Hen lysozyme amyloid fibrils induce aggregation of erythrocytes and lipid vesicles
Author:
Publisher
Springer Science and Business Media LLC
Subject
Cell Biology,Clinical Biochemistry,Molecular Biology,General Medicine
Link
http://link.springer.com/content/pdf/10.1007/s11010-009-0091-8.pdf
Reference44 articles.
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2. Pepys MB, Hawkins PN, Booth DR, Vigushin DM, Tennent GA, Soutar AK, Totty N, Nguyen O, Blake CC, Terry CJ, Feest TG, Zalin AM, Hsuan JJ (1993) Human lysozyme gene mutations cause hereditary systemic amyloidosis. Nature 362:553–557. doi: 10.1038/362553a0
3. Booth DR, Sunde M, Bellotti V, Robinson CV, Hutchinson WL, Fraser PE, Hawkins PN, Dobson CM, Radford SE, Blake CC, Pepys MB (1997) Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis. Nature 385:787–793. doi: 10.1038/385787a0
4. Morozova-Roche LA, Zurdo J, Spencer A, Noppe W, Receveur V, Archer DB, Joniau M, Dobson CM (2000) Amyloid fibril formation and seeding by wild-type human lysozyme and its disease-related mutational variants. J Struct Biol 130:339–351. doi: 10.1006/jsbi.2000.4264
5. Krebs MR, Wilkins DK, Chung EW, Pitkeathly MC, Chamberlain AK, Zurdo J, Robinson CV, Dobson CM (2000) Formation and seeding of amyloid fibrils from wild-type hen lysozyme and a peptide fragment from the beta-domain. J Mol Biol 300:541–549. doi: 10.1006/jmbi.2000.3862
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