Tarun V. Kamath

TL;DR: It is demonstrated that phosphorylated or mutant aggregation prone recombinant tau undergoes LLPS, as does high molecular weight soluble phospho‐tau isolated from human Alzheimer brain, and it is suggested that LLPS represents a biophysical process with a role in multiple different neurodegenerative diseases.

TL;DR: In vivo two-photon Ca2+ imaging of layer 2/3 cortical neurons in mice expressing human Aβ and tau reveals a dramatic tau-dependent suppression of activity and silencing of many neurons, which dominates over Aβ-dependent neuronal hyperactivity.

TL;DR: A molecular analysis of tau from patients with sporadic Alzheimer’s disease reveals striking diversity in biochemical properties between patients, which influences seeding activity and correlates with the aggressiveness of the disease.

TL;DR: This kinetic assay confirms and refines the concept of heterogeneity in the characteristics of tau proteopathic seeds among individuals with Alzheimer’s disease and is a method by which future studies may characterize longitudinal changes in tau aggregation and the cellular processes which may influence these changes.

TL;DR: Testing the hypothesis that heritable factors may influence the rate of propagation of tau pathology across brain regions in a model system in mice found some strains showed more tau spreading than others while tau misfolding accumulated at the same rate in all tested mouse strains.