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

Minute quantities of misfolded mutant superoxide dismutase-1 cause amyotrophic lateral sclerosis.

Brain : a journal of neurology - 1 Jan 2004

Jonsson P Andreas, Ernhill Karin, Andersen Peter M, Bergemalm Daniel, Brännström Thomas, Gredal Ole, Nilsson Peter, Marklund Stefan L

Abstract excerpt

Mutant forms of superoxide dismutase-1 (SOD1) cause amyotrophic lateral sclerosis (ALS) by an unknown noxious mechanism. Using an antibody against a novel epitope in the G127insTGGG mutation, mutant SOD1 was studied for the first time in spinal cord and brain of an ALS patient. The level was below 0.5% of the SOD1 level in controls. In corresponding transgenic mice the content of mutant SOD1 was also low,...

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 Detergents

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

Share to Mice, Transgenic

Share to Solubility

Share to Spinal Cord

Share to Superoxide Dismutase

Share to Superoxide Dismutase-1

Share to Survival Analysis

Source

Identifiers

PMID: 14534160
DOI: 10.1093/brain/awh005

Genes

SOD1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 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

Minute quantities of misfolded mutant superoxide dismutase-1 cause amyotrophic lateral sclerosis.PMID 14534160Read ↗

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

Soluble misfolded subfractions of mutant superoxide dismutase-1s are enriched in spinal cords throughout life in murine ALS models.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 ↗

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

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

Oxidized/misfolded superoxide dismutase-1: the cause of all 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 ↗

Endoplasmic reticulum stress leads to accumulation of wild-type SOD1 aggregates associated with sporadic amyotrophic lateral sclerosis.Semantic proximity Read ↗

SOD1 oligomers in amyotrophic lateral sclerosis.Semantic proximity Read ↗

Accumulation of Misfolded SOD1 in Dorsal Root Ganglion Degenerating Proprioceptive Sensory Neurons of Transgenic Mice with Amyotrophic Lateral SclerosisSemantic proximity Read ↗

Oxidation-induced misfolding and aggregation of superoxide dismutase and its implications for amyotrophic lateral sclerosis.Semantic proximity Read ↗

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