Abstract
In this review, we focus on what we have learned from Nuclear Magnetic Resonance (NMR) studies on the neuronal microtubule-associated protein Tau. We consider both the mechanistic details of Tau: the tubulin relationship and its aggregation process. Phosphorylation of Tau is intimately linked to both aspects. NMR spectroscopy has depicted accurate phosphorylation patterns by different kinases, and its non-destructive character has allowed functional assays with the same samples. Finally, we will discuss other post-translational modifications of Tau and its interaction with other cellular factors in relationship to its (dys)function.
| Original language | English |
|---|---|
| Article number | 28 |
| Journal | Biomolecules |
| Volume | 6 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - 06-2016 |
All Science Journal Classification (ASJC) codes
- Biochemistry
- Molecular Biology