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Aβ(1–42) fibril structure illuminates self-recognition and replication of amyloid in Alzheimer's dis...

Aβ(1–42) fibril structure illuminates self-recognition and replication of amyloid in Alzheimer's dis...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_miscellaneous_1709166828

Aβ(1–42) fibril structure illuminates self-recognition and replication of amyloid in Alzheimer's disease

About this item

Full title

Aβ(1–42) fibril structure illuminates self-recognition and replication of amyloid in Alzheimer's disease

Publisher

New York: Nature Publishing Group US

Journal title

Nature structural & molecular biology, 2015-06, Vol.22 (6), p.499-505

Language

English

Formats

Publication information

Publisher

New York: Nature Publishing Group US

More information

Scope and Contents

Contents

Aβ(1–42) is the most pathogenic amyloid-β species in Alzheimer's disease (AD). The solid-state NMR–based atomic model of an Aβ(1–42) fibril elucidates the mechanism of fibril formation and propagation in AD and other amyloid diseases.
Increasing evidence has suggested that formation and propagation of misfolded aggregates of 42-residue human amy...

Alternative Titles

Full title

Aβ(1–42) fibril structure illuminates self-recognition and replication of amyloid in Alzheimer's disease

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_proquest_miscellaneous_1709166828

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_miscellaneous_1709166828

Other Identifiers

ISSN

1545-9993,1545-9985

E-ISSN

1545-9985

DOI

10.1038/nsmb.2991

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