Author

L. M. Murschall

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

Click to filter author papers

Biochemistry· 2

Signature Assays, Organisms & Methods

Click to filter · or open tag

Research Focus:cell signaling & trafficking· 2 Approach:experimental assay· 2 Organism:human· 2 Research Focus:cell type annotation· 1 Assay:imaging· 1 Research Focus:protein folding & dynamics· 1 Assay:protein structure· 1 Assay:proteomics· 1

Frequent Co-Authors

J. Riemer· 2 shared A. M. Schlagowski· 1 shared A. Sachez Vicente· 1 shared B. Morgan· 1 shared B. Westermann· 1 shared F. Boos· 1 shared F. Stein· 1 shared G. Charvin· 1 shared

Activity by Year

2021-2021 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 37 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

2 shared papersBiochemistry

J. Riemer

Mutual co-authors in cluster

Author profile →

2 papers

Recent·Most cited

Thioredoxin reductase controls the capacity of peroxiredoxins to limit mitochondrial H2O2 release

M. N. Hoehne, L. J. Jacobs, K. J. Lapacz, L. M. Murschall, T. Marker, B. Morgan, M. Fricker, V. Belousov, J. Riemer

The paper investigates mitochondrial H2O2 release in mammalian cells and finds that peroxiredoxins 1 and 2 control H2O2 gradients and handling through dynamic adaptation of thioredoxin reductase.

bioRxiv · Jul 8, 2021 · PreprintBiochemistry

Increased levels of the mitochondrial import factor Mia40 prevent the aggregation of polyQ proteins in the cytosol

A. M. Schlagowski, K. Knöringer, S. Morlot, A. Sachez Vicente, F. Boos, N. Khalid, S. Ahmed, J. Schramm, L. M. Murschall, P. Haberkant, F. Stein, J. Riemer, B. Westermann, R. J. Braun, K. F. Winklhofer, , J. M. Herrmann

The paper shows that overexpressing Mia40 reduces toxic polyQ protein aggregates in yeast and human cells by competing for chaperone and proteasome resources.

bioRxiv · Feb 2, 2021Biochemistry