Michele Vendruscolo

This study shows melanin suppresses Aβ42 aggregation and toxicity in vitro and in a cell model, suggesting potential therapeutic applications for Alzheimer's disease.

This paper introduces a new spectral single-molecule microscopy technique using spatially patterned detectors, achieving spectral and positional resolution without complex optical components.

This study shows that complex coacervation changes tau aggregation by redirecting it to a distinct kinetic regime and altering amyloid properties.

This paper develops a method to isolate holocellulose nanofibrils that preserves native cellulose-xylan architecture, leading to high-performance sustainable materials.

This paper predicts antibody non-specificity using protein language models and biophysical parameters, showing that heavy variable domains and isoelectric point are key predictors.

The paper evaluates how specific PTMs affect tau protein aggregation using HCG and atomistic MD simulations, showing their impact on structural properties and aggregation behavior.

This study shows that disordered protein sequences encode characteristic small molecule binding pathways, identified through molecular dynamics simulations and machine learning.

The paper identifies microglial transcriptional programs as predictors of inter-individual variation in neuronal aging using single-nucleus RNA sequencing data from 226 adults.

The paper identifies metabolite-specific failure thresholds in yeast linked to network topology, solubility, and translational control, revealing mechanisms of metabolic toxicity and resilience.

This study shows human iPSC-derived microglia uptake and process tau fibrils, leading to secretion in extracellular vesicles that can seed tau aggregation in neurons.

OmniBind predicts small-molecule promiscuity across the human proteome using a neural network, enabling faster early-stage drug screening with improved specificity over affinity alone.

The paper maps the alpha-synuclein proteostasis network in Parkinson's disease, defines a proteostasis activity score, and applies it to drug repurposing and target identification.

This study shows that structural defects in amyloid-β fibrils are key sites for secondary nucleation, suggesting new strategies for drug design to inhibit amyloid disorders.

This study uses mouse models with tau mutations to show two distinct pathogenic mechanisms in tauopathies, with different progression patterns and responses to amyloid.

Metadiffusion introduces a meta-energy biasing layer to diffusion models to generate diverse biomolecular conformations without retraining, matching molecular dynamics simulations.

This study identifies helix III destabilization as the initial trigger for SAA1-76 misfolding by exposing its amyloidogenic core through computational simulations.

This paper introduces a Markov State Model to describe small molecule interactions with disordered proteins, identifying dynamic binding paths and druggable regions.

This study shows Ca2+ induces PDIA6 phase separation, enhancing proinsulin folding and preventing aggregation through recruitment of PDIA3.

This paper introduces ASA-PD, an imaging method to detect and map α-synuclein oligomers in Parkinson's disease brain tissue, revealing a specific subpopulation of nanoscale oligomers as an early hallmark of the disease.

This study investigates tau filament assembly using mutant recombinant tau and brain homogenates, finding that specific mutations produce filaments resembling AD pathology.

This study characterizes the aging behavior of FUS condensates using microfluidic technology and surface-based techniques, revealing phase transitions and structural changes associated with material properties.

The paper develops an in vitro tau aggregation assay combined with machine learning to identify polymorph-specific tau inhibitors, validated in a Drosophila model.

This study identifies secondary nucleation of α-Synuclein as the key mechanism driving mitochondrial dysfunction and Lewy body formation in Parkinson's Disease.

The paper identifies microglial activation and alpha-synuclein oligomers as drivers of early neuroinflammation in Parkinson's disease using transcriptomic and aggregate profiling in early-stage brain samples.

The paper maps α-synuclein oligomers in Parkinson's disease brain tissue to identify aggregation-susceptible cells and proposes a population-level model for early pathology.

The paper uses a conditional diffusion model to design a small molecule inhibitor of secondary nucleation in alpha-synuclein aggregation, showing it effectively inhibits fibril proliferation.

This paper develops a global kinetic model of lipid-induced alpha-synuclein aggregation and identifies how squalamine inhibits this process by reducing lipid-dependent primary nucleation.

This study defines proteostasis signatures across 32 human diseases, revealing disease-specific perturbations, temporal changes, and the impact of smoking on proteostasis.

The paper maps the proteostasis network of membraneless organelles, revealing the role of anabolic components and molecular chaperones in regulating protein conformations.