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Marie Olšinová

Researcher at Charles University in Prague

Publications -  12
Citations -  255

Marie Olšinová is an academic researcher from Charles University in Prague. The author has contributed to research in topics: Membrane & Transmembrane protein. The author has an hindex of 5, co-authored 11 publications receiving 160 citations. Previous affiliations of Marie Olšinová include Academy of Sciences of the Czech Republic.

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Reactivation of Dihydroorotate Dehydrogenase-Driven Pyrimidine Biosynthesis Restores Tumor Growth of Respiration-Deficient Cancer Cells.

TL;DR: It is shown that pyrimidine biosynthesis dependent on respiration-linked dihydroorotate dehydrogenase (DHODH) is required to overcome cell-cycle arrest, while mitochondrial ATP generation is dispensable for tumorigenesis, pointing to inhibitors of DHODH as potential anti-cancer agents.
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Peripheral and Integral Membrane Binding of Peptides Characterized by Time-Dependent Fluorescence Shifts: Focus on Antimicrobial Peptide LAH4

TL;DR: These experiments suggest that the time-dependent fluorescence shift (TDFS) of Laurdan can help when distinguishing between peripheral and integral membrane binding and can be a useful, novel tool for studying the impact of transmembrane peptides (TMP) on membrane organization under near-physiological conditions.
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Di- and tri-oxalkyl derivatives of a boron dipyrromethene (BODIPY) rotor dye in lipid bilayers.

TL;DR: The limits of BODIPY-based molecular rotors as environmental sensors in cellular membranes with complex lipid composition are demonstrated and the results strongly indicate that fluorescence properties of such probes are influenced not only by lipid packing but also by the orientation of the probe in membranes.
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Expansion microscopy facilitates quantitative super-resolution studies of cytoskeletal structures in kinetoplastid parasites

TL;DR: Expansion microscopy (ExM) has become a powerful super-resolution method in cell biology as mentioned in this paper, which does not require any instrumentation or reagents beyond those present in a standard microscopy facility.
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Roughness of Transmembrane Helices Reduces Lipid Membrane Dynamics.

TL;DR: Using synthetic peptides, it is demonstrated that transmembrane helices interfere with the mobility of membrane components by trapping lipid acyl chains on their rough surfaces, suggesting that roughness is a general property of helical trans Membrane segments that affects local membrane dynamics and organization.