• DOI:10.1097/00001756-199604100-00024
Corpus ID: 45520472

Preservation of native conformation during aluminium‐induced aggregation of tau protein

@article{Madhav1996PreservationON,
  title={Preservation of native conformation during aluminium‐induced aggregation of tau protein},
  author={T. Madhav and S. Vatsala and T. Ramakrishna and J. Ramesh and K. Easwaran},
  journal={NeuroReport},
  year={1996},
  volume={7},
  pages={1072–1076}
}

• T. Madhav, S. Vatsala, +2 authors K. Easwaran
• Published 1996
• Chemistry, Medicine
• NeuroReport

ALUMINIUM exposure has been shown to result in aggregation of microtubule-associated protein tau in vitro. In the light of recent observations that the native random structure of tau protein is maintained in its monomeric and dimeric states as well as in the paired helical filaments characteristic of Alzheimer's disease, it is likely that factors playing a causative role in neurofibrillary pathology would not drastically alter the native conformation of tau protein. We have studied the… Expand

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