By binding to Fc gamma receptor IIb, amyloid beta induces a series of phosphorylation events that mediate the damaging effects of hyperphosphorylated tau proteins in Alzheimer's disease.

Tau proteins can convert from an inert shape to a misfolded shape that seeds the growth of fibers that contribute to the pathology of Alzheimer's disease.

Super-resolution imaging reveals that the microtubule-associated protein Tau regulates the Fyn kinase organisation in dendrites, and that the frontotemporal dementia mutant Tau promotes aberrant Fyn clustering, potentially leading to synaptic dysfunction.

Bioinformatics and experimental approaches identify families of membrane proteins requiring the co-ordinated action of the Sec pathway and Tat pathways for their integration and define features of the polypeptides that mediate interaction with these pathways.

AFF4 increases the combined selectivity of HIV Tat and TAR for super elongation complexes 330-fold over P-TEFb alone.

The amyloid patterns overlap with the default-mode network, whereas the tau patterns overlap with distinct functional networks and are associated with a loss of anatomical connectivity and multiple cognitive functions.

A prominent model for the structural organisation of the Tat (twin-arginine translocase) protein transport system fails live cell tests.

Evolutionary bioinformatics and experimentation are applied to the components of the Tat protein transport system to elucidate the structure of the membrane-bound receptor complex and to deduce a molecular description for its substrate-triggered activation.

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.

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