Author

M. Ehrmann

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· 1 Cancer Biology· 1 Microbiology· 1 Pathology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Organism:human· 2 Assay:bulk RNA-seq· 1 Research Focus:cell type annotation· 1 Research Focus:cell-cell communication· 1 Research Focus:differential expression· 1 Research Focus:drug response / drug discovery· 1 Research Focus:host-pathogen & immune response· 1

Frequent Co-Authors

F. Kaschani· 2 shared M. Kaiser· 2 shared A. Bonaud· 1 shared A. Carpinteiro· 1 shared A. Jaccard· 1 shared A. Lampis· 1 shared A. Paschen· 1 shared A. Rinsant· 1 shared

Activity by Year

2020-2025 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 20 mutual co-author links

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2 shared papersBiochemistry

F. Kaschani

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

A mouse model of cardiac AL amyloidosis unveils mechanisms of tissue accumulation and toxicity of amyloid fibrils

G. Martinez-Rivas, M. V. Ayala, S. Bender, G. R. Codo, K. W. Swiderska, A. Lampis, L. Pedroza, M. Merdanovic, P. Sicard, E. Pinault, L. Richard, F. Lavatelli, D. Canetti, A. Rinsant, K. Sihem, , C. Sirac

This paper develops a mouse model of cardiac AL amyloidosis that reproduces human disease features, including amyloid deposits and cardiac dysfunction, and identifies a role for partial LC degradation in fibril formation.

Nature Communications · Mar 27, 2025Peer-reviewedPathology

A single residue within the MCR-1 protein confers anticipatory resilience

R. Frantz, K. Gwozdzinski, N. Gisch, S. P. Doijad, M. Hudel, M. Wille, M. A. Mraheil, D. Schwudke, C. Imirzalioglu, L. Falgenhauer, M. Ehrmann, T. Chakraborty

This study identifies a single residue in MCR-1 that modulates its interaction with the ESR system, affecting colistin resistance and bacterial resilience to environmental stressors.

bioRxiv · Jul 8, 2022 · PreprintMicrobiology

High resolution analysis of proteolytic substrate processing

J. Schillinger, M. Koci, K. Bravo Rodriguez, G. Heilmann, F. Kaschani, M. Kaiser, C. Beuck, H. Luecke, R. Huber, D. Hellerschmied, S. G. Burston, M. Ehrmann

The paper develops an integrated method to analyze proteolytic substrate processing at high resolution using time-resolved mass spectrometry and other techniques.

bioRxiv · Mar 24, 2022Biochemistry

Persister state-directed transitioning and vulnerability in melanoma

H. Chauvistre, B. Shannan, S. M. Daignault, R. J. Ju, D. Picard, S. Egetemaier, R. Varaljai, A. Sechi, F. Kaschani, O. Keminer, S. J. Stehbens, Q. Liu, X. Yin, K. Jeyakumar, F. C. E. Vogel, , A. Roesch

This study identifies a compound that induces a persister state in melanoma cells, promoting differentiation and sensitizing them to a prodrug, offering a dual-target strategy for treatment.

bioRxiv · Apr 1, 2020Cancer Biology