Formation of amyloid-like fibrils upon limited proteolysis of bovine α-lactalbumin
- 31 March 2005
- journal article
- Published by Elsevier in International Dairy Journal
- Vol. 15 (3) , 219-229
- https://doi.org/10.1016/j.idairyj.2004.07.004
Abstract
No abstract availableKeywords
This publication has 26 references indexed in Scilit:
- Mixtures of Wild-type and a Pathogenic (E22G) Form of Aβ40 in Vitro Accumulate Protofibrils, Including Amyloid PoresJournal of Molecular Biology, 2003
- Protein folding revisited. A polypeptide chain at the folding ? misfolding ? nonfolding cross-roads: which way to go?Cellular and Molecular Life Sciences, 2003
- A General Model for Amyloid Fibril Assembly Based on Morphological Studies Using Atomic Force MicroscopyBiophysical Journal, 2003
- Formation and seeding of amyloid fibrils from wild-type hen lysozyme and a peptide fragment from the β-domainJournal of Molecular Biology, 2000
- In-situ atomic force microscopy study of β-amyloid fibrillizationJournal of Molecular Biology, 2000
- High Density Lipoprotein Inhibits Assembly of Amyloid β-Peptides into FibrilsBiochemical and Biophysical Research Communications, 2000
- Assembly of Aβ Amyloid Protofibrils: An in Vitro Model for a Possible Early Event in Alzheimer's DiseaseBiochemistry, 1999
- A specific hydrophobic core in the α-lactalbumin molten globuleJournal of Molecular Biology, 1998
- Isolation and amino acid sequence of a glutamic acid specific endopeptidase from Bacillus licheniformisEuropean Journal of Biochemistry, 1992
- Controlled environment vitrification system: An improved sample preparation techniqueJournal of Electron Microscopy Technique, 1988