Abnormal tau phosphorylation at Ser396 in alzheimer's disease recapitulates development and contributes to reduced microtubule binding

@article{Bramblett1993AbnormalTP,
  title={Abnormal tau phosphorylation at Ser396 in alzheimer's disease recapitulates development and contributes to reduced microtubule binding},
  author={Gregory T. Bramblett and Michel Goedert and Ross Jakes and Sandra E. Merrick and John Q. Trojanowski and Virginia M. -Y. Lee},
  journal={Neuron},
  year={1993},
  volume={10},
  pages={1089-1099}
}
Abnormally phosphorylated tau proteins (A68) are the building blocks of Alzheimer's disease (AD) paired helical filaments. The biological consequences of the conversion of normal adult tau to A68 remain unknown. Here we demonstrate that native A68 does not bind to microtubules (MTs), yet dephosphorylated A68 regains the ability to bind to MTs. Ser396 is phosphorylated in A68, but not in normal adult tau, whereas fetal tau is phosphorylated transiently at this site. Phosphorylation of tau at… Expand
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  • M. Goedert, R. Jakes, +6 authors V. Lee
  • Biology, Medicine
  • Proceedings of the National Academy of Sciences of the United States of America
  • 1993
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