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Intramolecular interaction kinetically regulates fibril formation by human and mouse α-synuclein

Intramolecular interaction kinetically regulates fibril formation by human and mouse α-synuclein

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_10610d7d92d34ae0ab1fa5b064e5d988

Intramolecular interaction kinetically regulates fibril formation by human and mouse α-synuclein

About this item

Full title

Intramolecular interaction kinetically regulates fibril formation by human and mouse α-synuclein

Publisher

London: Nature Publishing Group UK

Journal title

Scientific reports, 2023-07, Vol.13 (1), p.10885-10885, Article 10885

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

Regulation of α-synuclein (αS) fibril formation is a potent therapeutic strategy for αS-related neurodegenerative disorders. αS, an intrinsically disordered 140-residue intraneural protein, comprises positively charged N-terminal, hydrophobic non-amyloid β component (NAC), and negatively charged C-terminal regions. Although mouse and human αS share...

Alternative Titles

Full title

Intramolecular interaction kinetically regulates fibril formation by human and mouse α-synuclein

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_doaj_primary_oai_doaj_org_article_10610d7d92d34ae0ab1fa5b064e5d988

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_10610d7d92d34ae0ab1fa5b064e5d988

Other Identifiers

ISSN

2045-2322

E-ISSN

2045-2322

DOI

10.1038/s41598-023-38070-4

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