Author

C. Bjorkegren

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· 1 Biophysics· 1 Cell Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1 Research Focus:chromatin & epigenetic regulation· 1 Research Focus:host-pathogen & immune response· 1 Research Focus:protein folding & dynamics· 1 Organism:yeast· 1

Frequent Co-Authors

A. F. Pinto· 1 shared A. Kouznetsova· 1 shared A. Nordstrom· 1 shared A.-G. Thorsell· 1 shared B. Pradhan· 1 shared E. Kim· 1 shared E. Loverli· 1 shared E. M. De La Cruz· 1 shared

Activity by Year

2018-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 22 mutual co-author links

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1 shared paperBiochemistry

A. F. Pinto

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3 papers

Recent·Most cited

A system for inducible mitochondria-specific protein degradation in vivo

S. Sanyal, A. Kouznetsova, C. Bjorkegren

The paper develops an inducible system for mitochondria-specific protein degradation in yeast using mf-Lon protease and a PDT tag, enabling analysis of proteins localized to both mitochondria and nucleus.

bioRxiv · Dec 20, 2022Cell Biology

The Smc5/6 complex is a DNA loop extruding motor

B. Pradhan, T. Kanno, M. U. Igarashi, M. D. Baaske, J. S. K. Wong, K. Jeppsson, C. Bjorkegren, E. Kim

The paper identifies Smc5/6 as a DNA-loop-extruding motor, showing it extrudes loops via dimerization and ATP hydrolysis at 1 kb/s.

bioRxiv · May 13, 2022Biophysics

14-3-3 proteins activate Pseudomonas exotoxins-S and -T by chaperoning a hydrophobic surface

T. Karlberg, P. Hornyak, A. F. Pinto, S. Milanova, M. Ebrahimi, M. Lindberg, N. Pullen, A. Nordstrom, E. Loverli, R. Caraballo, E. V. Wong, K. Nareoja, A.-G. Thorsell, M. Elofsson, E. M. De La Cruz, , H. Schuler

This study identifies a novel hydrophobic interface between 14-3-3 proteins and Pseudomonas exotoxins-S and -T, showing 14-3-3 activates these toxins by preventing aggregation, independent of their C-terminal phosphopeptide binding motifs.

bioRxiv · Jun 8, 2018Biochemistry