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

An examination of alpha B-crystallin as a modifier of SOD1 aggregate pathology and toxicity in models of familial amyotrophic lateral sclerosis.

Journal of neurochemistry - 1 Jun 2010

Karch Celeste M, Borchelt David R

Abstract excerpt

Amyotrophic lateral sclerosis is a progressively paralytic neurodegenerative disease that can be caused by mutations in Cu,Zn-superoxide dismutase 1 (SOD1). Transgenic mice that over-express mutant SOD1 develop paralysis and accumulate aggregates of mutant protein in the brainstem and spinal cord...

Read the complete abstract on PubMed

Topics

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

Share to alpha-Crystallin B Chain
Share to Amyotrophic Lateral Sclerosis
Share to Centrifugation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Detergents

Share to Kaplan-Meier Estimate

Share to Superoxide Dismutase

Share to Superoxide Dismutase-1

Share to Survival Analysis

Source

Open in PubMed Open full text

Identifiers

PMID: 20067574
DOI: 10.1111/j.1471-4159.2010.06572.x
PMCID: PMC3971727

Genes

SOD1

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-20067574-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

An examination of alpha B-crystallin as a modifier of SOD1 aggregate pathology and toxicity in models of familial amyotrophic lateral sclerosis.PMID 20067574Read ↗

Somatodendritic accumulation of misfolded SOD1-L126Z in motor neurons mediates degeneration: αB-crystallin modulates aggregationSemantic proximity Read ↗

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

Amyotrophic lateral sclerosis: Protein chaperone dysfunction revealed by proteomic studies of animal models.Semantic proximity Read ↗

Inducible superoxide dismutase 1 aggregation in transgenic amyotrophic lateral sclerosis mouse fibroblasts.Semantic proximity Read ↗

Aggregation and motor neuron toxicity of an ALS-linked SOD1 mutant independent from wild-type SOD1.Semantic proximity Read ↗

Protein aggregation and protein instability govern familial amyotrophic lateral sclerosis patient survival.Semantic proximity Read ↗

Transgenic mouse models of amyotrophic lateral sclerosis.Semantic proximity Read ↗

Inhibition of chaperone activity is a shared property of several Cu,Zn-superoxide dismutase mutants that cause amyotrophic lateral sclerosis.Semantic proximity Read ↗

Misfolded CuZnSOD and amyotrophic lateral sclerosis.Semantic proximity Read ↗

Differences in protein quality control correlate with phenotype variability in 2 mouse models of familial amyotrophic lateral sclerosis.Semantic proximity Read ↗

Wild-type human SOD1 overexpression does not accelerate motor neuron disease in mice expressing murine Sod1 G86R.Semantic proximity Read ↗

Aggregation of mutant Cu/Zn superoxide dismutase proteins in a culture model of ALS.Semantic proximity Read ↗

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