Mechanism

Acetylated tau

Assets acting on this target.

Class
Anti-acetylated-tau monoclonal antibody

Tau is a protein that normally stabilizes microtubules, the internal scaffolding that gives neurons their shape and supports transport of materials along axons. Tau's activity is regulated by chemical modifications added after it is made, including acetylation, the attachment of an acetyl group to specific lysine residues. In several neurodegenerative diseases collectively called tauopathies, of which Alzheimer's disease is the most prominent, tau becomes abnormally modified, detaches from microtubules, and misfolds into aggregates that can move from one neuron to another, a process thought to underlie the spread of pathology through the brain. Acetylation at particular sites has been linked to reduced tau turnover and to increased propensity for this pathological aggregation and spreading. An antibody engineered to recognize acetylated tau, rather than tau in general, is designed to selectively capture the disease-associated form circulating outside cells or in the extracellular space, potentially interrupting cell-to-cell transmission and clearing toxic species. This selectivity is intended to leave functionally normal, non-acetylated tau undisturbed, minimizing interference with the protein's ordinary role in supporting microtubules and axonal transport. This mechanism broadly matters for tauopathies where tau pathology tracks with cognitive and functional decline.

Research

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