| P50 | author | Yoshiaki Furukawa | Q57339180 |
| P2093 | author name string | Yoshiaki Furukawa | |
| P2860 | cites work | Factors controlling the uptake of yeast copper/zinc superoxide dismutase into mitochondria. | Q44441857 |
| | Amyotrophic lateral sclerosis mutations have the greatest destabilizing effect on the apo- and reduced form of SOD1, leading to unfolding and oxidative aggregation. | Q45251257 |
| | Quantifying amyloid by congo red spectral shift assay | Q46504553 |
| | Intense superoxide dismutase-1 immunoreactivity in intracytoplasmic hyaline inclusions of familial amyotrophic lateral sclerosis with posterior column involvement | Q49023143 |
| | Inclusion bodies: Specificity in their aggregation process and amyloid-like structure | Q57956808 |
| | [18] Quantification of β-sheet amyloid fibril structures with thioflavin T | Q60547063 |
| | Mutant SOD1 causes motor neuron disease independent of copper chaperone-mediated copper loading | Q77754821 |
| | Disulphide-reduced superoxide dismutase-1 in CNS of transgenic amyotrophic lateral sclerosis models | Q81579334 |
| | Rats Expressing Human Cytosolic Copper–Zinc Superoxide Dismutase Transgenes with Amyotrophic Lateral Sclerosis: Associated Mutations Develop Motor Neuron Disease | Q94029459 |
| | Aggregation and Motor Neuron Toxicity of an ALS-Linked SOD1 Mutant Independent from Wild-Type SOD1 | Q22299419 |
| | Disulfide cross-linked protein represents a significant fraction of ALS-associated Cu, Zn-superoxide dismutase aggregates in spinal cords of model mice | Q24544265 |
| | Molecular basis of metal-ion selectivity and zeptomolar sensitivity by CueR | Q27641964 |
| | Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis | Q28131805 |
| | Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein) | Q28252462 |
| | Unique features of the sodC-encoded superoxide dismutase from Mycobacterium tuberculosis, a fully functional copper-containing enzyme lacking zinc in the active site | Q28487595 |
| | A prokaryotic superoxide dismutase paralog lacking two Cu ligands: from largely unstructured in solution to ordered in the crystal | Q28907138 |
| | Femtomolar sensitivity of metalloregulatory proteins controlling zinc homeostasis | Q29615199 |
| | Unraveling the mechanisms involved in motor neuron degeneration in ALS | Q29619073 |
| | Oxidized redox state of glutathione in the endoplasmic reticulum | Q29619789 |
| | Familial amyotrophic lateral sclerosis mutants of copper/zinc superoxide dismutase are susceptible to disulfide reduction | Q30165054 |
| | Aggregation of ALS mutant superoxide dismutase expressed in Escherichia coli | Q30759182 |
| | Destabilization of apoprotein is insufficient to explain Cu,Zn-superoxide dismutase-linked ALS pathogenesis. | Q33897544 |
| | Formation and transfer of disulphide bonds in living cells | Q34157680 |
| | Conversion to the amyotrophic lateral sclerosis phenotype is associated with intermolecular linked insoluble aggregates of SOD1 in mitochondria | Q34565165 |
| | Decreased stability and increased formation of soluble aggregates by immature superoxide dismutase do not account for disease severity in ALS. | Q34572921 |
| | Folding of Cu/Zn superoxide dismutase suggests structural hotspots for gain of neurotoxic function in ALS: parallels to precursors in amyloid disease | Q34771957 |
| | Familial ALS-superoxide dismutases associate with mitochondria and shift their redox potentials. | Q35012498 |
| | An over-oxidized form of superoxide dismutase found in sporadic amyotrophic lateral sclerosis with bulbar onset shares a toxic mechanism with mutant SOD1 | Q35882558 |
| | Molecular immunocytochemistry of the CuZn superoxide dismutase in rat hepatocytes | Q36221020 |
| | SHuffle, a novel Escherichia coli protein expression strain capable of correctly folding disulfide bonded proteins in its cytoplasm | Q36478560 |
| | The redox environment in the mitochondrial intermembrane space is maintained separately from the cytosol and matrix | Q36944848 |
| | Role of mutant SOD1 disulfide oxidation and aggregation in the pathogenesis of familial ALS | Q37175256 |
| | Activation of Cu,Zn-superoxide dismutase in the absence of oxygen and the copper chaperone CCS. | Q37372995 |
| | Amyloids in bacterial inclusion bodies | Q37568883 |
| | Oxidative stress in ALS: key role in motor neuron injury and therapeutic target | Q37647061 |
| | Decreased metallation and activity in subsets of mutant superoxide dismutases associated with familial amyotrophic lateral sclerosis. | Q38291855 |
| | Modeling amyloids in bacteria. | Q39494485 |
| | Complete loss of post-translational modifications triggers fibrillar aggregation of SOD1 in the familial form of amyotrophic lateral sclerosis | Q39972533 |
| | Loss of in vitro metal ion binding specificity in mutant copper-zinc superoxide dismutases associated with familial amyotrophic lateral sclerosis | Q41712822 |
| | Impaired post-translational folding of familial ALS-linked Cu, Zn superoxide dismutase mutants | Q41969514 |
| | Oxygen-induced maturation of SOD1: a key role for disulfide formation by the copper chaperone CCS. | Q41987289 |
| | Characterization of the amyloid bacterial inclusion bodies of the HET-s fungal prion | Q42023365 |
| | Amyloid-like properties of bacterial inclusion bodies. | Q42651430 |
| | Disulfide scrambling describes the oligomer formation of superoxide dismutase (SOD1) proteins in the familial form of amyotrophic lateral sclerosis. | Q43244834 |
| | Subcellular distribution of superoxide dismutases (SOD) in rat liver: Cu,Zn-SOD in mitochondria | Q43708597 |
| | Histological Evidence of Protein Aggregation in Mutant SOD1 Transgenic Mice and in Amyotrophic Lateral Sclerosis Neural Tissues | Q43821139 |
| | Oxidation-induced misfolding and aggregation of superoxide dismutase and its implications for amyotrophic lateral sclerosis | Q44160891 |
| | Bicarbonate-dependent peroxidase activity of human Cu,Zn-superoxide dismutase induces covalent aggregation of protein: intermediacy of tryptophan-derived oxidation products | Q44397887 |
| P921 | main subject | amyotrophic lateral sclerosis | Q206901 |
| P304 | page(s) | 240 | |
| P577 | publication date | 2013-11-27 | |
| P1433 | published in | Frontiers in Cellular Neuroscience | Q2131509 |
| P1476 | title | Redox environment is an intracellular factor to operate distinct pathways for aggregation of Cu,Zn-superoxide dismutase in amyotrophic lateral sclerosis | |
| P478 | volume | 7 | |