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

Effects of gem-dihydroperoxides against mutant copper‑zinc superoxide dismutase-mediated neurotoxicity.

Molecular and cellular neurosciences - 1 Oct 2018

Ueda Tomoyuki, Inden Masatoshi, Asaka Yuta, Masaki Yuji, Kurita Hisaka, Tanaka Wakako, Yamaguchi Eiji, Itoh Akichika, Hozumi Isao

Abstract excerpt

Amyotrophic lateral sclerosis (ALS) is a neurodegenerative disorder characterized by progressive muscle weakness, paralysis, and death. Although its neuropathology is well investigated, currently, effective treatments are unavailable. The mechanism of ALS involves the aggregation and accumulation of several mutant proteins, including mutant copper‑zinc superoxide dismutase (SOD1), TAR DNA binding protein 43 kDa...

Read the complete abstract on PubMed

Topics

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

Share to Cell Line, Tumor
Share to Free Radical Scavengers

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Neurons

Share to Neuroprotective Agents

Share to Oxidative Stress

Share to Peroxides

Share to Superoxide Dismutase-1

Source

Identifiers

PMID: 30193933
DOI: 10.1016/j.mcn.2018.09.001

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

Effects of gem-dihydroperoxides against mutant copper‑zinc superoxide dismutase-mediated neurotoxicity.PMID 30193933Read ↗

Neuroprotection by monocarbonyl dimethoxycurcumin C: ameliorating the toxicity of mutant TDP-43 via HO-1.Semantic proximity Read ↗

Role of Oxidative Stress in the Pathogenesis of Amyotrophic Lateral Sclerosis: Antioxidant Metalloenzymes and Therapeutic Strategies.Semantic proximity Read ↗

Novel chemical inhibitor against SOD1 misfolding and aggregation protects neuron-loss and ameliorates disease symptoms in ALS mouse model.Semantic proximity Read ↗

Bisdemethoxycurcumin, a novel potent polyphenolic compound, effectively inhibits the formation of amyloid aggregates in ALS-associated hSOD1 mutant (L38R).Semantic proximity Read ↗

EPI-589, a redox-active neuroprotectant, potently protects cultured cells from oxidative stress and alleviates symptomatic and pathological progression of motor neuron disease in the wobbler mouseSemantic proximity Read ↗

Intracellular spatially-targeted chemical chaperones increase native state stability of mutant SOD1 barrel.Semantic proximity Read ↗

A novel SOD1-dependent mechanism for the iron-induced production of toxic SOD1 and oxidative stress that initiates ALSSemantic proximity Read ↗

Copper-containing ROS-scavenging nanozyme paradoxically drives α-synucleinopathy by amplifying nitrosative stressSemantic proximity Read ↗

MG132 enhances neurite outgrowth in neurons overexpressing mutant TAR DNA-binding protein-43 via increase of HO-1.Semantic proximity Read ↗

Enhanced oxidative damage by the familial amyotrophic lateral sclerosis-associated Cu,Zn-superoxide dismutase mutants.Semantic proximity Read ↗

Glutaredoxin 2 prevents aggregation of mutant SOD1 in mitochondria and abolishes its toxicity.Semantic proximity Read ↗

Implications of fALS Mutations on Sod1 Function and Oligomerization in Cell Models.Semantic proximity Read ↗

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