| P50 | author | Aron Workman | Q85760831 |
| P2860 | cites work | The copper chaperone for superoxide dismutase | Q24311669 |
| | DJ-1 is a copper chaperone acting on SOD1 activation | Q24338208 |
| | Amyloid-like filaments and water-filled nanotubes formed by SOD1 mutant proteins linked to familial ALS | Q27641284 |
| | Atomic structures of wild-type and thermostable mutant recombinant human Cu,Zn superoxide dismutase | Q27642611 |
| | Structural and Biophysical Properties of the Pathogenic SOD1 Variant H46R/H48Q † | Q27653849 |
| | SOD1 integrates signals from oxygen and glucose to repress respiration | Q27935827 |
| | The rate and equilibrium constants for a multistep reaction sequence for the aggregation of superoxide dismutase in amyotrophic lateral sclerosis | Q28287224 |
| | pEF-BOS, a powerful mammalian expression vector | Q29547606 |
| | Protein aggregation and protein instability govern familial amyotrophic lateral sclerosis patient survival | Q33356197 |
| | Progressive aggregation despite chaperone associations of a mutant SOD1-YFP in transgenic mice that develop ALS. | Q33403156 |
| | Metal-free ALS variants of dimeric human Cu,Zn-superoxide dismutase have enhanced populations of monomeric species | Q33559671 |
| | Immature copper-zinc superoxide dismutase and familial amyotrophic lateral sclerosis. | Q33772493 |
| | Recent progress in the genetics of motor neuron disease | Q34402851 |
| | Cu,Zn-superoxide dismutase without Zn is folded but catalytically inactive | Q34647281 |
| | Superoxide dismutase is an abundant component in cell bodies, dendrites, and axons of motor neurons and in a subset of other neurons | Q34667159 |
| | Disulfide-reduced ALS variants of Cu, Zn superoxide dismutase exhibit increased populations of unfolded species | Q34788369 |
| | Superoxide dismutase 1 with mutations linked to familial amyotrophic lateral sclerosis possesses significant activity | Q35693516 |
| | Metal-free superoxide dismutase forms soluble oligomers under physiological conditions: a possible general mechanism for familial ALS | Q35854965 |
| | SOD1 aggregation in ALS mice shows simplistic test tube behavior | Q35961208 |
| | Human superoxide dismutase 1 (hSOD1) maturation through interaction with human copper chaperone for SOD1 (hCCS) | Q36187334 |
| | Amyotrophic lateral sclerosis associated with mutations in the CuZn superoxide dismutase gene | Q36392290 |
| | Detergent-insoluble aggregates associated with amyotrophic lateral sclerosis in transgenic mice contain primarily full-length, unmodified superoxide dismutase-1. | Q36512177 |
| | A novel variant of human superoxide dismutase 1 harboring amyotrophic lateral sclerosis-associated and experimental mutations in metal-binding residues and free cysteines lacks toxicity in vivo | Q36995776 |
| | Is SOD1 loss of function involved in amyotrophic lateral sclerosis? | Q37043070 |
| | Role of mutant SOD1 disulfide oxidation and aggregation in the pathogenesis of familial ALS | Q37175256 |
| | Variation in aggregation propensities among ALS-associated variants of SOD1: correlation to human disease. | Q37295060 |
| | Activation of Cu,Zn-superoxide dismutase in the absence of oxygen and the copper chaperone CCS. | Q37372995 |
| | Disease-associated mutations at copper ligand histidine residues of superoxide dismutase 1 diminish the binding of copper and compromise dimer stability | Q37375549 |
| | Genetic epidemiology of motor neuron disease-associated variants in the Scottish population | Q37635851 |
| | Distinctive features of the D101N and D101G variants of superoxide dismutase 1; two mutations that produce rapidly progressing motor neuron disease | Q37677384 |
| | Oxygen and the copper chaperone CCS regulate posttranslational activation of Cu,Zn superoxide dismutase | Q37681868 |
| | SOD1 Function and Its Implications for Amyotrophic Lateral Sclerosis Pathology: New and Renascent Themes | Q38285976 |
| | A limited role for disulfide cross-linking in the aggregation of mutant SOD1 linked to familial amyotrophic lateral sclerosis. | Q38291545 |
| | Mutant superoxide dismutase-1 indistinguishable from wild-type causes ALS. | Q39346490 |
| | SOD1 mutations targeting surface hydrogen bonds promote amyotrophic lateral sclerosis without reducing apo-state stability | Q41049208 |
| | Susceptibility of Mutant SOD1 to Form a Destabilized Monomer Predicts Cellular Aggregation and Toxicity but Not In vitro Aggregation Propensity. | Q41668065 |
| | Oxygen-induced maturation of SOD1: a key role for disulfide formation by the copper chaperone CCS. | Q41987289 |
| | High molecular weight complexes of mutant superoxide dismutase 1: age-dependent and tissue-specific accumulation | Q43918294 |
| | Fibrillar inclusions and motor neuron degeneration in transgenic mice expressing superoxide dismutase 1 with a disrupted copper-binding site | Q44070818 |
| | Copper-binding-site-null SOD1 causes ALS in transgenic mice: aggregates of non-native SOD1 delineate a common feature | Q44579313 |
| | Monomeric Cu,Zn-superoxide dismutase is a common misfolding intermediate in the oxidation models of sporadic and familial amyotrophic lateral sclerosis. | Q44735743 |
| | Mechanistic aspects of hSOD1 maturation from the solution structure of Cu(I) -loaded hCCS domain 1 and analysis of disulfide-free hSOD1 mutants | Q44778683 |
| | Inducible superoxide dismutase 1 aggregation in transgenic amyotrophic lateral sclerosis mouse fibroblasts. | Q44808073 |
| | Long distance charge redistribution upon Cu,Zn-superoxide dismutase reduction: significance for dismutase function. | Q45029755 |
| | Faster superoxide dismutase mutants designed by enhancing electrostatic guidance | Q45965859 |
| | Clinical Spectrum of Amyotrophic Lateral Sclerosis (ALS). | Q46017258 |
| | ALS-linked SOD1 mutant G85R mediates damage to astrocytes and promotes rapidly progressive disease with SOD1-containing inclusions. | Q46135324 |
| | Superoxide dismutase undergoes proteolysis and fragmentation following oxidative modification and inactivation | Q46314983 |
| | Complex I is the major site of mitochondrial superoxide production by paraquat | Q46881393 |
| | ALSoD: A user-friendly online bioinformatics tool for amyotrophic lateral sclerosis genetics | Q47427105 |
| | An intersubunit disulfide bond prevents in vitro aggregation of a superoxide dismutase-1 mutant linked to familial amytrophic lateral sclerosis | Q47700139 |
| | Real-time analysis and direct observations of different superoxide dismutase (SOD1) molecules bindings to aggregates in temporal evolution step. | Q51317866 |
| | Superoxide dismutase: a comparison of rate constants. | Q53745613 |
| | Variation in the biochemical/biophysical properties of mutant superoxide dismutase 1 enzymes and the rate of disease progression in familial amyotrophic lateral sclerosis kindreds. | Q54089001 |
| | Oxidation versus aggregation - how do SOD1 mutants cause ALS? | Q54598711 |
| | A pulse radiolysis study of superoxide dismutase | Q70374009 |
| | Copper- and zinc-containing superoxide dismutase can act as a superoxide reductase and a superoxide oxidase | Q73004226 |
| | The coupling between disulphide status, metallation and dimer interface strength in Cu/Zn superoxide dismutase | Q79311744 |
| | Coincident thresholds of mutant protein for paralytic disease and protein aggregation caused by restrictively expressed superoxide dismutase cDNA | Q80939419 |
| | Stochastic Formation of Fibrillar and Amorphous Superoxide Dismutase Oligomers Linked to Amyotrophic Lateral Sclerosis | Q87465414 |
| P433 | issue | 1-2 | |
| P304 | page(s) | 117-128 | |
| P577 | publication date | 2020-02-13 | |
| P1433 | published in | Molecular and Cellular Biochemistry | Q1573176 |
| P1476 | title | Nucleation and kinetics of SOD1 aggregation in human cells for ALS1 | |
| P478 | volume | 466 | |