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

Histological evidence of redox system breakdown caused by superoxide dismutase 1 (SOD1) aggregation is common to SOD1-mutated motor neurons in humans and animal models.

Acta neuropathologica - 1 Feb 2004

Kato Shinsuke, Saeki Yusuke, Aoki Masashi, Nagai Makiko, Ishigaki Aya, Itoyama Yasuto, Kato Masako, Asayama Kohtaro, Awaya Akira, Hirano Asao, Ohama Eisaku

Abstract excerpt

Living cells produce reactive oxygen species (ROSs). To protect themselves from these ROSs, the cells have developed both an antioxidant system containing superoxide dismutase 1 (SOD1) and a redox system including peroxiredoxin2 (Prx2, thioredoxin peroxidase) and glutathione peroxidase1 (GPx1): S...

Read the complete abstract on PubMed

Topics

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

Share to Glutathione Peroxidase
Share to Glutathione Peroxidase GPX1

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Lewy Bodies

Share to Motor Neurons

Share to Peroxidases

Share to Peroxiredoxins

Share to Spinal Cord

Share to Superoxide Dismutase-1

Source

Identifiers

PMID: 14648077
DOI: 10.1007/s00401-003-0791-1

Genes

SOD1

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-14648077-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Histological evidence of redox system breakdown caused by superoxide dismutase 1 (SOD1) aggregation is common to SOD1-mutated motor neurons in humans and animal models.PMID 14648077Read ↗

Redox system expression in the motor neurons in amyotrophic lateral sclerosis (ALS): immunohistochemical studies on sporadic ALS, superoxide dismutase 1 (SOD1)-mutated familial ALS, and SOD1-mutated ALS animal models.Semantic proximity Read ↗

Advanced glycation endproduct-modified superoxide dismutase-1 (SOD1)-positive inclusions are common to familial amyotrophic lateral sclerosis patients with SOD1 gene mutations and transgenic mice expressing human SOD1 with a G85R mutation.Semantic proximity Read ↗

Formation of advanced glycation end-product-modified superoxide dismutase-1 (SOD1) is one of the mechanisms responsible for inclusions common to familial amyotrophic lateral sclerosis patients with SOD1 gene mutation, and transgenic mice expressing human SOD1 gene mutation.Semantic proximity Read ↗

Highlight Commentary on "Redox proteomics analysis of oxidatively modified proteins in G93A-SOD1 transgenic mice--a model of familial amyotrophic lateral sclerosis".Semantic proximity Read ↗

Selective formation of certain advanced glycation end products in spinal cord astrocytes of humans and mice with superoxide dismutase-1 mutation.Semantic proximity Read ↗

Overexpression of ferroptosis defense enzyme Gpx4 retards motor neuron disease of SOD1G93A mice.Semantic proximity Read ↗

Conversion to the amyotrophic lateral sclerosis phenotype is associated with intermolecular linked insoluble aggregates of SOD1 in mitochondria.Semantic proximity Read ↗

New consensus research on neuropathological aspects of familial amyotrophic lateral sclerosis with superoxide dismutase 1 (SOD1) gene mutations: inclusions containing SOD1 in neurons and astrocytes.Semantic proximity Read ↗

Oxidative stress in ALS: key role in motor neuron injury and therapeutic target.Semantic proximity Read ↗

SOD1 mutations disrupt redox-sensitive Rac regulation of NADPH oxidase in a familial ALS model.Semantic proximity Read ↗

Monomeric Cu,Zn-superoxide dismutase is a common misfolding intermediate in the oxidation models of sporadic and familial amyotrophic lateral sclerosis.Semantic proximity Read ↗

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

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