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

A limited role for disulfide cross-linking in the aggregation of mutant SOD1 linked to familial amyotrophic lateral sclerosis.

The Journal of biological chemistry - 16 May 2008

Karch Celeste M, Borchelt David R

Abstract excerpt

One of the mechanisms by which mutations in superoxide dismutase 1 (SOD1) cause familial amyotrophic lateral sclerosis (fALS) is proposed to involve the accumulation of detergent-insoluble, disulfide-cross-linked, mutant protein. Recent studies have implicated cysteine residues at positions 6 and...

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 Cross-Linking Reagents
Share to Cysteine

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Disulfides

Share to Mice, Transgenic

Share to Protein Folding

Share to Superoxide Dismutase

Share to Superoxide Dismutase-1

Source

Open in PubMed Open full text

Identifiers

PMID: 18316367
DOI: 10.1074/jbc.M800564200
PMCID: PMC2376231

Genes

SOD1

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-18316367-2026-09-02.2. 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

A limited role for disulfide cross-linking in the aggregation of mutant SOD1 linked to familial amyotrophic lateral sclerosis.PMID 18316367Read ↗

Role of disulfide cross-linking of mutant SOD1 in the formation of inclusion-body-like structures.Semantic proximity Read ↗

Cysteine 111 affects aggregation and cytotoxicity of mutant Cu,Zn-superoxide dismutase associated with familial amyotrophic lateral sclerosis.Semantic proximity Read ↗

Role of mutant SOD1 disulfide oxidation and aggregation in the pathogenesis of familial ALS.Semantic proximity Read ↗

An intersubunit disulfide bond prevents in vitro aggregation of a superoxide dismutase-1 mutant linked to familial amytrophic lateral sclerosis.Semantic proximity Read ↗

Disulfide bond mediates aggregation, toxicity, and ubiquitylation of familial amyotrophic lateral sclerosis-linked mutant SOD1.Semantic proximity Read ↗

Decreased stability and increased formation of soluble aggregates by immature superoxide dismutase do not account for disease severity in ALS.Semantic proximity Read ↗

Disulfide scrambling describes the oligomer formation of superoxide dismutase (SOD1) proteins in the familial form of amyotrophic lateral sclerosis.Semantic proximity Read ↗

Aggregation modulating elements in mutant human superoxide dismutase 1.Semantic proximity Read ↗

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

Intermolecular transmission of superoxide dismutase 1 misfolding in living cells.Semantic 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 ↗

Aggregation-triggering segments of SOD1 fibril formation support a common pathway for familial and sporadic ALS.Semantic proximity Read ↗

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