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

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

Journal of neurochemistry - 1 Jan 2014

Ayers Jacob, Lelie Herman, Workman Aron, Prudencio Mercedes, Brown Hilda, Fromholt Susan, Valentine Joan, Whitelegge Julian, Borchelt David

Abstract excerpt

Mutations in superoxide dismutase 1 (SOD1) associated with familial amyotrophic lateral sclerosis induce misfolding and aggregation of the protein with the inherent propensity of mutant SOD1 to aggregate generally correlating, with a few exceptions, to the duration of illness in patients with the same mutation. One notable exception was the D101N variant, which has been described as wild-type-like. The D101N...

Read the complete abstract on PubMed

Topics

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

Share to SOD1 gene
Share to HEK293 Cells

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Motor Neuron Disease

Share to Mutation

Share to Protein Folding

Share to Superoxide Dismutase

Share to Superoxide Dismutase-1

Source

Open in PubMed Open full text

Identifiers

PMID: 24032979
DOI: 10.1111/jnc.12451
PMCID: PMC3971632

Genes

SOD1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Distinctive features of the D101N and D101G variants of superoxide dismutase 1; two mutations that produce rapidly progressing motor neuron disease.PMID 24032979Read ↗

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

How do ALS-associated mutations in superoxide dismutase 1 promote aggregation of the protein?Semantic proximity Read ↗

Variation in aggregation propensities among ALS-associated variants of SOD1: correlation to human disease.Semantic proximity Read ↗

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

Cellular analysis of SOD1 protein-aggregation propensity and toxicity: a case of ALS with slow progression harboring homozygous SOD1-D92G mutation.Semantic proximity Read ↗

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

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

Nonamyloid aggregates arising from mature copper/zinc superoxide dismutases resemble those observed in amyotrophic lateral sclerosis.Semantic proximity Read ↗

Superoxide dismutase 1 encoding mutations linked to ALS adopts a spectrum of misfolded states.Semantic proximity Read ↗

Toxic SOD1 trimers are off-pathway in the formation of amyloid-like fibrils in ALS.Semantic proximity Read ↗

Nonnative SOD1 trimer is toxic to motor neurons in a model of amyotrophic lateral sclerosis.Semantic proximity Read ↗

Pathogenic superoxide dismutase structure, folding, aggregation and turnover.Semantic proximity Read ↗

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