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

The potential role of misfolded wild-type SOD1 protein in sporadic amyotrophic lateral sclerosis (ALS): a review of the evidence.

Neurobiology of disease - 1 Nov 2025

Marlow Thomas R, Bowden Katie M, Collins Mark O, Shaw Pamela J

Abstract excerpt

Amyotrophic lateral sclerosis (ALS) is a progressive neurodegenerative disorder characterised by the selective loss of motor neurons in the motor cortex, brainstem and spinal cord. In 1993, the first ALS-linked gene mutations were identified in the Cu,Zn superoxide dismutase (SOD1) gene, which account for approximately 20 % of familial ALS cases. The mechanism of toxicity in this subset of patients is thought to...

Read the complete abstract on PubMed

Topics

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

Share to Amyotrophic Lateral Sclerosis
Share to SOD1 gene

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Motor Neurons

Share to Mutation

Share to Protein Folding

Share to Superoxide Dismutase-1

Source

Identifiers

PMID: 41005573
DOI: 10.1016/j.nbd.2025.107124

Genes

SOD1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 16 Oct 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The potential role of misfolded wild-type SOD1 protein in sporadic amyotrophic lateral sclerosis (ALS): a review of the evidence.PMID 41005573Read ↗

An emerging role for misfolded wild-type SOD1 in sporadic ALS pathogenesisSemantic proximity Read ↗

Protein misfolding in the late-onset neurodegenerative diseases: common themes and the unique case of amyotrophic lateral sclerosis.Semantic proximity Read ↗

Many roads lead to Rome? Multiple modes of Cu,Zn superoxide dismutase destabilization, misfolding and aggregation in amyotrophic lateral sclerosis.Semantic proximity Read ↗

Misfolded CuZnSOD and amyotrophic lateral sclerosis.Semantic proximity Read ↗

Pathological Roles of Wild-Type Cu, Zn-Superoxide Dismutase in Amyotrophic Lateral SclerosisSemantic proximity Read ↗

SOD1 in neurotoxicity and its controversial roles in SOD1 mutation-negative ALS.Semantic proximity Read ↗

Structure, folding, and misfolding of Cu,Zn superoxide dismutase in amyotrophic lateral sclerosis.Semantic proximity Read ↗

A Proposed Mechanism for Neurodegeneration in Movement Disorders Characterized by Metal Dyshomeostasis and Oxidative Stress.Semantic proximity Read ↗

Oxidized/misfolded superoxide dismutase-1: the cause of all amyotrophic lateral sclerosis?Semantic proximity Read ↗

Mutant SOD1 instability: implications for toxicity in amyotrophic lateral sclerosis.Semantic proximity Read ↗

Misfolded SOD1 Accumulation and Mitochondrial Association Contribute to the Selective Vulnerability of Motor Neurons in Familial ALS: Correlation to Human Disease.Semantic proximity Read ↗

Protein misdirection inside and outside motor neurons in Amyotrophic Lateral Sclerosis (ALS): a possible clue for therapeutic strategies.Semantic proximity Read ↗

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