Distinct differences in prion-like seeding and aggregation between Tau protein variants provide mechanistic insights into tauopathies.

@article{Strang2018DistinctDI,
  title={Distinct differences in prion-like seeding and aggregation between Tau protein variants provide mechanistic insights into tauopathies.},
  author={Kevin H. Strang and Cara L Croft and Zachary A. Sorrentino and Paramita Chakrabarty and Todd E Golde and Benoit I Giasson},
  journal={The Journal of biological chemistry},
  year={2018},
  volume={293 7},
  pages={
          2408-2421
        }
}
The accumulation of aberrantly aggregated MAPT (microtubule-associated protein Tau) defines a spectrum of tauopathies, including Alzheimer's disease. Mutations in the MAPT gene cause frontotemporal dementia with Parkinsonism linked to chromosome 17 (FTDP-17), characterized by neuronal pathological Tau inclusions in the form of neurofibrillary tangles and Pick bodies and in some cases glial Tau pathology. Increasing evidence points to the importance of prion-like seeding as a mechanism for the… CONTINUE READING
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