Author

S. Elsasser

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

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Approach:biophysical modeling· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:chromatin & epigenetic regulation· 1 Research Focus:host-pathogen & immune response· 1 Organism:mouse· 1 Research Focus:protein folding & dynamics· 1 Assay:proteomics· 1

Frequent Co-Authors

D. Finley· 2 shared A. Matouschek· 1 shared B. L. Spaller· 1 shared B.-H. Lee· 1 shared C. Davis· 1 shared D. Van Dalen· 1 shared E. Choi· 1 shared E. Sakata· 1 shared

Activity by Year

2021-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 25 mutual co-author links

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2 shared papersBiochemistry

D. Finley

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2 papers

Recent·Most cited

A strict requirement in proteasome substrates for spacing between ubiquitin tag and degradation initiation elements

C. Davis, B. L. Spaller, E. Choi, J. B. Kurrasch, H. Chong, S. Elsasser, D. Finley, A. Matouschek

The paper shows that the distance between ubiquitin tags and degradation initiation elements determines proteasome-mediated protein degradation efficiency.

bioRxiv · Aug 8, 2023 · PreprintBiochemistry

Allosteric control of Ubp6 and the proteasome via a bidirectional switch

K. Y. S. Hung, S. Klumpe, M. R. Eisele, S. Elsasser, G. Tian, S. Sun, J. A. Moroco, T. C. Cheng, T. Joshi, T. Seibel, D. Van Dalen, X.-H. Feng, Y. Lu, H. Ovaa, J. R. Engen, , D. Finley

This study identifies an allosteric switch that controls Ubp6 and the proteasome, showing their active states are mutually exclusive.

bioRxiv · Jul 16, 2021Biochemistry