Author

C. Kampmeyer

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· 4

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:protein folding & dynamics· 3 Organism:yeast· 3 Research Focus:cell signaling & trafficking· 2 Research Focus:chromatin & epigenetic regulation· 2 Assay:proteomics· 2 Approach:biophysical modeling· 1 Research Focus:cell type annotation· 1

Frequent Co-Authors

K. Lindorff-Larsen· 4 shared R. Hartmann-Petersen· 4 shared A. Stein· 3 shared C. Andreasson· 2 shared M. Gronbaek-Thygesen· 2 shared T. Ravid· 2 shared A. B. Abildgaard· 1 shared A. Caregnato· 1 shared

Activity by Year

2020-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 34 mutual co-author links

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4 shared papersBiochemistry

K. Lindorff-Larsen

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4 papers

Recent·Most cited

Lysine deserts prevent adventitious ubiquitylation of ubiquitin-proteasome components

C. Kampmeyer, M. Gronbaek-Thygesen, N. Oelerich, M. H. Tatham, M. Cagiada, K. Lindorff-Larsen, W. Boomsma, K. Hofmann, R. Hartmann-Petersen

The paper identifies lysine deserts in UPS proteins and shows that introducing lysines increases ubiquitylation, with functional consequences for protein stability and function.

bioRxiv · Dec 8, 2022Biochemistry

HSP70-binding motifs function as protein quality control degrons

A. B. Abildgaard, V. Voutsinos, S. D. Petersen, F. B. Larsen, C. Kampmeyer, K. E. Johansson, A. Stein, T. Ravid, C. Andreasson, M. K. Jensen, K. Lindorff-Larsen, R. Hartmann-Petersen

The paper shows that Hsp70-binding motifs can function as PQC degrons, targeting misfolded proteins for degradation in yeast and human cells.

bioRxiv · Dec 22, 2021Biochemistry

Disease-linked mutations trigger exposure of a protein quality control degron in the DHFR protein

C. Kampmeyer, S. Larsen-Ledet, M. R. Wagnkilde, M. Michelsen, H. K. M. Iversen, S. V. Nielsen, S. Lindemose, A. Caregnato, T. Ravid, A. Stein, K. Teilum, K. Lindorff-Larsen, R. Hartmann-Petersen

The paper identifies two PQC degrons in DHFR that become exposed in disease-linked missense variants, leading to proteasomal degradation.

bioRxiv · Nov 4, 2021Biochemistry

Evolutionarily conserved chaperone-mediated proteasomal degradation of a disease-linked aspartoacylase variant

S. K. Gersing, Y. Wang, M. Gronbaek-Thygesen, C. Kampmeyer, L. Clausen, C. Andreasson, A. Stein, K. Lindorff-Larsen, R. Hartmann-Petersen

This study investigates the degradation pathway of a disease-linked ASPA variant, finding it is degraded via the proteasome and dependent on Hsp70 and Hsp110.

bioRxiv · Sep 4, 2020Biochemistry