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A natural product inhibits the initiation of [alpha]-synuclein aggregation and suppresses its toxici...

A natural product inhibits the initiation of [alpha]-synuclein aggregation and suppresses its toxici...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_journals_1876858856

A natural product inhibits the initiation of [alpha]-synuclein aggregation and suppresses its toxicity

About this item

Full title

A natural product inhibits the initiation of [alpha]-synuclein aggregation and suppresses its toxicity

Publisher

Washington: National Academy of Sciences

Journal title

Proceedings of the National Academy of Sciences - PNAS, 2017-02, Vol.114 (6), p.E1009

Language

English

Formats

Publication information

Publisher

Washington: National Academy of Sciences

More information

Scope and Contents

Contents

The self-assembly of a-synuclein is closely associated with Parkinson's disease and related syndromes. We show that squalamine, a natural product with known anticancer and antiviral activity, dramatically affects a-synuclein aggregation in vitro and in vivo. We elucidate the mechanism of action of squalamine by investigating its interaction with li...

Alternative Titles

Full title

A natural product inhibits the initiation of [alpha]-synuclein aggregation and suppresses its toxicity

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_proquest_journals_1876858856

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_journals_1876858856

Other Identifiers

ISSN

0027-8424

E-ISSN

1091-6490

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