Nonamyloid Aggregates Arising from Mature Copper/Zinc Superoxide Dismutases Resemble Those Observed in Amyotrophic Lateral Sclerosis (original) (raw)
Dimerization, Oligomerization, and Aggregation of Human Amyotrophic Lateral Sclerosis Copper/Zinc Superoxide Dismutase 1 Protein Mutant Forms in Live Cells
Arnaud Ogier
Journal of Biological Chemistry, 2014
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Cu/Zn superoxide dismutase mutants associated with amyotrophic lateral sclerosis show enhanced formation of aggregates in vitro
Jessica Rumfeldt
Proceedings of the National Academy of Sciences, 2003
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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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Oxidation-induced misfolding and aggregation of superoxide dismutase and its implications for amyotrophic lateral sclerosis
Neil Cashman
2002
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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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Copper and Zinc Metallation Status of Copper-Zinc Superoxide Dismutase from Amyotrophic Lateral Sclerosis Transgenic Mice
Joan S Valentine, H. Lelie, Julian Whitelegge
Journal of Biological Chemistry, 2011
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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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Folding of Cu, Zn Superoxide Dismutase and Familial Amyotrophic Lateral Sclerosis
Nikolay Dokholyan
Journal of Molecular Biology, 2003
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Folding and Aggregation of Cu, Zn-Superoxide Dismutase
Jessica Rumfeldt
Amyotrophic Lateral Sclerosis, 2012
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Common dynamical signatures of familial amyotrophic lateral sclerosis-associated structurally diverse Cu, Zn superoxide dismutase mutants
Nikolay Dokholyan
Proceedings of the National Academy of Sciences, 2006
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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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Disulfide cross-linked protein represents a significant fraction of ALS-associated Cu, Zn-superoxide dismutase aggregates in spinal cords of model mice
Han-Xiang Deng
Proceedings of the National Academy of Sciences, 2006
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Metal Deficiency Increases Aberrant Hydrophobicity of Mutant Superoxide Dismutases That Cause Amyotrophic Lateral Sclerosis
Lawrence Hayward
Journal of Biological Chemistry, 2009
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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
Phong dinh
PLOS One, 2009
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Aggregation propensities of superoxide dismutase G93 hotspot mutants mirror ALS clinical phenotypes
John Tainer
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Loss of in Vitro Metal Ion Binding Specificity in Mutant Copper-Zinc Superoxide Dismutases Associated with Familial Amyotrophic Lateral Sclerosis
Edith Gralla
Journal of Biological Chemistry, 2000
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Metal-deficient SOD1 in amyotrophic lateral sclerosis
Peter ofosu Antwi crouch
Journal of Molecular Medicine, 2015
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Cysteine 111 affects aggregation and cytotoxicity of mutant Cu, Zn-superoxide dismutase associated with familial amyotrophic lateral sclerosis
Anne Ferri
Journal of Biological …, 2008
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The Structure of Holo and Metal-deficient Wild-type Human Cu, Zn Superoxide Dismutase and its Relevance to Familial Amyotrophic Lateral Sclerosis
Lawrence Hayward
Journal of Molecular Biology, 2003
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Mutations in copper-zinc superoxide dismutase that cause amyotrophic lateral sclerosis alter the zinc binding site and the redox behavior of the protein
Edith Gralla
Proceedings of the National Academy of Sciences, 1996
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Aberrantly Increased Hydrophobicity Shared by Mutants of Cu,Zn-Superoxide Dismutase in Familial Amyotrophic Lateral Sclerosis
ashutosh tiwari
Journal of Biological Chemistry, 2005
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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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Impaired copper binding by the H46R mutant of human Cu,Zn superoxide dismutase, involved in amyotrophic lateral sclerosis
Andrea Battistoni
Febs Letters, 1994
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Decreased Metallation and Activity in Subsets of Mutant Superoxide Dismutases Associated with Familial Amyotrophic Lateral Sclerosis
ashutosh tiwari
Journal of Biological Chemistry, 2002
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