Reduced Global Cooperativity is a Common Feature Underlying the Amyloidogenicity of Pathogenic Lysozyme Mutations
- 1 February 2005
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 346 (3) , 773-788
- https://doi.org/10.1016/j.jmb.2004.11.020
Abstract
No abstract availableKeywords
This publication has 35 references indexed in Scilit:
- Probing the origins, diagnosis and treatment of amyloid diseases using antibodiesBiochimie, 2004
- A Highly Amyloidogenic Region of Hen LysozymeJournal of Molecular Biology, 2004
- Folding proteins in fatal waysNature, 2003
- Protein folding and misfoldingNature, 2003
- Therapeutic approaches to protein-misfolding diseasesNature, 2003
- Therapeutic strategies for human amyloid diseasesNature Reviews Drug Discovery, 2002
- Characterization of the structure and dynamics of amyloidogenic variants of human lysozyme by NMR spectroscopyProtein Science, 2001
- MOLMOL: A program for display and analysis of macromolecular structuresJournal of Molecular Graphics, 1996
- Cooperative Elements in Protein Folding Monitored by Electrospray Ionization Mass SpectrometryJournal of the American Chemical Society, 1995
- The Refolding of Human Lysozyme: A Comparison with the Structurally Homologous Hen LysozymeBiochemistry, 1994