Metal-free Superoxide Dismutase-1 and Three Different Amyotrophic Lateral Sclerosis Variants Share a Similar Partially Unfolded β-Barrel at Physiological Temperature
Open Access
- 1 December 2009
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 284 (49), 34382-34389
- https://doi.org/10.1074/jbc.m109.052076
Abstract
No abstract availableKeywords
This publication has 32 references indexed in Scilit:
- A Common Property of Amyotrophic Lateral Sclerosis-associated VariantsJournal of Biological Chemistry, 2009
- Loss of Metal Ions, Disulfide Reduction and Mutations Related to Familial ALS Promote Formation of Amyloid-Like Aggregates from Superoxide DismutasePLOS ONE, 2009
- Initiation and elongation in fibrillation of ALS-linked superoxide dismutaseProceedings of the National Academy of Sciences, 2008
- Detergent-insoluble Aggregates Associated with Amyotrophic Lateral Sclerosis in Transgenic Mice Contain Primarily Full-length, Unmodified Superoxide Dismutase-1Journal of Biological Chemistry, 2008
- Electrostatic Potential Energy within a Protein Monitored by Metal Charge-Dependent Hydrogen ExchangeBiophysical Journal, 2006
- Reduced Global Cooperativity is a Common Feature Underlying the Amyloidogenicity of Pathogenic Lysozyme MutationsJournal of Molecular Biology, 2004
- Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosisNature, 1993
- Amide proton exchange and surface conformation of the basic pancreatic trypsin inhibitor in solutionJournal of Molecular Biology, 1982
- A general multistate model for the analysis of hydrogen-exchange kineticsBiopolymers, 1980
- Structural interpretation of the amide proton exchange in the basic pancreatic trypsin inhibitor and related proteinsJournal of Molecular Biology, 1979