Proteasomal inhibition by alpha-synuclein filaments and oligomers.

@article{Lindersson2004ProteasomalIB,
  title={Proteasomal inhibition by alpha-synuclein filaments and oligomers.},
  author={Evo K Lindersson and Rasmus Beedholm and Peter H{\o}jrup and Torben Moos and Weiping Gai and Klavs B. Hendil and Poul Henning Jensen},
  journal={The Journal of biological chemistry},
  year={2004},
  volume={279 13},
  pages={
          12924-34
        }
}
A unifying feature of many neurodegenerative disorders is the accumulation of polyubiquitinated protein inclusions in dystrophic neurons, e.g. containing alpha-synuclein, which is suggestive of an insufficient proteasomal activity. We demonstrate that alpha-synuclein and 20 S proteasome components co-localize in Lewy bodies and show that subunits from 20 S proteasome particles, in contrast to subunits of the 19 S regulatory complex, bind efficiently to aggregated filamentous but not monomeric… CONTINUE READING

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