Exposure of Hydrophobic Surfaces Initiates Aggregation of Diverse ALS-Causing Superoxide Dismutase-1 Mutants
Open Access
- 24 April 2010
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 399 (3), 512-525
- https://doi.org/10.1016/j.jmb.2010.04.019
Abstract
No abstract availableKeywords
This publication has 55 references indexed in Scilit:
- Metal-free Superoxide Dismutase-1 and Three Different Amyotrophic Lateral Sclerosis Variants Share a Similar Partially Unfolded β-Barrel at Physiological TemperatureJournal of Biological Chemistry, 2009
- Role of mutant SOD1 disulfide oxidation and aggregation in the pathogenesis of familial ALSProceedings of the National Academy of Sciences, 2009
- Progressive aggregation despite chaperone associations of a mutant SOD1-YFP in transgenic mice that develop ALSProceedings of the National Academy of Sciences, 2009
- Initiation and elongation in fibrillation of ALS-linked superoxide dismutaseProceedings of the National Academy of Sciences, 2008
- Selective association of misfolded ALS-linked mutant SOD1 with the cytoplasmic face of mitochondriaProceedings of the National Academy of Sciences, 2008
- Extrinsic Fluorescent Dyes as Tools for Protein CharacterizationPharmaceutical Research, 2008
- Soluble misfolded subfractions of mutant superoxide dismutase-1s are enriched in spinal cords throughout life in murine ALS modelsProceedings of the National Academy of Sciences, 2007
- Metal-free superoxide dismutase forms soluble oligomers under physiological conditions: A possible general mechanism for familial ALSProceedings of the National Academy of Sciences, 2007
- Impaired post-translational folding of familial ALS-linked Cu, Zn superoxide dismutase mutantsThe EMBO Journal, 2007
- Rationalization of the effects of mutations on peptide andprotein aggregation ratesNature, 2003