Matthew W. Cotton

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.

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.