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

Wild-type Cu/Zn superoxide dismutase stabilizes mutant variants by heterodimerization.

Neurobiology of disease - 1 Feb 2014

Weichert Anna, Besemer Anna S, Liebl Martina, Hellmann Nadja, Koziollek-Drechsler Ingrid, Ip Philbert, Decker Heinz, Robertson Janice, Chakrabartty Avijit, Behl Christian, Clement Albrecht M

Abstract excerpt

Mutations in the gene encoding Cu/Zn superoxide dismutase (SOD1) are responsible for a subset of amyotrophic lateral sclerosis cases presumably by the acquisition of as yet unknown toxic properties. Additional overexpression of wild-type SOD1 in mutant SOD1 transgenic mice did not improve but rather accelerated the disease course. Recently, it was documented that the presence of wild-type SOD1 (SOD(WT)) reduced...

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 Mutation

Share to Protein Multimerization

Share to Superoxide Dismutase

Share to Superoxide Dismutase-1

Source

Identifiers

PMID: 24200866
DOI: 10.1016/j.nbd.2013.10.027

Genes

SOD1

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Wild-type Cu/Zn superoxide dismutase stabilizes mutant variants by heterodimerization.PMID 24200866Read ↗

Wild-type Cu/Zn superoxide dismutase (SOD1) does not facilitate, but impedes the formation of protein aggregates of amyotrophic lateral sclerosis causing mutant SOD1.Semantic proximity Read ↗

Characterization of the activity, aggregation, and toxicity of heterodimers of WT and ALS-associated mutant Sod1.Semantic proximity Read ↗

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

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

Molecular and pharmacological chaperones for SOD1.Semantic proximity Read ↗

Copper-binding-site-null SOD1 causes ALS in transgenic mice: aggregates of non-native SOD1 delineate a common feature.Semantic proximity Read ↗

Dimerization, oligomerization, and aggregation of human amyotrophic lateral sclerosis copper/zinc superoxide dismutase 1 protein mutant forms in live cells.Semantic proximity Read ↗

Structural Properties and Interaction Partners of Familial ALS-Associated SOD1 MutantsSemantic proximity Read ↗

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

Strategies for stabilizing superoxide dismutase (SOD1), the protein destabilized in the most common form of familial amyotrophic lateral sclerosis.Semantic proximity Read ↗

Heteroaggregation of Wild-Type and ALS Mutant SOD1.Semantic proximity Read ↗

Complete loss of post-translational modifications triggers fibrillar aggregation of SOD1 in the familial form of amyotrophic lateral sclerosis.Semantic proximity Read ↗

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