Author

T. Schirmeister

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 Cell Biology· 1 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:drug response / drug discovery· 2 Research Focus:host-pathogen & immune response· 1 Organism:human· 1 Assay:metabolomics· 1 Research Focus:protein folding & dynamics· 1 Assay:structural biology· 1

Frequent Co-Authors

C. Kersten· 2 shared U. A. Hellmich· 2 shared A. Bauer· 1 shared A. Vilcinskas· 1 shared D. Bender· 1 shared E. Hildt· 1 shared E. Jaenicke· 1 shared H. Neuweiler· 1 shared

Activity by Year

2020-2024 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 18 mutual co-author links

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2 shared papersMicrobiology

C. Kersten

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Late stages of the Zika virus life cycle are impaired by a selective TRPML2 agonist

K. K. Schwickert, M. Glitscher, D. Bender, R. Murra, K. Schwickert, S. Pfalzgraf, T. Schirmeister, U. A. Hellmich, E. Hildt

This study shows that the TRPML2 agonist ML2-SA1 inhibits late stages of Zika virus replication by affecting genome replication and intracellular cholesterol distribution.

bioRxiv · Feb 1, 2024 · PreprintCell Biology

Identification, Characterization and Synthesis of Natural Parasitic Cysteine Protease Inhibitors -- More Potent Falcitidin Analogs

S. Brinkmann, S. Semmler, C. Kersten, M. A. Patras, M. Kurz, N. Fuchs, S. J. Hammerschmidt, J. Legac, P. E. Hammann, A. Vilcinskas, P. J. Rosenthal, T. Schirmeister, A. Bauer, T. F. Schaeberle

The paper identifies and synthesizes natural falcitidin analogs with enhanced inhibitory activity against parasitic cysteine proteases.

bioRxiv · Oct 30, 2021 · PreprintMicrobiology

Structure, interdomain dynamics and pH-dependent autoactivation of pro-rhodesain, the main lysosomal cysteine protease from African trypanosomes

P. Johe, E. Jaenicke, H. Neuweiler, T. Schirmeister, C. Kersten, U. A. Hellmich

This study determines the crystal structure of pro-rhodesain, identifies interdomain dynamics, and reveals a pH-dependent autoactivation mechanism in trypanosomal cathepsin L-like proteases.

bioRxiv · Nov 10, 2020Biochemistry