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

Novel mutations in an otherwise strictly conserved domain of CuZn superoxide dismutase.

Molecular and cellular biochemistry - 1 Mar 1997

Luche R M, Maiwald R, Carlson E J, Epstein C J

Abstract excerpt

All mutations in the human gene for CuZn superoxide dismutase (CuZnSOD) reported to date are associated with the disease amyotrophic lateral sclerosis (ALS). These mutations, mostly of a familial nature (ALS 1, MIM 105400), span all of the coding region of this enzyme except for a highly conserve...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Sequence
Share to Conserved Sequence
Share to SOD1 gene

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Molecular Sequence Data

Share to Mutation

Share to Superoxide Dismutase

Source

Identifiers

PMID: 9062909
DOI: 10.1023/a:1006871524623

Genes

SOD1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-9062909-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Novel mutations in an otherwise strictly conserved domain of CuZn superoxide dismutase.PMID 9062909Read ↗

Identification of three novel mutations in the gene for Cu/Zn superoxide dismutase in patients with familial amyotrophic lateral sclerosis.Semantic proximity Read ↗

A novel variant of human superoxide dismutase 1 harboring amyotrophic lateral sclerosis-associated and experimental mutations in metal-binding residues and free cysteines lacks toxicity in vivo.Semantic proximity Read ↗

Novel in-frame duplication variant of SOD1 in a Japanese family with familial amyotrophic lateral sclerosis.Semantic proximity Read ↗

Transgenics, toxicity and therapeutics in rodent models of mutant SOD1-mediated familial ALS.Semantic proximity Read ↗

Sixteen novel mutations in the Cu/Zn superoxide dismutase gene in amyotrophic lateral sclerosis: a decade of discoveries, defects and disputesSemantic proximity Read ↗

Motor neuron degeneration in mice that express a human Cu,Zn superoxide dismutase mutation.Semantic proximity Read ↗

A novel p.E121G SOD1 mutation in slowly progressive form of amyotrophic lateral sclerosis induces cytoplasmic aggregates in cultured motor neurons and reduces cell viability.Semantic proximity Read ↗

Mitochondrial defects in transgenic mice expressing Cu,Zn superoxide dismutase mutations: the role of copper chaperone for SOD1.Semantic proximity Read ↗

Exon 5 encoded domain is not required for the toxic function of mutant SOD1 but essential for the dismutase activity: identification and characterization of two new SOD1 mutations associated with familial amyotrophic lateral sclerosis.Semantic proximity Read ↗

Identification of six novel SOD1 gene mutations in familial amyotrophic lateral sclerosis.Semantic proximity Read ↗

Characterization of three yeast copper-zinc superoxide dismutase mutants analogous to those coded for in familial amyotrophic lateral sclerosis.Semantic proximity Read ↗

Copper chaperone for superoxide dismutase is essential to activate mammalian Cu/Zn superoxide dismutase.Semantic proximity Read ↗

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