Justin L. P. Benesch

This paper introduces a method for continuous mass photometry of single molecules, enabling long-term observation of biomolecular interactions with high mass precision and temporal resolution.

This study develops an integrated mass spectrometry strategy to quantify the proteoform diversity of O-glycoprotein osteopontin, revealing systematic underestimation of glycan sialylation by bottom-up methods.

The paper studies the evolution of the RNA exosome, showing how an ancient active RNase evolved into a regulatory hub coordinating sequential RNase activities.

This paper introduces a method using mass photometry with supported lipid bilayers to detect and measure proteins in complex mixtures without prior purification.

This paper introduces modular DNA nanosensors that enable label-free, multiplexed single-molecule mass photometry to resolve protein biochemical states in complex media without washing or immobilisation.

This paper introduces a deep learning method to classify mass photometry events, improving single-molecule mass measurement accuracy by reducing artifacts and enhancing resolving power.

This paper provides guidelines for optimizing mass photometry to achieve high mass resolution and detection limits while maintaining simplicity.

This study investigates the light-induced conformational changes in Drosophila cryptochrome using simulations and spectroscopy, revealing a blue-light induced state that may mediate signal transduction.

The paper investigates how cardiac stress regulates Filamin C dimerisation through phosphorylation-modulated interactions with HSPB7, revealing evolutionary conservation of this mechanism.

This paper introduces native ES-IBD for preparing high-purity, ice-free cryo-EM samples, showing structural integrity but limitations in 2D classes and 3D EM density maps.

The paper shows that dimeric subunits of sHsps are functional units for substrate capture, and that dimer stability affects chaperone efficiency.

This study identifies how αB-crystallin inhibits amyloid formation by destabilizing aggregation nuclei using NMR and chemical kinetics.