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

Targeting of monomer/misfolded SOD1 as a therapeutic strategy for amyotrophic lateral sclerosis.

The Journal of neuroscience : the official journal of the Society for Neuroscience - 27 Jun 2012

Liu Hsueh-Ning, Tjostheim Sonja, Dasilva Kevin, Taylor David, Zhao Beibei, Rakhit Rishi, Brown Mary, Chakrabartty Avijit, McLaurin Joanne, Robertson Janice

Abstract excerpt

There is increasing evidence that toxicity of mutant superoxide dismutase-1 (SOD1) in amyotrophic lateral sclerosis (ALS) is linked to its propensity to misfold and to aggregate. Immunotargeting of differently folded states of SOD1 has provided therapeutic benefit in mutant SOD1 transgenic mice. The specific region(s) of the SOD1 protein to which these immunization approaches target are, however, unknown. In...

Read the complete abstract on PubMed

Topics

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

Share to Antibodies
Share to Axons

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Gliosis

Share to Motor Neurons

Share to Psychomotor Performance

Share to Spinal Cord

Share to Superoxide Dismutase-1

Share to Vaccination

Source

Open in PubMed Open full text

Identifiers

PMID: 22745481
DOI: 10.1523/JNEUROSCI.5053-11.2012
PMCID: PMC6622344

Genes

SOD1

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 3 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Targeting of monomer/misfolded SOD1 as a therapeutic strategy for amyotrophic lateral sclerosis.PMID 22745481Read ↗

Blocking an epitope of misfolded SOD1 ameliorates disease phenotype in a model of amyotrophic lateral sclerosis.Semantic proximity Read ↗

Induction of protective immunity by vaccination with wild-type apo superoxide dismutase 1 in mutant SOD1 transgenic mice.Semantic proximity Read ↗

SOD1-positive aggregate accumulation in the CNS predicts slower disease progression and increased longevity in a mutant SOD1 mouse model of ALSSemantic proximity Read ↗

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

Identification of a misfolded region in superoxide dismutase 1 that is exposed in amyotrophic lateral sclerosis.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 structure-guided antibody detects SOD1 oligomers in diverse ALS genotypesSemantic proximity Read ↗

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

The potential role of misfolded wild-type SOD1 protein in sporadic amyotrophic lateral sclerosis (ALS): a review of the evidence.Semantic proximity Read ↗

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

Destabilized Soluble SOD1 Species as Potential Determinants of Disease Severity in Familial Amyotrophic Lateral Sclerosis.Semantic proximity Read ↗

Nonnative SOD1 trimer is toxic to motor neurons in a model of amyotrophic lateral sclerosis.Semantic proximity Read ↗

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