N-terminal fragments of tau inhibit full-length tau polymerization in vitro.

@article{Horowitz2006NterminalFO,
  title={N-terminal fragments of tau inhibit full-length tau polymerization in vitro.},
  author={Peleg Horowitz and N Lapointe and Angela L. Guillozet-Bongaarts and Robert W. Berry and Lester I. Binder},
  journal={Biochemistry},
  year={2006},
  volume={45 42},
  pages={12859-66}
}
The polymerization of the microtubule-associated protein, tau, into insoluble filaments is a common thread in Alzheimer's disease and in a variety of frontotemporal dementias. The conformational change required for tau to transition from an extended monomeric state to a filamentous state with a high beta-sheet content involves the extreme N-terminus coming into contact with distal portions of the molecule; however, these exact interactions are incompletely understood. Here we report that a… CONTINUE READING

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