Author

C. Groh

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· 3 Cell Biology· 1

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Research Focus:cell signaling & trafficking· 3 Approach:experimental assay· 3 Assay:proteomics· 2 Approach:deep learning· 1 Organism:human· 1 Research Focus:protein folding & dynamics· 1 Approach:statistical model· 1 Organism:yeast· 1

Frequent Co-Authors

J. M. Herrmann· 4 shared F. Boos· 3 shared B. Morgan· 1 shared E. Paz· 1 shared E. Richling· 1 shared F. den Brave· 1 shared F. Stein· 1 shared H. Becker· 1 shared

Activity by Year

2020-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 20 mutual co-author links

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4 shared papersBiochemistry

J. M. Herrmann

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4 papers

Recent·Most cited

Mitochondrial dysfunction rapidly modulates the abundance and thermal stability of cellular proteins

C. Groh, P. Haberkant, F. Stein, S. Filbeck, S. Pfeffer, M. M. Savitski, F. Boos, J. M. Herrmann

The paper develops ppTPP to study mitochondrial dysfunction's effects on proteome stability and abundance, revealing group-specific response patterns in eukaryotic cells.

bioRxiv · Oct 27, 2022Biochemistry

The metabolite-controlled ubiquitin conjugase Ubc8 promotes mitochondrial protein import by enhancing assembly of the TOM complex

S. Roedl, F. den Brave, M. Raeschle, S. Lenhard, C. Groh, H. Becker, J. Zimmermann, B. Morgan, E. Richling, T. Becker, J. M. Herrmann

This study shows that Ubc8 promotes mitochondrial protein import by enhancing TOM complex assembly during metabolic transitions in yeast.

bioRxiv · Apr 26, 2022 · PreprintBiochemistry

The unfolded protein response of the endoplasmic reticulum supports mitochondrial biogenesis by buffering non-imported proteins

K. Knoeringer, C. Groh, L. Kraemer, K. C. Stein, K. G. Hansen, J. M. Herrmann, J. Frydman, F. Boos

The paper shows that mitochondrial membrane proteins accumulate in the endoplasmic reticulum during import defects, triggering the UPRER to maintain protein homeostasis.

bioRxiv · May 19, 2021Cell Biology

More than just a ticket canceller: The mitochondrial processing peptidase matures complex precursor proteins at internal cleavage sites

J. Friedl, M. R. Knopp, C. Groh, E. Paz, S. B. Gould, F. Boos, J. M. Herrmann

The paper shows that mitochondrial processing peptidase (MPP) cleaves precursor proteins at internal sites, not just N-terminal presequences, using the Arg5,6 polyprotein as a model.

bioRxiv · Jul 2, 2020Biochemistry