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Helge Ewers

Researcher at Free University of Berlin

Publications -  87
Citations -  5053

Helge Ewers is an academic researcher from Free University of Berlin. The author has contributed to research in topics: Microscopy & Super-resolution microscopy. The author has an hindex of 29, co-authored 75 publications receiving 4255 citations. Previous affiliations of Helge Ewers include École Polytechnique Fédérale de Lausanne & King's College London.

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Superresolution imaging of amyloid fibrils with binding-activated probes.

TL;DR: BALM imaging is employed to acquire superresolution images of α-synuclein amyloid fibrils with unprecedented optical resolution and it is proposed that BALM imaging can be extended to study the structure of other amyloids, for differential diagnosis of amyloidal-related diseases and for discovery of drugs that perturbAmyloid structure for therapy.
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Nanoscale Structural Plasticity of the Active Zone Matrix Modulates Presynaptic Function

TL;DR: A model whereby neuronal activity modulates presynaptic function in a homeostatic manner by altering the clustering state of the AZ matrix is proposed, which is inversely correlated with local VGCC recruitment and vesicle cycling.
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Even illumination in total internal reflection fluorescence microscopy using laser light.

TL;DR: The design and construction of an objective‐launch total internal reflection fluorescence microscopy system with excellent evenness of specimen illumination achieved by azimuthal rotation of the incoming illuminating laser beam is reported.
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Probing the dynamics of protein-protein interactions at neuronal contacts by optical imaging.

TL;DR: The present work presents a meta-analysis of FRET and its applications in Protein/Protein Interactions and Fluorescence Lifetime Imaging (FLIM), which aims at determining the mode of action of proteins in response to FRET-like signals.
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Single-molecule microscopy of molecules tagged with GFP or RFP derivatives in mammalian cells using nanobody binders

TL;DR: This work illustrates in detail how to use small, high affinity nanobody binders against GFP and RFP family proteins for highly generic labeling of fusion constructs with bright organic dyes and provides detailed protocols and examples for their application in superresolution imaging and single particle tracking.