022 · PreprintBiochemistry

A molecular network of conserved factors keeps ribosomes dormant in the egg

K. F. Leesch, L. Lorenzo-Orts, C. Pribitzer, I. Grishkovskaya, M. Matzinger, E. Roitinger, K. Belacic, S. Kandolf, T.-Y. Lin, K. Mechtler, A. Meinhart, D. Haselbach, A. Pauli

The paper identifies conserved factors that maintain ribosome dormancy in zebrafish and Xenopus eggs and embryos, transitioning to an active state during early development.

bioRxiv · Nov 3, 2021Biochemistry

Quantifying the heterogeneity of macromolecular machines by mass photometry

A. Sonn Segev, K. Belacic, T. Bodrug, G. Young, R. T. VanderLinden, B. Schulman, J. Schimpf, T. Friedrich, P. Vinh Dip, T. Schwartz, B. Bauer, J.-M. Peters, W. B. Struwe, J. L. Benesch, N. G. Brown, , P. Kukura

This paper demonstrates that mass photometry accurately quantifies sample heterogeneity with high resolution and minimal volume, outperforming negative stain electron microscopy in detecting proteasome assemblies.

bioRxiv · Dec 4, 2019Biophysics