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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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High-speed single-particle tracking of GM1 in model membranes reveals anomalous diffusion due to interleaflet coupling and molecular pinning.

TL;DR: It is shown that molecular pinning and interleaflet coupling between lipid tail domains on a nanoscopic scale suffice to induce transient immobilization and thereby anomalous subdiffusion on the millisecond time scale.
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Nanoscopic compartmentalization of membrane protein motion at the axon initial segment.

TL;DR: A new mechanistic model for the AIS diffusion barrier is proposed using single-particle tracking time course experiments and it is shown that the mobility of lipid-anchored molecules in the A IS is enriched in specific molecules.
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Unblending of transcriptional condensates in human repeat expansion disease

TL;DR: A molecular classification of TF IDRs is presented, which provides a framework to dissect TF function in diseases associated with transcriptional dysregulation and suggests that unblending of transcriptional condensates may underlie human pathologies.
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A Septin-Dependent Diffusion Barrier at Dendritic Spine Necks

TL;DR: It is found that, during development, a marker of the septin complex, Septin7 (Sept7), becomes localized to the spine neck where it forms a stable structure underneath the plasma membrane, which indicates that Sept7 regulates membrane protein access to spines.
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Label-Free Optical Detection and Tracking of Single Virions Bound to Their Receptors in Supported Membrane Bilayers

TL;DR: An interferometric optical detection scheme is applied to image and track unlabeled single virions and promises to be generally applicable to studying the motion of unlabeling macromolecules on membranes.