TDP-43 is intrinsically aggregation-prone, and amyotrophic lateral sclerosis-linked mutations accelerate aggregation and increase toxicity.

@article{Johnson2009TDP43II,
  title={TDP-43 is intrinsically aggregation-prone, and amyotrophic lateral sclerosis-linked mutations accelerate aggregation and increase toxicity.},
  author={Brian S Johnson and David B Snead and Jonathan Jun Jie Lee and J. Michael McCaffery and James Shorter and Aaron D Gitler},
  journal={The Journal of biological chemistry},
  year={2009},
  volume={284 30},
  pages={20329-39}
}
Non-amyloid, ubiquitinated cytoplasmic inclusions containing TDP-43 and its C-terminal fragments are pathological hallmarks of amyotrophic lateral sclerosis (ALS), a fatal motor neuron disorder, and frontotemporal lobar degeneration with ubiquitin-positive inclusions (FTLD-U). Importantly, TDP-43 mutations are linked to sporadic and non-SOD1 familial ALS. However, TDP-43 is not the only protein in disease-associated inclusions, and whether TDP-43 misfolds or is merely sequestered by other… CONTINUE READING
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NUMBER 30 JOURNAL OF BIOLOGICAL CHEMISTRY 20339 at U nirsity of P ennylvania

  • E. Yeger-Lotem, L. Riva, +9 authors E. Fraenkel
  • Nat. Genet
  • 2009

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