Cryo-EM structure of a light chain-derived amyloid fibril from a patient with systemic AL amyloidosis

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MAK33 antibody light chain amyloid fibrils are similar to oligomeric precursors

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Fibril structure of amyloid-β(1–42) by cryo–electron microscopy

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Polymorphism of Amyloid Fibrils In Vivo

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Clarifying immunoglobulin gene usage in systemic and localized immunoglobulin light-chain amyloidosis by mass spectrometry

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Cryo-EM reveals the steric zipper structure of a light chain-derived amyloid fibril

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Light Chain Amyloid Fibrils Cause Metabolic Dysfunction in Human Cardiomyocytes

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The repertoire of   light chains causing predominant amyloid heart involvement and identification of a preferentially involved germline gene, IGLV1-44

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FoldAmyloid: a method of prediction of amyloidogenic regions from protein sequence

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Globular Tetramers of β2-Microglobulin Assemble into Elaborate Amyloid Fibrils

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Amyloidogenic determinants are usually not buried

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Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7

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