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Article

Identification of physiological and toxic conformations in Abeta42 aggregates.

Chembiochem : a European journal of chemical biology - 26 Jan 2009

Masuda Yuichi, Uemura Satoko, Ohashi Ryutaro, Nakanishi Azusa, Takegoshi K, Shimizu Takahiko, Shirasawa Takuji, Irie Kazuhiro

Abstract excerpt

Aggregation of the 42-residue amyloid beta-protein (Abeta42) plays a crucial role in the pathogenesis of Alzheimer's disease (AD). Despite numerous structural studies on Abeta aggregates, the relationship between tertiary structure and toxicity remains unclear. Our proline scanning and solid-state NMR studies suggested that aggregates both of wild-type Abeta42 and of E22K-Abeta42 (one of the mutants related to...

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PMID: 19115328
DOI: 10.1002/cbic.200800411

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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