Author

M. Kschonsak

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 Bioengineering· 1 Cell Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:chromatin & epigenetic regulation· 2 Assay:cryo-EM· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:drug response / drug discovery· 1 Approach:microscopy & imaging analysis· 1 Assay:proteomics· 1

Frequent Co-Authors

A. Khmelinskii· 1 shared A. L. Rohou· 1 shared C. C. Jao· 1 shared C. Ciferri· 1 shared C. H. Haering· 1 shared C. P. Arthur· 1 shared C. Stober· 1 shared D. H. Hackos· 1 shared

Activity by Year

2020-2022 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 22 mutual co-author links

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1 shared paperCell Biology

A. Khmelinskii

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3 papers

Recent·Most cited

CryoEM reveals unprecedented binding site for NaV1.7 inhibitors enabling rational design of potent hybrid inhibitors

M. Kschonsak, C. C. Jao, C. P. Arthur, A. L. Rohou, P. Bergeron, D. Ortwine, S. J. McKerrall, D. H. Hackos, L. Deng, J. Chen, D. S. Peter, M. Volgraf, M. Wright, J. Payandeh, C. Ciferri, J. C. Tellis

This study uses cryo-EM to reveal a new binding site for NaV1.7 inhibitors, enabling the design of hybrid inhibitors with improved selectivity and properties.

bioRxiv · Nov 10, 2022Bioengineering

A hold-and-feed mechanism drives directional DNA loop extrusion by condensin

I. A. Shaltiel, S. Datta, L. Lecomte, M. Hassler, M. Kschonsak, S. Bravo, C. Stober, S. Eustermann, C. H. Haering

This study reveals that condensin uses a hold-and-feed mechanism to extrude DNA loops bidirectionally by separating motor and anchor functions in distinct chambers.

bioRxiv · Oct 29, 2021Biochemistry

Mechanisms of up-regulation of Ubiquitin-Proteasome activity in the absence of NatA dependent N-terminal acetylation

I. Kats, M. Kschonsak, A. Khmelinskii, L. Armbruster, T. Ruppert, M. Knop

The paper investigates how UPS activity increases in NatA mutants and identifies mechanisms involving Rpn4 regulation, E3 ligase abundance, and Tom1's role as an E4 ligase.

bioRxiv · Mar 23, 2020 · PreprintCell Biology