Formation and seeding of amyloid fibrils from wild-type hen lysozyme and a peptide fragment from the β-domain
- 1 July 2000
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 300 (3), 541-549
- https://doi.org/10.1006/jmbi.2000.3862
Abstract
No abstract availableKeywords
This publication has 43 references indexed in Scilit:
- Protein misfolding, evolution and diseaseTrends in Biochemical Sciences, 1999
- Mechanistic Studies of the Folding of Human Lysozyme and the Origin of Amyloidogenic Behavior in Its Disease-Related VariantsBiochemistry, 1999
- Designing conditions for in vitro formation of amyloid protofilaments and fibrilsProceedings of the National Academy of Sciences, 1999
- Responsive gels formed by the spontaneous self-assembly of peptides into polymeric β-sheet tapesNature, 1997
- Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesisNature, 1997
- Thermodynamic consequences of the removal of a disulphide bridge from hen lysozymeJournal of Molecular Biology, 1992
- ELECTRON MICROSCOPY OF NETWORK STRUCTURES IN THERMALLY‐INDUCED GLOBULAR PROTEIN GELSInternational Journal of Peptide and Protein Research, 1981
- Formation and Structure of Gels and Fibrils from GlucagonEuropean Journal of Biochemistry, 1969
- Structure of Hen Egg-White Lysozyme: A Three-dimensional Fourier Synthesis at 2 Å ResolutionNature, 1965
- The X-ray interpretation of denaturation and the structure of the seed globulinsBiochemical Journal, 1935