Thomas C. T. Michaels

This study shows lipidic α-synuclein fibrils catalyze the formation of mature fibrils through a heterogeneous nucleation mechanism, lowering the energy barrier and following Ostwald's Rule of Stages.

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 introduces QuPID-MS to measure protein phase separation in cells, showing weak interactions drive proteome demixing and influence environmental response.

The paper develops a quantitative theory of enzymatic catalysis in phase-separated systems, showing condensates can act as tunable catalytic switches with optimal activity at biologically relevant sizes.

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 shows Ambroxol inhibits α-synuclein-lipid coaggregation by displacing α-synuclein from membranes and preventing early coaggregate formation in GBA mutation models.

This study investigates ATP condensate aging, revealing liquid-to-solid phase transitions and dynamic behaviors like dialytaxis and internal flows driven by the Marangoni effect.

This study shows that nuclear mechanostability arises from satellite DNA condensation into chromocenters, which help dissipate mechanical stress and protect genome integrity.

This study develops an analytical model to describe lipid-induced protein aggregation kinetics, capturing both one-step and two-step nucleation mechanisms and predicting key kinetic observables.

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 paper introduces a theoretical model using Fisher information to explain multicellular aging dynamics, showing non-monotonic behavior based on competition and cooperation balance.

This paper shows that Alzheimer's amyloid-beta peptide forms biomolecular condensates on lipid bilayers, accelerating amyloid aggregation and revealing a new early step in the disease mechanism.

This study reveals that lipids promote α-synuclein aggregation by enabling elongation, using a kinetic model to describe the co-aggregation process in vitro.