ArticleProceedings of the National Academy of Sciences of the United States of America1992
Atomic structures of wild-type and thermostable mutant recombinant human Cu,Zn superoxide dismutase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 94 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
94 citing papers in PubMed.
- N-Truncated Superoxide Dismutase-1 in Cerebrospinal Fluid Is Folded and Active.Journal of neurochemistry · 2026Article
- The structure, redox chemistry and motor neuron toxicity of heterodimeric zinc-deficient SOD1-implications for the toxic gain of function observed in ALS.Neurobiology of disease · 2025Article
- The structure, redox chemistry and motor neuron toxicity of heterodimeric zinc-deficient SOD1-Implications for the toxic gain of function observed in ALS.bioRxiv : the preprint server for biology · 2025Article
- Therapeutic Applications and Mechanisms of Superoxide Dismutase (SOD) in Different Pathogenesis.Biomolecules · 2025Review
- Bioactive Ingredients, Functions, and Development Strategies ofFood science & nutrition · 2025Review
- Inhibitory effect of Fisetin against the aggregation process of SOD1 E100K mutant: computer-based drug design as a potential therapeutic for ALS disease.Frontiers in chemistry · 2025Article
- Molecular Mechanisms of Aggregation of Canine SOD1 E40K Amyloidogenic Mutant Protein.Molecules (Basel, Switzerland) · 2022Article
- Structural analysis of the overoxidized Cu/Zn-superoxide dismutase in ROS-induced ALS filament formation.Communications biology · 2022Article
- Toxic SOD1 trimers are off-pathway in the formation of amyloid-like fibrils in ALS.Biophysical journal · 2022Article
- Chlorogenic Acid Attenuates Oxidative Stress-Induced Intestinal Epithelium Injury by Co-Regulating the PI3K/Akt and IκBα/NF-κB Signaling.Antioxidants (Basel, Switzerland) · 2021Article
- N-terminal Domain of TDP43 Enhances Liquid-Liquid Phase Separation of Globular Proteins.Journal of molecular biology · 2021Article
- Anion-Dependent Synthesis of Cu(II) Complexes with 2-(1Bioinorganic chemistry and applications · 2021Article
- [Selenium and zinc: "antioxidants" for healthy aging?]Zeitschrift fur Gerontologie und Geriatrie · 2020Review
- Nucleation and kinetics of SOD1 aggregation in human cells for ALS1.Molecular and cellular biochemistry · 2020Article
- A Novel SOD1 Intermediate Oligomer, Role of Free Thiols and Disulfide Exchange.Frontiers in neuroscience · 2020Article
- Integrative Protein Modeling in RosettaNMR from Sparse Paramagnetic Restraints.Structure (London, England : 1993) · 2019Article
- Experimental Mutations in Superoxide Dismutase 1 Provide Insight into Potential Mechanisms Involved in Aberrant Aggregation in Familial Amyotrophic Lateral Sclerosis.G3 (Bethesda, Md.) · 2019Article
- Effects of maturation on the conformational free-energy landscape of SOD1.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Caffeine Intake and Its Association with Body Composition Measures and Macronutrient Intakes in People Living with HIV in the Miami Adult Studies on HIV Cohort.Journal of caffeine and adenosine research · 2018Article
- Pathological hydrogen peroxide triggers the fibrillization of wild-type SOD1 via sulfenic acid modification of Cys-111.Cell death & disease · 2018Article
34 more citing papers are in PubMed but not listed here.
Corrections and comments
- Erratum issued
Authors and funding
3 authors.
Funding
Abstract
Superoxide dismutase enzymes protect aerobic organisms from oxygen-mediated free-radical damage. Crystallographic structures of recombinant human Cu,Zn superoxide dismutase have been determined, refined, and analyzed at 2.5 A resolution for wild-type and a designed thermostable double-mutant enzyme (Cys-6----Ala, Cys-111----Ser). The 10 subunits (five dimers) in the crystallographic asymmetric unit form an unusual stable open lattice with 80-A-diameter channels. The 10 independently fit and refined subunits provide high accuracy, error analysis, and insights on loop conformations. There is a helix dipole interaction with the Zn site, and 14 residues form two or more structurally conserved side-chain to main-chain hydrogen bonds that appear critical to active-site architecture, loop conformation, and the increased stability resulting from the Cys-111----Ser mutation.
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