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Elisabeth Fischer-Friedrich

Researcher at Dresden University of Technology

Publications -  43
Citations -  2628

Elisabeth Fischer-Friedrich is an academic researcher from Dresden University of Technology. The author has contributed to research in topics: Biology & Actin. The author has an hindex of 17, co-authored 33 publications receiving 2009 citations. Previous affiliations of Elisabeth Fischer-Friedrich include Weizmann Institute of Science & Max Planck Society.

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Real-time deformability cytometry: on-the-fly cell mechanical phenotyping

TL;DR: Real-time deformability cytometry (RT-DC) is introduced for continuous cell mechanical characterization of large populations with analysis rates greater than 100 cells/s and adds a new marker-free dimension to flow cytometry with diverse applications in biology, biotechnology and medicine.
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Spatial regulators for bacterial cell division self-organize into surface waves in vitro.

TL;DR: A reaction-diffusion model of the MinD and MinE dynamics is presented that accounts for the experimental observations and also captures the in vivo oscillations and formed planar surface waves on a flat membrane in vitro.
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Extracting Cell Stiffness from Real-Time Deformability Cytometry: Theory and Experiment

TL;DR: This work disentangle mutual contributions of cell size and cell stiffness to cell deformation by a theoretical analysis in terms of hydrodynamics and linear elasticity theory and demonstrates that the analytical model not only predicts deformed shapes inside the channel but also allows for quantification of cell mechanical parameters.
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Min protein patterns emerge from rapid rebinding and membrane interaction of MinE

TL;DR: It is proposed that protein detachment at the rear of the wave, and the formation of the E-ring, are accomplished by two complementary processes: first, local accumulation of MinE due to rapid rebinding, leading to dynamic instability; and second, a structural change induced by membrane-interaction of Min E in an equimolar MinD–MinE (MinDE) complex, which supports the robustness of pattern formation.