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In situ kinetic measurements of α-synuclein aggregation reveal large population of short-lived oligo...

In situ kinetic measurements of α-synuclein aggregation reveal large population of short-lived oligo...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_plos_journals_2479993208

In situ kinetic measurements of α-synuclein aggregation reveal large population of short-lived oligomers

About this item

Full title

In situ kinetic measurements of α-synuclein aggregation reveal large population of short-lived oligomers

Publisher

United States: Public Library of Science

Journal title

PloS one, 2021, Vol.16 (1), p.e0245548

Language

English

Formats

Publication information

Publisher

United States: Public Library of Science

More information

Scope and Contents

Contents

Knowledge of the mechanisms of assembly of amyloid proteins into aggregates is of central importance in building an understanding of neurodegenerative disease. Given that oligomeric intermediates formed during the aggregation reaction are believed to be the major toxic species, methods to track such intermediates are clearly needed. Here we present...

Alternative Titles

Full title

In situ kinetic measurements of α-synuclein aggregation reveal large population of short-lived oligomers

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_plos_journals_2479993208

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_plos_journals_2479993208

Other Identifiers

ISSN

1932-6203

E-ISSN

1932-6203

DOI

10.1371/journal.pone.0245548

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