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

Different immunoreactivity against monoclonal antibodies between wild-type and mutant copper/zinc superoxide dismutase linked to amyotrophic lateral sclerosis.

The Journal of biological chemistry - 11 Feb 2005

Fujiwara Noriko, Miyamoto Yasuhide, Ogasahara Kyoko, Takahashi Motoko, Ikegami Takahisa, Takamiya Rina, Suzuki Keiichiro, Taniguchi Naoyuki

Abstract excerpt

Although more than 100 mutations have been identified in the copper/zinc superoxide dismutase (Cu/Zn-SOD) in familial amyotrophic lateral sclerosis (FALS), the mechanism responsible for FALS remains unclear. The finding of the present study shows that FALS-causing mutant Cu/Zn-SOD proteins (FALS mutant SODs), but not wild-type SOD, are barely detected by three monoclonal antibodies (mAbs) in Western blot...

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 Antibodies, Monoclonal

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Circular Dichroism

Share to Dithiothreitol

Share to Enzyme-Linked Immunosorbent Assay

Share to Sodium Dodecyl Sulfate

Share to Superoxide Dismutase

Share to Ultraviolet Rays

Source

Identifiers

PMID: 15522870
DOI: 10.1074/jbc.M406106200

Genes

SDS

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 · 9 closest

Different immunoreactivity against monoclonal antibodies between wild-type and mutant copper/zinc superoxide dismutase linked to amyotrophic lateral sclerosis.PMID 15522870Read ↗

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

MS785-MS27 Reactive Misfolded/Non-Native Zn-Deficient SOD1 Species Exhibit Cytotoxicity and Adopt Heterozygous Conformations in Motor Neurons.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 ↗

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

The perplexing role of copper-zinc superoxide dismutase in amyotrophic lateral sclerosis (Lou Gehrig's disease).Semantic proximity Read ↗

Identification of high-performing antibodies for Superoxide dismutase [Cu-Zn] 1 (SOD1) for use in Western blot, immunoprecipitation, and immunofluorescenceSemantic proximity Read ↗

Conformational specificity of the C4F6 SOD1 antibody; low frequency of reactivity in sporadic ALS cases.Semantic proximity Read ↗

Highly specific monoclonal antibodies for allosteric inhibition and immunodetection of the human pancreatic zinc transporter ZnT8.Semantic proximity Read ↗

Glycation proceeds faster in mutated Cu, Zn-superoxide dismutases related to familial amyotrophic lateral sclerosis.Semantic proximity Read ↗

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