Glycosylation of microtubule–associated protein tau: An abnormal posttranslational modification in Alzheimer's disease

@article{Wang1996GlycosylationOM,
  title={Glycosylation of microtubule–associated protein tau: An abnormal posttranslational modification in Alzheimer's disease},
  author={Jian-Zhi Wang and Inge Grundke-Iqbal and Khalid Iqbal},
  journal={Nature Medicine},
  year={1996},
  volume={2},
  pages={871-875}
}
Alzheimer's disease (AD) is characterized by the presence of numerous neurons with neurofibrillary tangles of paired helical filaments (PHFs). The microtubule–associated protein tau in abnormally hyperphosphorylated form is the major protein subunit of the PHF. We now show that PHF tangles isolated from AD brains are glycosylated, whereas no glycan is detected in normal tau. Deglycosylation of PHF tangles by endoglycosidase F/N–glycosidase F converts them into bundles of straight filaments 2.5… CONTINUE READING

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