Michele Vendruscolo

Professor

University of Cambridge

United Kingdom

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Professor Michele Vendruscolo is a faculty member at the University of Cambridge in the United Kingdom. His research focuses on protein aggregation and interactions related to neurodegenerative diseases, particularly Alzheimer's and synucleinopathies. Recent articles authored by Professor Vendruscolo explore topics such as tau filament amplification, intermolecular interactions in aging proteins, and the modulation of phase separation by amyloid-beta. He is actively involved in advancing our understanding of proteostasis and its implications for human health.

Articles (20)

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2025

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2023

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2023

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2023

Collaborators (16)

Tuomas Knowles

Professor of Physical Chemistry and Biophysics

University of Cambridge

UNITED KINGDOM

Michele Vendruscolo

Research Interests

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Articles (20)

Nanoscale profiling of evolving intermolecular interactions in ageing FUS condensates

Natural aminosterols inhibit <scp>NMDA</scp> receptors with low nanomolar potency

Serial amplification of tau filaments using Alzheimer's brain homogenates and C322A or C322S recombinant tau

Recruitment of Aβ into α-Synuclein Condensates Catalyzes Primary Nucleation of α-Synuclein Aggregation

Targeted Protein Modification with an Antibody-Based System

Sequence-based virtual screening using transformers

Aβ42 promotes the aggregation of α‐synuclein splice isoforms via heterogeneous nucleation

Amyloid-β modulates the phase separation and aggregation of α-synuclein

Proteostasis signatures in human diseases

The thermodynamic hypothesis of protein aggregation

Amyloid formation as a protein phase transition

Spontaneous nucleation and fast aggregate-dependent proliferation of α-synuclein aggregates within liquid condensates at neutral pH

FuzPred: a web server for the sequence-based prediction of the context-dependent binding modes of proteins

Formation of amyloid loops in brain tissues is controlled by the flexibility of protofibril chains

Characterization of Pairs of Toxic and Nontoxic Misfolded Protein Oligomers Elucidates the Structural Determinants of Oligomer Toxicity in Protein Misfolding Diseases

Secondary Processes Dominate the Quiescent, Spontaneous Aggregation of α-Synuclein at Physiological pH with Sodium Salts

Determination of the Structure and Dynamics of the Fuzzy Coat of an Amyloid Fibril of IAPP Using Cryo-Electron Microscopy

Thermodynamic and kinetic approaches for drug discovery to target protein misfolding and aggregation

Exploration and Exploitation Approaches Based on Generative Machine Learning to Identify Potent Small Molecule Inhibitors of α-Synuclein Secondary Nucleation

Sequence-based prediction of pH-dependent protein solubility using CamSol

Collaborators (16)

Tuomas Knowles

Peter M. Tessier

M Bonomi

Giulia Fani

Silvio Tosatto

Maarten Hardenberg

Thomas Michaels

Monika Fuxreiter

Francesco Simone Ruggeri

David Klenerman

Daoyuan Qian

Fabrizio Chiti

Nunilo Cremades

Ryan Limbocker

Andela Saric

Sara Linse

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