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Article

Amyloid fibril formation and seeding by wild-type human lysozyme and its disease-related mutational variants.

Journal of structural biology - 1 Jun 2000

Morozova-Roche L A, Zurdo J, Spencer A, Noppe W, Receveur V, Archer D B, Joniau M, Dobson C M

Abstract excerpt

Wild-type human lysozyme and its two stable amyloidogenic variants have been found to form partially folded states at low pH. These states are characterized by extensive disruption of tertiary interactions and partial loss of secondary structure. Incubation of the proteins at pH 2.0 and 37 degrees C (Ile56Thr and Asp67His variants) or 57 degrees C (wild-type) results in the formation of large numbers of fibrils...

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Source

Identifiers

PMID: 10940237
DOI: 10.1006/jsbi.2000.4264

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

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