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

Insight into the Autosomal-Dominant Inheritance Pattern of SOD1-Associated ALS from Native Mass Spectrometry.

Journal of molecular biology - 20 Nov 2020

Cveticanin Jelena, Mondal Tridib, Meiering Elizabeth M, Sharon Michal, Horovitz Amnon

Abstract excerpt

About 20% of all familial amyotrophic lateral sclerosis (ALS) cases are associated with mutations in superoxide dismutase (SOD1), a homodimeric protein. The disease has an autosomal-dominant inheritance pattern. It is, therefore, important to determine whether wild-type and mutant SOD1 subunits self-associate randomly or preferentially. A measure for the extent of bias in subunit association is the coupling...

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 Gene Expression Regulation, Enzymologic

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mass Spectrometry

Share to Mutant Proteins

Share to Mutation

Share to Protein Conformation

Share to Protein Subunits

Share to Superoxide Dismutase-1

Source

Identifiers

PMID: 33058881
DOI: 10.1016/j.jmb.2020.09.025

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

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

Insight into the Autosomal-Dominant Inheritance Pattern of SOD1-Associated ALS from Native Mass Spectrometry.PMID 33058881Read ↗

Insight into the autosomal-dominant inheritance pattern of SOD1-associated ALS from native mass spectrometrySemantic 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 ↗

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

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

Familial amyotrophic lateral sclerosis-linked mutant SOD1 aberrantly interacts with tubulin.Semantic proximity Read ↗

Gibbs Energy of Superoxide Dismutase Heterodimerization Accounts for Variable Survival in Amyotrophic Lateral Sclerosis.Semantic proximity Read ↗

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

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

The folding, dimerization and allosteric landscapes of the ALS protein SOD1: a comprehensive mutational atlasSemantic proximity Read ↗

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 ↗

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

TNF receptor associated factor 6 interacts with ALS-linked misfolded superoxide dismutase 1 and promotes aggregationSemantic proximity Read ↗

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