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Daniel Klaue

Researcher at Dresden University of Technology

Publications -  11
Citations -  1021

Daniel Klaue is an academic researcher from Dresden University of Technology. The author has contributed to research in topics: Magnetic field & DNA supercoil. The author has an hindex of 8, co-authored 10 publications receiving 843 citations.

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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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Energetics at the DNA Supercoiling Transition

TL;DR: It is found that for a kinked DNA molecule the abrupt extension change occurs at significantly lower twist than the subsequent superhelix formation, which should allow pinning of the plectoneme position within supercoiled DNA if a kinky substrate is used, and enable the detection of enzymes and proteins which, themselves, bend or kink DNA.
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Camera-based three-dimensional real-time particle tracking at kHz rates and Ångström accuracy

TL;DR: This work demonstrates that camera-based imaging can provide a similar performance for all three dimensions of particle tracking with Ångström accuracy as laser detection through photodiodes, and provides a simple and robust way for high-resolution tweezers experiments using multiple particles at a time.
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Torsional Stiffness of Single Superparamagnetic Microspheres in an External Magnetic Field

TL;DR: By investigating the axial fluctuations of DNA-bound microspheres, it is found that considerable rotational microsphere fluctuations can occur and Quantitative noise analysis allowed us to determine the rotational stiffness of individual micro spheres, which was found to saturate at high magnetic fields.
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Nuclease activity of Saccharomyces cerevisiae Dna2 inhibits its potent DNA helicase activity

TL;DR: The nuclease of Dna2 inhibits its helicase by cleaving 5′ flaps that are required by the helicase domain for loading onto its substrate, which limits and controls the enzyme's capacity to unwind dsDNA.