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Atomic-resolution structure of a disease-relevant Aβ(1–42) amyloid fibril

Atomic-resolution structure of a disease-relevant Aβ(1–42) amyloid fibril

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_5003276

Atomic-resolution structure of a disease-relevant Aβ(1–42) amyloid fibril

About this item

Full title

Atomic-resolution structure of a disease-relevant Aβ(1–42) amyloid fibril

Publisher

United States: National Academy of Sciences

Journal title

Proceedings of the National Academy of Sciences - PNAS, 2016-08, Vol.113 (34), p.E4976-E4984

Language

English

Formats

Publication information

Publisher

United States: National Academy of Sciences

More information

Scope and Contents

Contents

Amyloid-β (Aβ) is present in humans as a 39- to 42-amino acid residue metabolic product of the amyloid precursor protein. Although the two predominant forms, Aβ(1–40) and Aβ(1–42), differ in only two residues, they display different biophysical, biological, and clinical behavior. Aβ(1–42) is the more neurotoxic species, aggregates much faster, and...

Alternative Titles

Full title

Atomic-resolution structure of a disease-relevant Aβ(1–42) amyloid fibril

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_5003276

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_5003276

Other Identifiers

ISSN

0027-8424

E-ISSN

1091-6490

DOI

10.1073/pnas.1600749113