Georg Meisl

This study identifies two distinct amyloid-β intermediates that drive Alzheimer's pathology and shows their suppression reduces plaque burden and improves cognition in mice.

This study designs de novo proteins that selectively inhibit alpha-synuclein aggregation by targeting specific intermediates, with one binder preferentially inhibiting oligomer formation and secondary nucleation.

The paper shows TNFα promotes tau aggregation at pre-synapses in human neurons, forming non-fibrillar aggregates that replicate rapidly.

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.

The paper identifies disease-specific molecular profiles of small tau aggregates across different tauopathies using single-molecule assays.

The paper examines tau aggregates in Alzheimer's disease synaptosomes, finding that small tau aggregates are associated with early synaptic pathology.

This study shows tau proteins from Alzheimer's and CTE folds catalyze Aβ42 aggregation in a fold-specific manner, increasing toxicity and offering new therapeutic insights.

The paper identifies rare bioactive tau oligomers in Alzheimer's brain that can induce templated misfolding and fibril formation, distinguishing them from non-bioactive oligomers.

The paper uses super-resolution microscopy and SIMOA to analyze alpha-synuclein aggregates in Parkinson's disease brain samples and mouse models, finding larger aggregates in PD samples and differences based on extraction methods.

The paper identifies a cellular tipping point between aggregate accumulation and removal as a universal feature of neurodegeneration, validated through live-cell assays and super-resolution imaging.

The paper introduces a method to link single-cell imaging and gene expression data through multimodal droplet barcoding, identifying genes correlated with phenotypic features.

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 investigates how inhibiting disulphide bonding in truncated tau affects its self-assembly into seed-competent structures, revealing enhanced aggregation rates and implications for tauopathy research.

SynPull combines single-molecule pulldown, super-resolution microscopy, and computational analysis to study protein aggregates in synaptosomes from human and mouse samples, revealing AT8-positive tau as the predominant aggregate in Alzheimer's disease.

The paper designs peptide traps that bind amyloidogenic segments in {beta}-strand and {beta}-hairpin conformations, effectively blocking fibril assembly for A{beta}42.

This study identifies an H-latch conformational switch in PrPC that drives prion toxicity and shows that disrupting this switch can protect against prion-related neurodegeneration.