Louise C. Serpell

The paper investigates the proteomic response in neuronal cells after exposure to a tau fragment, identifying pathways linked to tau pathology development.

This paper investigates the structure of amyloid fibrils formed by the human tau-derived hexapeptide VQIVYK, revealing a polymorphous population with a twisted protofilament architecture.

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.

The paper shows that HCN channel dysfunction is linked to tauopathies, with altered synaptic structure and function in Alzheimer's and Tau35 mouse models.

This study describes a de novo designed polypeptide that forms phase-separated droplets and fibers, showing droplet maturation into β-conformations similar to pathological assemblies.

The paper uses optical reporters to show that Aβ42 oligomers disrupt the endo-lysosomal pathway by impairing protein uptake and causing lysosomal accumulation.