Parkinson-causing α-synuclein missense mutations shift native tetramers to monomers as a mechanism f...
Parkinson-causing α-synuclein missense mutations shift native tetramers to monomers as a mechanism for disease initiation
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London: Nature Publishing Group UK
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English
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London: Nature Publishing Group UK
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β-Sheet-rich α-synuclein (αS) aggregates characterize Parkinson’s disease (PD). αS was long believed to be a natively unfolded monomer, but recent work suggests it also occurs in α-helix-rich tetramers. Crosslinking traps principally tetrameric αS in intact normal neurons, but not after cell lysis, suggesting a dynamic equilibrium. Here we show tha...
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Parkinson-causing α-synuclein missense mutations shift native tetramers to monomers as a mechanism for disease initiation
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TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4490410
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https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4490410
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ISSN
2041-1723
E-ISSN
2041-1723
DOI
10.1038/ncomms8314
