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

Simple and defined method to detect the SOD-1 mutants from patients with familial amyotrophic lateral sclerosis by mass spectrometry.

Journal of neuroscience methods - 1 Jun 1998

Nakanishi T, Kishikawa M, Miyazaki A, Shimizu A, Ogawa Y, Sakoda S, Ohi T, Shoji H

Abstract excerpt

Mutations in Cu/Zn superoxide dismutase (SOD1) cause a subset of cases of familial amyotrophic lateral sclerosis (FALS). We established a simple and defined method to detect the mutant SODI in erythrocytes by electrospray ionization mass spectrometry (ESIMS) using materials precipitated with specific antiserum. Hemolysate was mixed with anti-SOD1 antiserum and the generated precipitate, which was soluble in the...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Substitution
Share to DNA

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

Share to DNA Mutational Analysis

Share to Erythrocytes

Share to Genetic Testing

Share to Mutation

Share to Precipitin Tests

Share to Superoxide Dismutase

Source

Identifiers

PMID: 9696308
DOI: 10.1016/s0165-0270(98)00012-0

Genes

SOD1

Variants

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. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Simple and defined method to detect the SOD-1 mutants from patients with familial amyotrophic lateral sclerosis by mass spectrometry.PMID 9696308Read ↗

A systematic immunoprecipitation approach reinforces the concept of common conformational alterations in amyotrophic lateral sclerosis-linked SOD1 mutants.Semantic proximity Read ↗

Trimeric superoxide dismutase 1 antibody as a universal biomarker for ALSSemantic proximity Read ↗

Stability of mutant superoxide dismutase-1 associated with familial amyotrophic lateral sclerosis determines the manner of copper release and induction of thioredoxin in erythrocytes.Semantic proximity Read ↗

Novel chemical inhibitor against SOD1 misfolding and aggregation protects neuron-loss and ameliorates disease symptoms in ALS mouse model.Semantic proximity Read ↗

Identification of two novel mutations in the Cu/Zn superoxide dismutase gene with familial amyotrophic lateral sclerosis: mass spectrometric and genomic analyses.Semantic proximity Read ↗

Specific analysis of SOD1 enzymatic activity in CSF from ALS patients with and without SOD1 mutations.Semantic proximity Read ↗

MS785-MS27, a Commercially Available Antibody Cocktail against Misfolded SOD1, Recognizes Various Conformation-disordered SOD1 Species Lacking the Incorporated Zn ionSemantic proximity Read ↗

Pathological Roles of Wild-Type Cu, Zn-Superoxide Dismutase in Amyotrophic Lateral SclerosisSemantic proximity Read ↗

A novel monoclonal antibody reveals a conformational alteration shared by amyotrophic lateral sclerosis-linked SOD1 mutants.Semantic proximity Read ↗

Mitochondrial proteomic analysis of a cell line model of familial amyotrophic lateral sclerosis.Semantic proximity Read ↗

Structural Analysis of SOD1 Fibrils with Mass Spectrometry, Limited Proteolysis, and Atomic Force Microscopy (AFM).Semantic proximity Read ↗

A small-molecule inhibitor of SOD1-Derlin-1 interaction ameliorates pathology in an ALS mouse modelSemantic proximity Read ↗

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