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

Degradation of amyotrophic lateral sclerosis-linked mutant Cu,Zn-superoxide dismutase proteins by macroautophagy and the proteasome.

The Journal of biological chemistry - 13 Oct 2006

Kabuta Tomohiro, Suzuki Yasuyuki, Wada Keiji

Abstract excerpt

Mutations in the Cu,Zn-superoxide dismutase (SOD1) gene cause approximately 20% of familial cases of amyotrophic lateral sclerosis (fALS). Accumulating evidence indicates that a gain of toxic function of mutant SOD1 proteins is the cause of the disease. It has also been shown that the ubiquitin-proteasome pathway plays a role in the clearance and toxicity of mutant SOD1. In this study, we investigated the...

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 Antibiotics, Antineoplastic

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

Share to Autophagy

Share to Chlorocebus aethiops

Share to Proteasome Endopeptidase Complex

Share to Protein Synthesis Inhibitors

Share to Subcellular Fractions

Share to Superoxide Dismutase

Source

Identifiers

PMID: 16920710
DOI: 10.1074/jbc.M603337200

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.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Degradation of amyotrophic lateral sclerosis-linked mutant Cu,Zn-superoxide dismutase proteins by macroautophagy and the proteasome.PMID 16920710Read ↗

Altered macroautophagy in the spinal cord of SOD1 mutant mice.Semantic proximity Read ↗

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

Misfolded CuZnSOD and amyotrophic lateral sclerosis.Semantic proximity Read ↗

Modulating Macroautophagy: A Neuronal PerspectiveSemantic proximity Read ↗

Macroautophagy--a novel Beta-amyloid peptide-generating pathway activated in Alzheimer's disease.Semantic proximity Read ↗

ALS-Related Mutant SOD1 Aggregates Interfere with Mitophagy by Sequestering the Autophagy Receptor Optineurin.Semantic proximity Read ↗

Mutant copper-zinc superoxide dismutase (SOD1) induces protein secretion pathway alterations and exosome release in astrocytes: implications for disease spreading and motor neuron pathology in amyotrophic lateral sclerosis.Semantic proximity Read ↗

SQSTM1, a protective factor of SOD1-linked motor neuron disease, regulates the accumulation and distribution of ubiquitinated protein aggregates in neuron.Semantic proximity Read ↗

Proteasomal degradation of mutant superoxide dismutases linked to amyotrophic lateral sclerosis.Semantic proximity Read ↗

Insoluble mutant SOD1 is partly oligoubiquitinated in amyotrophic lateral sclerosis mice.Semantic proximity Read ↗

SOD1 protein aggregates stimulate macropinocytosis in neurons to facilitate their propagation.Semantic proximity Read ↗

cIAPs promote the proteasomal degradation of mutant SOD1 linked to familial amyotrophic lateral sclerosis.Semantic proximity Read ↗

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