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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 f...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4490410

Parkinson-causing α-synuclein missense mutations shift native tetramers to monomers as a mechanism for disease initiation

About this item

Full title

Parkinson-causing α-synuclein missense mutations shift native tetramers to monomers as a mechanism for disease initiation

Publisher

London: Nature Publishing Group UK

Journal title

Nature communications, 2015-06, Vol.6 (1), p.7314, Article 7314

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

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...

Alternative Titles

Full title

Parkinson-causing α-synuclein missense mutations shift native tetramers to monomers as a mechanism for disease initiation

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4490410

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4490410

Other Identifiers

ISSN

2041-1723

E-ISSN

2041-1723

DOI

10.1038/ncomms8314

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