Dynamics of α‐synuclein aggregation and inhibition of pore‐like oligomer development by β‐synuclein

@inproceedings{Tsigelny2007DynamicsO,
  title={Dynamics of α‐synuclein aggregation and inhibition of pore‐like oligomer development by β‐synuclein},
  author={Igor F. Tsigelny and Pazit Bar-On and Yuriy Sharikov and Leslie Crews and Makoto Hashimoto and Mark A. Miller and Steve Keller and Oleksandr Platoshyn and Jason X.-J. Yuan and Eliezer Masliah},
  year={2007}
}
Accumulation of α-synuclein resulting in the formation of oligomers and protofibrils has been linked to Parkinson's disease and Lewy body dementia. In contrast, β-synuclein (β-syn), a close homologue, does not aggregate and reduces α-synuclein (α-syn)-related pathology. Although considerable information is available about the conformation of α-syn at the initial and end stages of fibrillation, less is known about the dynamic process of α-syn conversion to oligomers and how interactions with… CONTINUE READING

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