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Aβ42 assembles into specific β-barrel pore-forming oligomers in membrane-mimicking environments

Aβ42 assembles into specific β-barrel pore-forming oligomers in membrane-mimicking environments

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_5047179

Aβ42 assembles into specific β-barrel pore-forming oligomers in membrane-mimicking environments

About this item

Full title

Aβ42 assembles into specific β-barrel pore-forming oligomers in membrane-mimicking environments

Publisher

United States: National Academy of Sciences

Journal title

Proceedings of the National Academy of Sciences - PNAS, 2016-09, Vol.113 (39), p.10866-10871

Language

English

Formats

Publication information

Publisher

United States: National Academy of Sciences

Subjects

Subjects and topics

More information

Scope and Contents

Contents

The formation of amyloid-β peptide (Aβ) oligomers at the cellular membrane is considered to be a crucial process underlying neurotoxicity in Alzheimer’s disease (AD). Therefore, it is critical to characterize the oligomers that form within a membrane environment. To contribute to this characterization, we have applied strategies widely used to exam...

Alternative Titles

Full title

Aβ42 assembles into specific β-barrel pore-forming oligomers in membrane-mimicking environments

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_5047179

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_5047179

Other Identifiers

ISSN

0027-8424

E-ISSN

1091-6490

DOI

10.1073/pnas.1605104113

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