Laboratory-based methods are presented that produce filamentous tau aggregates with the same structures as those observed in neurodegenerative disease.

Major cell types across various brain regions distinctively associate with tissue loss in 13 neurodegenerative conditions.

Tau protein exists as two conformational ensembles, one inert, and another that has intrinsic properties of self-association, triggers seeding in cells and in vitro, and is associated with Alzheimer's disease.

Tau monomer from aggregate-containing cell models and tauopathy brains adopts discrete structures that act as templates, dictating the conformation of distinct strains that result from its seeding activity.

Liquid-liquid phase separation of tau is demonstrated to be an equilibrium state, stable only within a narrow range near physiological conditions, and thus has the capacity to regulate biological processes.

Convergent screens targeting the levels of alpha-synuclein and tau identify TRIM28 as a driver of their stability, nuclear accumulation and subsequent toxicity.

Amphiphysin I is identified as a new substrate of AEP, and the resultant fragment induces synaptic dysfunction and promotes tau hyperphosphorylation via activating CDK5 kinase.

Aberrant ERK/MAPK signaling in cortical pyramidal neurons leads to selective disruption of layer 5 circuit development and generalized changes in neuronal excitability.

A traumatic brain injury model is invented for larval zebrafish and applied to a new fluorescent 'tauopathy reporter fish', revealing a role for seizures in progression towards dementias.

Mechanistic insight into the chaperone-like activity of NMNAT to phosphorylated Tau reveals a connection between NAD⁺metabolism and Tau homeostasis.