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Article

A method for probing the mutational landscape of amyloid structure.

Bioinformatics (Oxford, England) - 1 Jul 2011

O'Donnell Charles W, Waldispühl Jérôme, Lis Mieszko, Halfmann Randal, Devadas Srinivas, Lindquist Susan, Berger Bonnie

Abstract excerpt

MOTIVATION: Proteins of all kinds can self-assemble into highly ordered β-sheet aggregates known as amyloid fibrils, important both biologically and clinically. However, the specific molecular structure of a fibril can vary dramatically depending on sequence and environmental conditions, and mutations can drastically alter amyloid function and pathogenicity. Experimental structure determination has proven...

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Identifiers

PMID: 21685090
DOI: 10.1093/bioinformatics/btr238
PMCID: PMC3117379

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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