original ) (raw )Strategies for stabilizing superoxide dismutase (SOD1), the protein destabilized in the most common form of familial amyotrophic lateral sclerosis
Gregory Petsko
Proceedings of the National Academy of Sciences, 2010
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Oxidation-induced misfolding and aggregation of superoxide dismutase and its implications for amyotrophic lateral sclerosis
Neil Cashman
2002
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Superoxide Dismutase and Oxidative Stress in Amyotrophic Lateral Sclerosis
Alvaro Estevez
Current Advances in Amyotrophic Lateral Sclerosis, 2013
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Identification of a misfolded region in superoxide dismutase 1 that is exposed in amyotrophic lateral sclerosis
Melissa Rotunno
The Journal of biological chemistry, 2014
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Tryptophan 32 potentiates aggregation and cytotoxicity of a copper/zinc superoxide dismutase mutant associated with familial amyotrophic lateral sclerosis
Heather Durham
Journal of Biological …, 2007
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Decreased stability and increased formation of soluble aggregates by immature superoxide dismutase do not account for disease severity in ALS
Stanley Dunn
Proceedings of the National Academy of Sciences, 2011
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Detergent-insoluble Aggregates Associated with Amyotrophic Lateral Sclerosis in Transgenic Mice Contain Primarily Full-length, Unmodified Superoxide Dismutase-1
Edith Gralla
Journal of Biological Chemistry, 2008
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Metal-free superoxide dismutase forms soluble oligomers under physiological conditions: A possible general mechanism for familial ALS
lucia durazo
Proceedings of The National Academy of Sciences, 2007
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Monomeric Cu, Zn-superoxide dismutase is a common misfolding intermediate in the oxidation models of sporadic and familial amyotrophic lateral sclerosis
Neil Cashman
2004
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Experimental Mutations in Superoxide Dismutase 1 Provide Insight into Potential Mechanisms Involved in Aberrant Aggregation in Familial Amyotrophic Lateral Sclerosis
brittany roberts
G3: Genes|Genomes|Genetics
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Superoxide dismutase 1 with mutations linked to familial amyotrophic lateral sclerosis possesses significant activity
Michael Guarnieri
Proceedings of the National Academy of Sciences, 1994
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An over-oxidized form of superoxide dismutase found in sporadic amyotrophic lateral sclerosis with bulbar onset shares a toxic mechanism with mutant SOD1
Stefania Guareschi , Cristina Cereda
Proceedings of the National Academy of Sciences, 2012
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Modification of Superoxide Dismutase 1 (SOD1) Properties by a GFP Tag – Implications for Research into Amyotrophic Lateral Sclerosis (ALS)
Giampietro Schiavo
PLoS ONE, 2010
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Loss of metal ions, disulfide reduction and mutations related to familial ALS promote formation of amyloid-like aggregates from superoxide dismutase, PLoS ONE 4
Jeff Cohlberg
2009
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Superoxide Dismutase 1 (SOD1)-Derived Peptide Inhibits Amyloid Aggregation of Familial Amyotrophic Lateral Sclerosis SOD1 Mutants
Adrian Israelson
ACS Chem. Neurosci., 2016
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Advanced glycation endproduct-modified superoxide dismutase-1 (SOD1)-positive inclusions are common to familial amyotrophic lateral sclerosis patients with SOD1 gene mutations and transgenic mice expressing human SOD1 with a G85R mutation
Ryoji Nagai
Acta Neuropathologica, 2000
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Hydrogen Peroxide and Amyotrophic Lateral Sclerosis: From Biochemistry to Pathophysiology
Nitesh Sanghai
Antioxidants, 2021
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The rate and equilibrium constants for a multistep reaction sequence for the aggregation of superoxide dismutase in amyotrophic lateral sclerosis
Nikolay Dokholyan
Proceedings of the National Academy of Sciences, 2004
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Loss of Metal Ions, Disulfide Reduction and Mutations Related to Familial ALS Promote Formation of Amyloid-Like Aggregates from Superoxide Dismutase
jorge rodriguez
PLOS One, 2009
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Redox proteomics analysis of oxidatively modified proteins in G93A-SOD1 transgenic mice—a model of familial amyotrophic lateral sclerosis
Vittorio Calabrese , Fai Poon
Free Radical Biology and Medicine, 2005
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Mutant superoxide dismutase 1 forms aggregates in the brain mitochondrial matrix of amyotrophic lateral sclerosis mice
Chetan Vijayvergiya
The Journal of …, 2005
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Conversion to the amyotrophic lateral sclerosis phenotype is associated with intermolecular linked insoluble aggregates of SOD1 in mitochondria
Mohammad Khan
Proceedings of The National Academy of Sciences, 2006
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