Z. F. Brotzakis

This paper shows that AlphaFold can predict structural ensembles for disordered proteins by using inter-residue distances.

This study uses MEMMI to analyze the transient interactions between the fuzzy coat and cross-β core of Aβ42 filaments, revealing differences in solubility between familial and sporadic AD forms.

This paper introduces a single-molecule method using solid-state nanopores and DNA barcoding to detect and characterize misfolded protein oligomers, demonstrating its application to α-synuclein in Parkinson's disease.

This study identifies small molecules that inhibit alpha-synuclein aggregate proliferation using structure-based and kinetic assays.

The paper develops MEMMI, a cryo-EM method that determines structure and dynamics of large systems, and applies it to study the fuzzy coat of an IAPP amyloid fibril.

This paper uses structure-based machine learning to identify potent small molecule inhibitors of α-synuclein aggregation, achieving compounds two orders of magnitude more potent than previous reports.

This study investigates protein aggregation in SARS-CoV and SARS-CoV-2 proteomes, finding that several SARS-CoV-2 proteins form cytotoxic aggregates via a nucleation-dependent mechanism.

The paper determines the structural ensemble of a tau-microtubule complex using cryo-EM, revealing phosphorylation and acetylation sites that destabilize the complex.

This study predicts ligand binding modes and computes binding free energy and unbinding rates using a novel combination of computational methods, revealing water and solvation as dominant slow degrees of freedom.

The paper uses a variational approach to metadynamics to study conformational transitions in L99A T4 Lysozyme, identifying two intermediate states with reduced computational cost.