Author

Sophie M. Gutenthaler

Heinrich Heine University DüsseldorfORCID 0000-0002-8412-3328Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Microbiology· 2 Biochemistry· 1

Signature Assays, Organisms & Methods

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Organism:bacteria (other)· 2 Approach:experimental assay· 2 Assay:proteomics· 2 Approach:biophysical modeling· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1 Research Focus:chromatin & epigenetic regulation· 1 Research Focus:gene regulatory network inference· 1

Frequent Co-Authors

Lena Josefine DaumanniD· 3 shared Abigail C Major· 1 shared Aldwin Suryo RahmantoiD· 1 shared Alina Lobe· 1 shared Carl‐Eric WegneriD· 1 shared Christian RenziD· 1 shared Christian WiebeleriD· 1 shared Denitsa Yaneva· 1 shared

Activity by Year

2025-2026 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 27 mutual co-author links

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

Curved chords = mutual co-authorship

3 shared papersMicrobiology

Lena Josefine DaumannORCID

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Source-independent enrichment of light lanthanides: microbial mobilization, selective uptake, and intracellular storage

Linda Gorniak, Sophie M. Gutenthaler, Alina Lobe, Lena Josefine Daumann, Robin Steudtner, Thorsten Schäfer, Frank Steiniger, Martin Westermann, Kirsten Küsel, Carl‐Eric Wegner

This study investigates how a bacterium selectively enriches light lanthanides from various sources, revealing mechanisms for microbial lanthanide discrimination and storage.

Environmental Microbiology · Sep 1, 2026Peer-reviewedMicrobiology

There is no convincing evidence that Methylobacterium extorquens AM1 can produce N-deoxyschizokinen A

Sophie M. Gutenthaler, Patrick Weis, Lena Josefine Daumann

The paper investigates claims of N-deoxyschizokinen A production by Methylobacterium extorquens AM1 and concludes the detection is an artifact.

bioRxiv · Jul 6, 2026 · PreprintMicrobiology

Allosteric activation of the SPRTN protease by ubiquitin maintains genome stability

Sophie Dürauer, Hyun-Seo Kang, Christian Wiebeler, Yuka Machida, Dina S Schnapka, Denitsa Yaneva, Christian Renz, Maximilian J. Götz, Pedro Weickert, Abigail C Major, Aldwin Suryo Rahmanto, Sophie M. Gutenthaler, Lena Josefine Daumann, Petra Beli, Helle D. Ulrich, , Julian Stingele

This study shows that ubiquitin activates SPRTN protease to degrade DNA-protein crosslinks, maintaining genome stability and preventing disease.

Nature Communications · Jul 21, 2025Peer-reviewedBiochemistry