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

Familial ALS-superoxide dismutases associate with mitochondria and shift their redox potentials.

Proceedings of the National Academy of Sciences of the United States of America - 12 Sept 2006

Ferri Alberto, Cozzolino Mauro, Crosio Claudia, Nencini Monica, Casciati Arianna, Gralla Edith Butler, Rotilio Giuseppe, Valentine Joan Selverstone, Carrì Maria Teresa

Abstract excerpt

Recent studies suggest that the toxicity of familial amyotrophic lateral sclerosis mutant Cu, Zn superoxide dismutase (SOD1) arises from its selective recruitment to mitochondria. Here we demonstrate that each of 12 different familial ALS-mutant SOD1s with widely differing biophysical properties...

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 Cysteine

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mitochondria

Share to Motor Neurons

Share to Oxidation-Reduction

Share to Superoxide Dismutase

Share to Superoxide Dismutase-1

Source

Open in PubMed Open full text

Identifiers

PMID: 16945901
DOI: 10.1073/pnas.0605814103
PMCID: PMC1557633

Genes

SOD1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-16945901-2026-09-02.2. 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

Familial ALS-superoxide dismutases associate with mitochondria and shift their redox potentials.PMID 16945901Read ↗

Oligomerization of mutant SOD1 in mitochondria of motoneuronal cells drives mitochondrial damage and cell toxicity.Semantic proximity Read ↗

In vivo pathogenic role of mutant SOD1 localized in the mitochondrial intermembrane space.Semantic proximity Read ↗

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

Mutant Cu, Zn superoxide dismutase that causes motoneuron degeneration is present in mitochondria in the CNS.Semantic proximity Read ↗

Mutant SOD1 from spinal cord of G93A rats is destabilized and binds to inner mitochondrial membrane.Semantic proximity Read ↗

Mitochondrial dysfunction and its role in motor neuron degeneration in ALS.Semantic proximity Read ↗

Copper-zinc superoxide dismutase and amyotrophic lateral sclerosis.Semantic proximity Read ↗

Mitochondrial dysfunction and amyotrophic lateral sclerosis.Semantic proximity Read ↗

Role of mitochondria in mutant SOD1 linked amyotrophic lateral sclerosis.Semantic proximity Read ↗

Mutant superoxide dismutase 1 forms aggregates in the brain mitochondrial matrix of amyotrophic lateral sclerosis mice.Semantic proximity Read ↗

Different regulation of wild-type and mutant Cu,Zn superoxide dismutase localization in mammalian mitochondria.Semantic proximity Read ↗

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