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.

Tat uses unexpected regulatory mechanisms to reprogram target immune cells to promote viral replication and rewire pathways beneficial for HIV.

A new Cereblon-recruiting bifunctional tau ligand, QC-01-175, promotes aberrant tau degradation and rescue of stress vulnerability in human neuronal cell models of tauopathy.

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

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.

Tau deposition in the aging brain follows patterns of functional connectivity that correspond to specific neural memory networks, and this relationship is strengthened in the presence of amyloid-β.

Oligomeric Amyloid-β and Tau, two proteins involved in Alzheimer's disease pathogenesis, require Amyloid Precursor Protein to enter neurons and exert their detrimental effect on synaptic plasticity and memory.

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.

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

BIN1 forms a complex with Tau and voltage-gated calcium channels in neurons, and higher BIN1 levels promote neuronal activity, calcium influx, and bursting that is blocked by reducing Tau.