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The inhibitory action of the chaperone BRICHOS against the α-Synuclein secondary nucleation pathway

Here, the authors probe the mechanism of secondary nucleation inhibition of the BRICHOS domain of the lung surfactant protein (proSP-C) against α-Syn aggregation and amyloid formation using NMR and super-resolution fluorescence microscopy.

Dhiman Ghosh
Felix Torres
Roland Riek
ResearchOpen Access20 Nov 2024
Nature Communications

Volume: 15, P: 1-15
NMR and EPR reveal a compaction of the RNA-binding protein FUS upon droplet formation

An agarose hydrogel mimicking cytoskeleton stabilizes protein liquid droplets and enables precise quantification of protein percentage in phase-separated droplets and in the dispersed phases as well as intramolecular distances via NMR and EPR.

Leonidas Emmanouilidis
Laura Esteban-Hofer
Frédéric H.-T. Allain
Research08 Mar 2021
Nature Chemical Biology

Volume: 17, P: 608-614
Localized detection of ions and biomolecules with a force-controlled scanning nanopore microscope

Nanopore AFM is used for the stochastic sensing of secreted molecules and the activity of ion channels in arbitrary locations both inside and outside a cell.

Morteza Aramesh
Csaba Forró
János Vörös
Research15 Jul 2019
Nature Nanotechnology

Volume: 14, P: 791-798
Direct PIP₂ binding mediates stable oligomer formation of the serotonin transporter

The human serotonin transporter (SERT) mediates the uptake of neurotransmitters to terminate neuronal signalling. Here the authors use single-molecule imaging to get insight into the molecular origin of SERT oligomerization and their pre-set stoichiometry at the plasma membrane.

Andreas Anderluh
Tina Hofmaier
Gerhard J. Schütz
ResearchOpen Access19 Jan 2017
Nature Communications

Volume: 8, P: 1-9
Temporal analysis of T-cell receptor-imposed forces via quantitative single molecule FRET measurements

Mechanical forces acting on ligand-engaged T-cell receptors (TCRs) have previously been implicated in T-cell antigen recognition, yet their sensitivity and specificity are still poorly defined. Here, authors report a FRET-based sensor that informs directly on the magnitude and kinetics of TCR-imposed forces at the single molecule level.

Janett Göhring
Florian Kellner
Gerhard J. Schütz
ResearchOpen Access04 May 2021
Nature Communications

Volume: 12, P: 1-14
Mechanical forces regulate the interactions of fibronectin and collagen I in extracellular matrix

Assembly of a collagen extracellular matrix requires the presence of fibronectin, but the mechanisms that direct this assembly are not known. Here the authors show that collagen I uses relaxed fibronectin fibrils as a template for assembly, and in turn shield fibronectin fibrils from force-mediated stretching.

Kristopher E. Kubow
Radmila Vukmirovic
Viola Vogel
ResearchOpen Access14 Aug 2015
Nature Communications

Volume: 6, P: 1-11
Tuning membrane protein mobility by confinement into nanodomains

Streptavidin crystals grown on mica-supported lipid bilayers can be used as a platform to tune the lateral mobility of transmembrane proteins, allowing the conformation or docking of spatially confined proteins to be imaged with high-speed atomic force microscopy.

Andreas Karner
Benedikt Nimmervoll
Johannes Preiner
Research14 Nov 2016
Nature Nanotechnology

Volume: 12, P: 260-266
Barring the gates to the battleground: DDR1 promotes immune exclusion in solid tumors

Dimitrios L. Wagner
Enrico Klotzsch
Research HighlightsOpen Access13 Jan 2022
Signal Transduction and Targeted Therapy

Volume: 7, P: 1-2

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