Familial Parkinson disease-associated mutations alter the site-specific microenvironment and dynamics of α-synuclein.

@article{Sahay2015FamilialPD,
  title={Familial Parkinson disease-associated mutations alter the site-specific microenvironment and dynamics of α-synuclein.},
  author={Shruti Sahay and Dhiman Ghosh and Saumya Dwivedi and Arunagiri Anoop and Ganesh Maruti Mohite and Mamata H. Kombrabail and Guruswamy Krishnamoorthy and Samir K Maji},
  journal={The Journal of biological chemistry},
  year={2015},
  volume={290 12},
  pages={7804-22}
}
Human α-synuclein (α-Syn) is a natively unstructured protein whose aggregation into amyloid fibrils is associated with Parkinson disease (PD) pathogenesis. Mutations of α-Syn, E46K, A53T, and A30P, have been linked to the familial form of PD. In vitro aggregation studies suggest that increased propensity to form non-fibrillar oligomers is the shared property of these familial PD-associated mutants. However, the structural basis of the altered aggregation propensities of these PD-associated… CONTINUE READING
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