Abstract
Intracellular deposition of microtubule-associated protein tau in the form of filamentous aggregates is a prominent neuropathological feature of neurodegenerative disorders termed tauopathy. Formation of filamentous tau aggregates is presumably initiated by phosphorylation and/or conformational change of protein structure followed by oligomerization and fibril extension. These processes via intermediate oligomers have not yet been entirely resolved. To examine the biochemical properties of tau protein including oligomers, standardized isolation methods will invariably provide molecular mechanisms of tauopathy. In this chapter, we describe the procedures for isolating tau oligomers based on biochemical properties.
Sign-in/Register to access full text options 
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
