Author

D. Sehr

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 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Research Focus:cell type annotation· 1 Research Focus:host-pathogen & immune response· 1 Organism:human· 1 Assay:proteomics· 1

Frequent Co-Authors

A. Bylicki· 1 shared A. Meinhart· 1 shared A. Vogel· 1 shared A.-L. Kiffe-Delf· 1 shared D. Podlesainski· 1 shared E. T. Adeniyi· 1 shared F. Kaschani· 1 shared F. Schulz· 1 shared

Activity by Year

2022-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 24 mutual co-author links

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1 shared paperBiochemistry

A. Bylicki

Mutual co-authors in cluster

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2 papers

Recent·Most cited

The anti-tubercular callyaerins target the Mycobacterium tuberculosis-specific non-essential membrane protein Rv2113

D. Podlesainski, E. T. Adeniyi, Y. Groener, F. Schulz, V. Krisilia, N. Rehberg, T. Richter, D. Sehr, H. Xie, V. E. Simons, A.-L. Kiffe-Delf, F. Kaschani, T. R. Ioerger, M. Kaiser, R. Kalscheuer

This study identifies callyaerins as antitubercular agents targeting the M. tuberculosis-specific protein Rv2113, showing efficacy against drug-resistant strains with minimal cytotoxicity.

bioRxiv · Jul 12, 2023 · PreprintMicrobiology

UNC-45 assisted myosin folding depends on a conserved FX3HY motif implicated in Freeman Sheldon Syndrome

A. Vogel, R. Arnese, R. Gudino Carrillo, D. Sehr, A. Bylicki, A. Meinhart, T. Clausen

This study identifies the FX3HY motif as essential for UNC-45-mediated myosin folding, linking its disruption to Freeman Sheldon Syndrome and myopathies.

bioRxiv · Aug 8, 2022Biochemistry