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The C-terminal tail of α-synuclein protects against aggregate replication but is critical for oligom...

The C-terminal tail of α-synuclein protects against aggregate replication but is critical for oligom...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_3b30c2233d094c1fb5d89c40c979733a

The C-terminal tail of α-synuclein protects against aggregate replication but is critical for oligomerization

About this item

Full title

The C-terminal tail of α-synuclein protects against aggregate replication but is critical for oligomerization

Publisher

London: Nature Publishing Group UK

Journal title

Communications biology, 2022-02, Vol.5 (1), p.123-123, Article 123

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

Aggregation of the 140-residue protein α-synuclein (αSN) is a key factor in the etiology of Parkinson’s disease. Although the intensely anionic C-terminal domain (CTD) of αSN does not form part of the amyloid core region or affect membrane binding ability, truncation or reduction of charges in the CTD promotes fibrillation through as yet unknown me...

Alternative Titles

Full title

The C-terminal tail of α-synuclein protects against aggregate replication but is critical for oligomerization

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_doaj_primary_oai_doaj_org_article_3b30c2233d094c1fb5d89c40c979733a

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_3b30c2233d094c1fb5d89c40c979733a

Other Identifiers

ISSN

2399-3642

E-ISSN

2399-3642

DOI

10.1038/s42003-022-03059-8

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