Team TNA

Alzheimer’s disease is the most common form of dementia worldwide, affecting millions of patients, with no therapeutic options available to date. While amyloid plaques have long been recognized as hallmarks of the disease, recent evidence suggests that abnormal post-translational modifications of the Tau protein are strongly involved in disease manifestation and progression. In Alzheimer’s disease, Tau is unable to perform its normal function in the stabilization of microtubules and is prone to hyperphosphorylation, aggregation and secretion.

We study the network of Tau post-translational modifications, interactions between different types of modifications, and their impact on Tau function and dysfunction in the disease state using materials obtained from sporadic Alzheimer’s disease patients as well as neurons derived from induced pluripotent stem cells. Analytical and biochemical approaches and screening methods are used to identify tractable therapeutic targets in Tau post-translational modification pathways that can serve as starting points for the development of therapeutic agents. We aim to define a characteristic signature of pathologic Tau post-translational modifications that will serve as a biomarker to support the diagnosis and monitor the progression of Alzheimer’s disease.

Publications