Pseudophosphorylation and glycation of tau protein enhance but do not trigger fibrillization in vitro.

@article{Necula2004PseudophosphorylationAG,
  title={Pseudophosphorylation and glycation of tau protein enhance but do not trigger fibrillization in vitro.},
  author={Mihaela Necula and Jeff Kuret},
  journal={The Journal of biological chemistry},
  year={2004},
  volume={279 48},
  pages={49694-703}
}
Alzheimer's disease is defined in part by the intraneuronal aggregation of tau protein into filamentous lesions. The pathway is accompanied by posttranslational modifications including phosphorylation and glycation, each of which has been shown to promote tau fibrillization in vitro when present at high stoichiometry. To clarify the site-specific impact of posttranslational modification on tau fibrillization, the ability of recombinant full-length four repeat tau protein (htau40) and 11… CONTINUE READING
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