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

Fast and slow strains of misfolded mutant superoxide dismutase 1 in familial amyotrophic lateral sclerosis.

Acta neuropathologica communications - 25 Feb 2026

Xu Guilian, Dillon Kristy, Lopez Amanda, Brkic Selma, Fromholt Susan, Ostrow Lyle W, Glass Jonathan D, Chakrabarty Paramita, Ayers Jacob I, Borchelt David R

Abstract excerpt

Mutations in superoxide dismutase 1 (SOD1) account for ~ 10% of familial amyotrophic lateral sclerosis (fALS) cases. Most SOD1 ALS cases show a 2–5 year clinical course, but a subset of patients exhibit a slowly progressing illness lasting 10–20 years. Substantial evidence indicates that disease-causing mutations in SOD1 promote misfolding and aggregation. Spinal tissue homogenates from paralyzed transgenic mice...

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 Disease Models, Animal

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Disease Progression

Share to Mice, Transgenic

Share to Protein Folding

Share to Spinal Cord

Share to Superoxide Dismutase-1

Source

Open in PubMed Open full text

Identifiers

PMID: 41742309
DOI: 10.1186/s40478-026-02262-6
PMCID: PMC13041472

Genes

SOD1

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Fast and slow strains of misfolded mutant superoxide dismutase 1 in familial amyotrophic lateral sclerosis.PMID 41742309Read ↗

Spinal cord homogenates from SOD1 familial amyotrophic lateral sclerosis induce SOD1 aggregation in living cells.Semantic proximity Read ↗

Variation in the vulnerability of mice expressing human superoxide dismutase 1 to prion-like seeding: a study of the influence of primary amino acid sequence.Semantic proximity Read ↗

Experimental transmissibility of mutant SOD1 motor neuron disease.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 ↗

Distinct conformers of transmissible misfolded SOD1 distinguish human SOD1-FALS from other forms of familial and sporadic ALS.Semantic proximity Read ↗

Prion-like propagation of mutant SOD1 misfolding and motor neuron disease spread along neuroanatomical pathwaysSemantic proximity Read ↗

Distinctive features of the D101N and D101G variants of superoxide dismutase 1; two mutations that produce rapidly progressing motor neuron disease.Semantic proximity Read ↗

SOD1-positive aggregate accumulation in the CNS predicts slower disease progression and increased longevity in a mutant SOD1 mouse model of ALSSemantic proximity Read ↗

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

Direct observation of prion-like propagation of protein misfolding templated by pathogenic mutants.Semantic proximity Read ↗

Minute quantities of misfolded mutant superoxide dismutase-1 cause amyotrophic lateral sclerosis.Semantic proximity Read ↗

Mutant SOD1 aggregates formed in vitro and in cultured cells are polymorphic and differ from those arising in the CNS.Semantic proximity Read ↗

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