| review article | Q7318358 |
| scholarly article | Q13442814 |
| P50 | author | Clara Iannuzzi | Q63974689 |
| P2093 | author name string | Ivana Sirangelo | |
| P2860 | cites work | Metals in spinal cord tissue of patients dying of motor neuron disease | Q66970508 |
| The metal binding properties of the zinc site of yeast copper-zinc superoxide dismutase: implications for amyotrophic lateral sclerosis | Q73810547 | ||
| Decreased zinc affinity of amyotrophic lateral sclerosis-associated superoxide dismutase mutants leads to enhanced catalysis of tyrosine nitration by peroxynitrite | Q73829106 | ||
| The coupling between disulphide status, metallation and dimer interface strength in Cu/Zn superoxide dismutase | Q79311744 | ||
| The unusually stable quaternary structure of human Cu,Zn-superoxide dismutase 1 is controlled by both metal occupancy and disulfide status | Q80485358 | ||
| Metal ions as modulators of protein conformation and misfolding in neurodegeneration | Q57724534 | ||
| Prediction of the Absolute Aggregation Rates of Amyloidogenic Polypeptide Chains | Q58374785 | ||
| Penicillamine in amyotrophic lateral sclerosis | Q66701888 | ||
| SOD1 and amyotrophic lateral sclerosis: mutations and oligomerization | Q21090100 | ||
| Aggregation and Motor Neuron Toxicity of an ALS-Linked SOD1 Mutant Independent from Wild-Type SOD1 | Q22299419 | ||
| Binding of a single zinc ion to one subunit of copper-zinc superoxide dismutase apoprotein substantially influences the structure and stability of the entire homodimeric protein | Q24300789 | ||
| Copper Homeostasis as a Therapeutic Target in Amyotrophic Lateral Sclerosis with SOD1 Mutations | Q26748245 | ||
| Heterodimeric structure of superoxide dismutase in complex with its metallochaperone | Q27634428 | ||
| Structure and dynamics of copper-free SOD: The protein before binding copper | Q27639669 | ||
| Solution structure of Apo Cu,Zn superoxide dismutase: role of metal ions in protein folding | Q27641822 | ||
| Structural and Biophysical Properties of the Pathogenic SOD1 Variant H46R/H48Q † | Q27653849 | ||
| Structural and dynamic aspects related to oligomerization of apo SOD1 and its mutants | Q27654799 | ||
| Amyotrophic lateral sclerosis mutations have the greatest destabilizing effect on the apo- and reduced form of SOD1, leading to unfolding and oxidative aggregation. | Q45251257 | ||
| Relationship between mutant Cu/Zn superoxide dismutase 1 maturation and inclusion formation in cell models | Q46537325 | ||
| Aberrant zinc binding to immature conformers of metal-free copper-zinc superoxide dismutase triggers amorphous aggregation | Q46791114 | ||
| In-cell NMR reveals potential precursor of toxic species from SOD1 fALS mutants. | Q46809689 | ||
| Calorimetric analysis of thermodynamic stability and aggregation for apo and holo amyotrophic lateral sclerosis-associated Gly-93 mutants of superoxide dismutase | Q46890321 | ||
| On the stability of bovine superoxide dismutase. The effects of metals. | Q48004534 | ||
| Minute quantities of misfolded mutant superoxide dismutase-1 cause amyotrophic lateral sclerosis | Q48177170 | ||
| Direct Conversion of an Enzyme from Native-like to Amyloid-like Aggregates within Inclusion Bodies | Q50204472 | ||
| Visualization of redox-controlled protein fold in living cells. | Q50888274 | ||
| Kinetic stability of Cu/Zn superoxide dismutase is dependent on its metal ligands: implications for ALS. | Q51564313 | ||
| An adverse property of a familial ALS-linked SOD1 mutation causes motor neuron disease characterized by vacuolar degeneration of mitochondria | Q54965159 | ||
| Folding catalysis by transient coordination of Zn2+ to the Cu ligands of the ALS-associated enzyme Cu/Zn superoxide dismutase 1 | Q27664295 | ||
| Atomic structure and hierarchical assembly of a cross- amyloid fibril | Q27676898 | ||
| Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis | Q28131805 | ||
| Overloading of stable and exclusion of unstable human superoxide dismutase-1 variants in mitochondria of murine amyotrophic lateral sclerosis models | Q28235353 | ||
| Motor neurons in Cu/Zn superoxide dismutase-deficient mice develop normally but exhibit enhanced cell death after axonal injury | Q28511628 | ||
| Motor neuron degeneration in mice that express a human Cu,Zn superoxide dismutase mutation | Q29547561 | ||
| Calcium signalling: dynamics, homeostasis and remodelling | Q29547635 | ||
| Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases | Q29616535 | ||
| ALS: a disease of motor neurons and their nonneuronal neighbors | Q29618000 | ||
| Unraveling the mechanisms involved in motor neuron degeneration in ALS | Q29619073 | ||
| Amyotrophic lateral sclerosis | Q29619516 | ||
| Protein misfolding and aggregation: new examples in medicine and biology of the dark side of the protein world | Q29998861 | ||
| Metal-free superoxide dismutase-1 and three different amyotrophic lateral sclerosis variants share a similar partially unfolded beta-barrel at physiological temperature | Q30157094 | ||
| Zinc binding modulates the entire folding free energy surface of human Cu,Zn superoxide dismutase | Q30157502 | ||
| Local unfolding in a destabilized, pathogenic variant of superoxide dismutase 1 observed with H/D exchange and mass spectrometry | Q30159818 | ||
| Conserved patterns in the Cu,Zn superoxide dismutase family. | Q30194350 | ||
| Superoxide dismutase folding/unfolding pathway: role of the metal ions in modulating structural and dynamical features. | Q30333003 | ||
| Glycation in Demetalated Superoxide Dismutase 1 Prevents Amyloid Aggregation and Produces Cytotoxic Ages Adducts | Q30393668 | ||
| Loss of metal ions, disulfide reduction and mutations related to familial ALS promote formation of amyloid-like aggregates from superoxide dismutase | Q33423010 | ||
| Aggregation of copper-zinc superoxide dismutase in familial and sporadic ALS | Q33742742 | ||
| Destabilization of apoprotein is insufficient to explain Cu,Zn-superoxide dismutase-linked ALS pathogenesis. | Q33897544 | ||
| Insights into SOD1-linked amyotrophic lateral sclerosis from NMR studies of Ni(2+)- and other metal-ion-substituted wild-type copper-zinc superoxide dismutases | Q33942778 | ||
| Alzheimer's amyloid fibrils: structure and assembly | Q33971270 | ||
| pH-dependent migration of copper(II) to the vacant zinc-binding site of zinc-free bovine erythrocyte superoxide dismutase | Q33971629 | ||
| In-cell NMR in E. coli to monitor maturation steps of hSOD1. | Q34009391 | ||
| Rationalization of the effects of mutations on peptide and protein aggregation rates. | Q34222395 | ||
| Design of small molecules that target metal-A{beta} species and regulate metal-induced A{beta} aggregation and neurotoxicity. | Q34438376 | ||
| Mechanisms of the copper-dependent turnover of the copper chaperone for superoxide dismutase | Q34501464 | ||
| Copper and zinc metallation status of copper-zinc superoxide dismutase from amyotrophic lateral sclerosis transgenic mice. | Q34509452 | ||
| Spinal cord endoplasmic reticulum stress associated with a microsomal accumulation of mutant superoxide dismutase-1 in an ALS model | Q34596280 | ||
| Glial nuclear aggregates of superoxide dismutase-1 are regularly present in patients with amyotrophic lateral sclerosis | Q34892327 | ||
| Misfolded proteins in Alzheimer's disease and type II diabetes. | Q35535599 | ||
| Superoxide dismutase 1 with mutations linked to familial amyotrophic lateral sclerosis possesses significant activity | Q35693516 | ||
| Membrane disruption and early events in the aggregation of the diabetes related peptide IAPP from a molecular perspective | Q35737643 | ||
| Formation of high molecular weight complexes of mutant Cu, Zn-superoxide dismutase in a mouse model for familial amyotrophic lateral sclerosis. | Q35818148 | ||
| Metal-free superoxide dismutase forms soluble oligomers under physiological conditions: a possible general mechanism for familial ALS | Q35854965 | ||
| Local unfolding of Cu, Zn superoxide dismutase monomer determines the morphology of fibrillar aggregates | Q35873804 | ||
| An over-oxidized form of superoxide dismutase found in sporadic amyotrophic lateral sclerosis with bulbar onset shares a toxic mechanism with mutant SOD1 | Q35882558 | ||
| Common molecular signature in SOD1 for both sporadic and familial amyotrophic lateral sclerosis. | Q35928006 | ||
| Soluble misfolded subfractions of mutant superoxide dismutase-1s are enriched in spinal cords throughout life in murine ALS models | Q35956902 | ||
| Copper-zinc superoxide dismutase and amyotrophic lateral sclerosis | Q36161189 | ||
| 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 | ||
| Copper homeostasis and neurodegenerative disorders (Alzheimer's, prion, and Parkinson's diseases and amyotrophic lateral sclerosis). | Q36505371 | ||
| Activation of superoxide dismutases: putting the metal to the pedal | Q36530953 | ||
| SOD1 exhibits allosteric frustration to facilitate metal binding affinity | Q36673087 | ||
| How do ALS-associated mutations in superoxide dismutase 1 promote aggregation of the protein? | Q36701609 | ||
| Structural similarity of wild-type and ALS-mutant superoxide dismutase-1 fibrils using limited proteolysis and atomic force microscopy | Q36991027 | ||
| Oxidized/misfolded superoxide dismutase-1: the cause of all amyotrophic lateral sclerosis? | Q37030015 | ||
| Transient structural distortion of metal-free Cu/Zn superoxide dismutase triggers aberrant oligomerization | Q37416520 | ||
| Metal deficiency increases aberrant hydrophobicity of mutant superoxide dismutases that cause amyotrophic lateral sclerosis | Q37448164 | ||
| Mitochondrial dysfunction in amyotrophic lateral sclerosis. | Q37588819 | ||
| Folding of human superoxide dismutase: disulfide reduction prevents dimerization and produces marginally stable monomers | Q37619322 | ||
| Mechanisms for activating Cu- and Zn-containing superoxide dismutase in the absence of the CCS Cu chaperone | Q37646146 | ||
| Transgenic mice carrying a human mutant superoxide dismutase transgene develop neuronal cytoskeletal pathology resembling human amyotrophic lateral sclerosis lesions | Q37688651 | ||
| SOD1 aggregation and ALS: role of metallation states and disulfide status | Q38075887 | ||
| An emerging role for misfolded wild-type SOD1 in sporadic ALS pathogenesis | Q38174873 | ||
| Decreased metallation and activity in subsets of mutant superoxide dismutases associated with familial amyotrophic lateral sclerosis. | Q38291855 | ||
| Development of bifunctional stilbene derivatives for targeting and modulating metal-amyloid-β species. | Q39466684 | ||
| Complete loss of post-translational modifications triggers fibrillar aggregation of SOD1 in the familial form of amyotrophic lateral sclerosis | Q39972533 | ||
| Binding affinity of amyloid oligomers to cellular membranes is a generic indicator of cellular dysfunction in protein misfolding diseases | Q41074727 | ||
| Pathological roles of wild-type cu, zn-superoxide dismutase in amyotrophic lateral sclerosis. | Q41820610 | ||
| Calcium ions promote superoxide dismutase 1 (SOD1) aggregation into non-fibrillar amyloid: a link to toxic effects of calcium overload in amyotrophic lateral sclerosis (ALS)? | Q41955617 | ||
| Impaired post-translational folding of familial ALS-linked Cu, Zn superoxide dismutase mutants | Q41969514 | ||
| A two-site mechanism for the inhibition of IAPP amyloidogenesis by zinc | Q41986965 | ||
| Oxygen-induced maturation of SOD1: a key role for disulfide formation by the copper chaperone CCS. | Q41987289 | ||
| Cellular toxicity of mutant SOD1 protein is linked to an easily soluble, non-aggregated form in vitro | Q42160937 | ||
| Fibrillar inclusions and motor neuron degeneration in transgenic mice expressing superoxide dismutase 1 with a disrupted copper-binding site | Q44070818 | ||
| Oxidation-induced misfolding and aggregation of superoxide dismutase and its implications for amyotrophic lateral sclerosis | Q44160891 | ||
| Mechanisms of biosynthesis of mammalian copper/zinc superoxide dismutase | Q44483335 | ||
| Dysregulation of intracellular copper homeostasis is common to transgenic mice expressing human mutant superoxide dismutase-1s regardless of their copper-binding abilities. | Q44642611 | ||
| Monomeric Cu,Zn-superoxide dismutase is a common misfolding intermediate in the oxidation models of sporadic and familial amyotrophic lateral sclerosis. | Q44735743 | ||
| Dissociation of human copper-zinc superoxide dismutase dimers using chaotrope and reductant. Insights into the molecular basis for dimer stability | Q45107835 | ||
| P275 | copyright license | Creative Commons Attribution | Q6905323 |
| P6216 | copyright status | copyrighted | Q50423863 |
| P433 | issue | 9 | |
| P407 | language of work or name | English | Q1860 |
| P921 | main subject | inorganic compound | Q190065 |
| enzyme | Q8047 | ||
| amyotrophic lateral sclerosis | Q206901 | ||
| P5008 | on focus list of Wikimedia project | ScienceSource | Q55439927 |
| P577 | publication date | 2017-08-29 | |
| P1433 | published in | Molecules | Q151332 |
| P1476 | title | The Role of Metal Binding in the Amyotrophic Lateral Sclerosis-Related Aggregation of Copper-Zinc Superoxide Dismutase | |
| P478 | volume | 22 |
| Q49483837 | ALSUntangled 43: copper |
| Q91955383 | Dysregulated biodynamics in metabolic attractor systems precede the emergence of amyotrophic lateral sclerosis |
| Q47233517 | Impaired Cu-Zn Superoxide Dismutase (SOD1) and Calcineurin (Cn) Interaction in ALS: A Presumed Consequence for TDP-43 and Zinc Aggregation in Tg SOD1G93A Rodent Spinal Cord Tissue. |
| Q57170405 | Ionic Homeostasis Maintenance in ALS: Focus on New Therapeutic Targets |
| Q89603352 | Structural basis of the zinc-induced cytoplasmic aggregation of the RNA-binding protein SFPQ |
| Q90078219 | Temperature-dependent irreversible conformational change of recombinant ADAMTS13 upon metal ion chelation |
| Q47831358 | Zinc, Carnosine, and Neurodegenerative Diseases. |
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