Author

P. Stettler

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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Cell Biology· 2 Biochemistry· 1

Signature Assays, Organisms & Methods

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Research Focus:cell type annotation· 3 Approach:experimental assay· 2 Organism:human· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:chromatin & epigenetic regulation· 1 Research Focus:development & morphogenesis· 1 Assay:imaging· 1 Approach:microscopy & imaging analysis· 1

Frequent Co-Authors

A. Schneider· 3 shared T. Ochsenreiter· 2 shared A. Harsman· 1 shared A. Kalichava· 1 shared A. Khosrozadeh· 1 shared A. Noga· 1 shared B. D. Engel· 1 shared B. Haenni· 1 shared

Activity by Year

2022-2024 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 23 mutual co-author links

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3 shared papersCell Biology

A. Schneider

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Intermembrane space-localized twin Cx9C motif-containing TbTim15 is an essential subunit of the single mitochondrial inner membrane protein translocase of trypanosomes

C. von Kanel, S. Oeljeklaus, C. Wenger, P. Stettler, A. Harsman, B. Warscheid, A. Schneider

The paper identifies TbTim15 as an essential subunit of the trypanosome TIM complex, showing it mediates import of both presequence-containing and mitochondrial carrier proteins.

bioRxiv · Jan 31, 2024 · PreprintBiochemistry

Cryo-electron tomography sheds light on the largest protein in the Trypanosoma brucei tripartite attachment complex

I. Bregy, R. B. Eberle, J. Radecke, A. Khosrozadeh, J. Llodra, A. Noga, H. van den Hoek, M. Kern, B. Haenni, B. D. Engel, P. Stettler, A. Schneider, C. A. Siebert, T. Ishikawa, B. Zuber, T. Ochsenreiter

This study uses cryo-electron tomography to analyze the tripartite attachment complex in Trypanosoma brucei, revealing the structural dynamics of the complex during kDNA segregation.

bioRxiv · Mar 6, 2023 · PreprintCell Biology

The mitochondrial genome segregation system of T. brucei: Single p197 molecules connect the basal body with the outer membrane

S. Aeschlimann, A. Kalichava, B. Schimanski, P. Stettler, T. Ochsenreiter, A. Schneider

This paper identifies p197 as a key protein bridging the basal body and outer membrane in T. brucei, showing its three domains are essential for mitochondrial DNA segregation.

bioRxiv · Mar 10, 2022 · PreprintCell Biology