M. Vendruscolo

This study uses infrared nanospectroscopy to directly measure how bexarotene interacts with Aβ42 oligomers and fibrils, revealing a single hydrogen bond between the compound's carbonyl group and the aggregates.

This study examines lipid composition and amyloid beta interactions in naked mole-rat brain membranes, finding they are cholesterol-rich, highly phase-separated, and more susceptible to amyloid-induced damage compared to mouse membranes.

This study develops a Markov state model to determine the kinetic ensemble of Aβ42, revealing fast inter-state transitions and predominantly unfolded or short-lived partially-folded states.

This study investigates the dynamics of Aβ42 oligomers during amyloid fibril formation, revealing that most oligomers dissociate into monomers rather than forming fibrils.

This study uses kinetic analysis and binding measurements to compare four anti-Aβ antibodies, showing aducanumab uniquely reduces Aβ oligomer flux.

This study develops a kinetic theory to identify thermodynamic and kinetic signatures of effective protein aggregation inhibitors.

The paper quantifies protein supersaturation in muscle biopsies from PAM patients, showing it escalates near pathological inclusions and correlates with aggregation.

The paper measures proteome solubility changes in Neuro2a cells under various protein homeostasis stresses and finds widespread remodelling with specific patterns of solubility shifts.

This study uses cryo-EM and molecular dynamics to show that α-tubulin acetylation at K40 reduces loop disorder and may affect microtubule stability.

This study uses fast TG-FLIM to analyze α-synuclein and polyglutamine aggregation in aging C. elegans, revealing differences in their aggregation kinetics and amyloid-like features.

This study refines the native state ensemble of NCBD using chemical shifts and NOEs to accurately model its conformational dynamics.