Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Pro-Oxidant Activity of an ALS-Linked SOD1 Mutant in Zn-Deficient Form.

Molecules (Basel, Switzerland) - 7 Aug 2020

Nagao Chise, Kuroi Kunisato, Wakabayashi Taiyu, Nakabayashi Takakazu

Abstract excerpt

Cu, Zn superoxide dismutase (SOD1) is a representative antioxidant enzyme that catalyzes dismutation of reactive oxygen species in cells. However, (E,E)-SOD1 mutants in which both copper and zinc ions were deleted exhibit pro-oxidant activity, contrary to their antioxidant nature, at physiological temperatures, following denaturation and subsequent recombination of Cu2+. This oxidative property is likely related...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Kinetics
Share to Models, Molecular
Share to Mutation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Protein Conformation, beta-Strand

Share to Reactive Oxygen Species

Share to Superoxide Dismutase-1

Source

Open in PubMed Open full text

Identifiers

PMID: 32784718
DOI: 10.3390/molecules25163600
PMCID: PMC7464938

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Pro-Oxidant Activity of an ALS-Linked SOD1 Mutant in Zn-Deficient Form.PMID 32784718Read ↗

The structural analysis of the pro-oxidant copper-binding site of denatured apo-H43R SOD1 and the elucidation of the origin of the acquisition of the pro-oxidant activity.Semantic proximity Read ↗

Structural instability and Cu-dependent pro-oxidant activity acquired by the apo form of mutant SOD1 associated with amyotrophic lateral sclerosis.Semantic proximity Read ↗

Oxidative misfolding of Cu/Zn-superoxide dismutase triggered by non-canonical intramolecular disulfide formation.Semantic proximity Read ↗

SOD1 gains pro-oxidant activity upon aberrant oligomerization: change in enzymatic activity by intramolecular disulfide bond cleavage.Semantic proximity Read ↗

Disulfide-reduced ALS variants of Cu, Zn superoxide dismutase exhibit increased populations of unfolded species.Semantic proximity Read ↗

Production of Human Cu,Zn SOD with Higher Activity and Lower Toxicity in E. coli via Mutation of Free Cysteine Residues.Semantic proximity Read ↗

Denaturational stress induces formation of zinc-deficient monomers of Cu,Zn superoxide dismutase: implications for pathogenesis in amyotrophic lateral sclerosis.Semantic proximity Read ↗

Enhancement of Oxidative Reaction by the Intramolecular Electron Transfer between the Coordinated Redox-Active Metal Ions in SOD1.Semantic proximity Read ↗

The structure, redox chemistry and motor neuron toxicity of heterodimeric zinc-deficient SOD1-implications for the toxic gain of function observed in ALS.Semantic proximity Read ↗

Hydrogen peroxide damages the zinc-binding site of zinc-deficient Cu,Zn superoxide dismutase.Semantic proximity Read ↗

SOD1 Catalyses Thiol Oxidation to ThiosulfinatesSemantic proximity Read ↗

Mutation/metal deficiency in the "electrostatic loop" enhanced aggregation process in apo/holo SOD1 variants: implications for ALS diseasesSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.