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MS785-MS27 Reactive Misfolded/Non-Native Zn-Deficient SOD1 Species Exhibit Cytotoxicity and Adopt Heterozygous Conformations in Motor Neurons.
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- International Journal of Molecular Sciences, 2024, v. 25, n. 11, p. 5603, doi. 10.3390/ijms25115603
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- Article
FUS regulates RAN translation through modulating the G-quadruplex structure of GGGGCC repeat RNA in C9orf72-linked ALS/FTD.
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- eLife, 2023, p. 1, doi. 10.7554/eLife.84338
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- Article
A Metal-Free, Disulfide Oxidized Form of Superoxide Dismutase 1 as a Primary Misfolded Species with Prion-Like Properties in the Extracellular Environments Surrounding Motor Neuron-Like Cells.
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- International Journal of Molecular Sciences, 2021, v. 22, n. 8, p. 4155, doi. 10.3390/ijms22084155
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- Article
Does wild-type Cu/Zn-superoxide dismutase have pathogenic roles in amyotrophic lateral sclerosis?
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- Translational Neurodegeneration, 2020, v. 9, n. 1, p. N.PAG, doi. 10.1186/s40035-020-00209-y
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- Article
Wild-type Cu/Zn-superoxide dismutase is misfolded in cerebrospinal fluid of sporadic amyotrophic lateral sclerosis.
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- Molecular Neurodegeneration, 2019, v. 14, n. 1, p. N.PAG, doi. 10.1186/s13024-019-0341-5
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- Article
Cu/Zn-superoxide dismutase forms fibrillar hydrogels in a pH-dependent manner via a water-rich extended intermediate state.
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- PLoS ONE, 2018, v. 13, n. 10, p. 1, doi. 10.1371/journal.pone.0205090
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- Article
A misfolded dimer of Cu/Zn-superoxide dismutase leading to pathological oligomerization in amyotrophic lateral sclerosis.
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- Protein Science: A Publication of the Protein Society, 2017, v. 26, n. 3, p. 484, doi. 10.1002/pro.3094
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- Article
Immunochemical characterization on pathological oligomers of mutant Cu/Znsuperoxide dismutase in amyotrophic lateral sclerosis.
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- Molecular Neurodegeneration, 2017, v. 12, p. 1, doi. 10.1186/s13024-016-0145-9
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- Article
Copper Homeostasis as a Therapeutic Target in Amyotrophic Lateral Sclerosis with SOD1 Mutations.
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- International Journal of Molecular Sciences, 2016, v. 17, n. 5, p. 636, doi. 10.3390/ijms17050636
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- Article
Low autophagy capacity implicated in motor system vulnerability to mutant superoxide dismutase.
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- Acta Neuropathologica Communications, 2016, v. 4, p. 1, doi. 10.1186/s40478-016-0274-y
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- Article
Overexpression of metallothionein-I, a copper-regulating protein, attenuates intracellular copper dyshomeostasis and extends lifespan in a mouse model of amyotrophic lateral sclerosis caused by mutant superoxide dismutase-1.
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- Human Molecular Genetics, 2014, v. 23, n. 5, p. 1271, doi. 10.1093/hmg/ddt517
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- Article
Dysregulation of intracellular copper trafficking pathway in a mouse model of mutant copper/zinc superoxide dismutase-linked familial amyotrophic lateral sclerosis.
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- Journal of Neurochemistry, 2009, v. 111, n. 1, p. 181, doi. 10.1111/j.1471-4159.2009.06310.x
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- Article
Ammonium tetrathiomolybdate, a copper-chelating drug, suppresses superoxide disumtase1 aggregation and has therapeutic effects in a mouse model of myotrophic lateral sclerosis.
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- Annals of Indian Academy of Neurology, 2008, v. 11, p. S174
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- Article