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Astrid Schauss
Researcher at University of Cologne
Publications - 56
Citations - 3621
Astrid Schauss is an academic researcher from University of Cologne. The author has contributed to research in topics: Mitochondrion & Mitochondrial fission. The author has an hindex of 25, co-authored 50 publications receiving 2832 citations. Previous affiliations of Astrid Schauss include University of Ottawa & Max Planck Society.
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Journal ArticleDOI
The i-AAA protease YME1L and OMA1 cleave OPA1 to balance mitochondrial fusion and fission
Ruchika Anand,Timothy Wai,Michael J. Baker,Nikolay Kladt,Astrid Schauss,Elena I. Rugarli,Thomas Langer,Thomas Langer +7 more
TL;DR: OPA1 processing by YEM1L and OMA1 is dispensable for mitochondrial fusion and instead drives mitochondrial fragmentation, which is crucial for mitochondrial integrity and quality control.
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Cargo-selected transport from the mitochondria to peroxisomes is mediated by vesicular carriers.
Margaret Neuspiel,Astrid Schauss,Emelie Braschi,Rodolfo Zunino,Peter Rippstein,Richard A. Rachubinski,Miguel A. Andrade-Navarro,Heidi M. McBride +7 more
TL;DR: The data are the first to identify MAPL, describe and characterize MDVs, and define a new intracellular transport route between mitochondria and peroxisomes, marking the first evidence for a direct relationship between these two functionally related organelles.
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Extracellular vesicle measurements with nanoparticle tracking analysis – An accuracy and repeatability comparison between NanoSight NS300 and ZetaView
Daniel Bachurski,Maximiliane Schuldner,Phuong Hien Nguyen,Alexandra Malz,Katrin S. Reiners,Patricia C. Grenzi,Felix Babatz,Astrid Schauss,Hinrich P. Hansen,Michael Hallek,Elke Pogge von Strandmann +10 more
TL;DR: ZetaView provided a more accurate and repeatable depiction of EV concentration, whereas NanoSight NS300 supplied size measurements of higher resolution that failed to report a peak EV diameter below 60 nm compared to TEM and SP-IRIS.
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The SUMO protease SENP5 is required to maintain mitochondrial morphology and function
TL;DR: It is demonstrated that the cytosolic pool of SENP5 catalyzes the cleavage of SUMO1 from a number of mitochondrial substrates, impacting mitochondrial morphology and metabolism.
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A novel multiplex bead-based platform highlights the diversity of extracellular vesicles
Nina Koliha,Yvonne Wiencek,Ute Heider,Christian Jüngst,Nikolay Kladt,Susanne Krauthäuser,Ian C.D. Johnston,Andreas Bosio,Astrid Schauss,Stefan Wild +9 more
TL;DR: A novel multiplex bead-based platform to investigate up to 39 different surface markers in one sample and show for the first time that NK cell–derived EVs and platelet-derived EVs are devoid of CD9 or CD81, respectively, and that EVs isolated from activated B cells comprise different EV subpopulations.