Physiological and pathological properties of alpha-synuclein.

@article{Tofaris2007PhysiologicalAP,
  title={Physiological and pathological properties of alpha-synuclein.},
  author={George K Tofaris and Maria Grazia Spillantini},
  journal={Cellular and molecular life sciences : CMLS},
  year={2007},
  volume={64 17},
  pages={2194-201}
}
alpha-Synuclein belongs to a small group of natively unfolded proteins that can transiently bind to lipid membranes and acquire a partial alpha-helical conformation. Under certain pathogenic conditions, alpha-synuclein aggregates to form oligomers and insoluble fibrils with increased ss-sheet configuration. Although genetic mutations and multiplications of the gene have been found in familial cases, the mechanism by which this protein aggregates in sporadic cases of Parkinson's disease… CONTINUE READING

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