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

Structural properties and neuronal toxicity of amyotrophic lateral sclerosis-associated Cu/Zn superoxide dismutase 1 aggregates.

The Journal of cell biology - 10 Oct 2005

Matsumoto Gen, Stojanovic Aleksandar, Holmberg Carina I, Kim Soojin, Morimoto Richard I

Abstract excerpt

The appearance of protein aggregates is a characteristic of protein misfolding disorders including familial amyotrophic lateral sclerosis, a neurodegenerative disease caused by inherited mutations in Cu/Zn superoxide dismutase 1 (SOD1). Here, we use live cell imaging of neuronal and nonneuronal cells to show that SOD1 mutants (G85R and G93A) form an aggregate structure consisting of immobile scaffolds, through...

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 Cell Death

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to HSP70 Heat-Shock Proteins

Share to Macromolecular Substances

Share to PC12 Cells

Share to Proteasome Endopeptidase Complex

Share to Protein Folding

Share to Superoxide Dismutase

Source

Open in PubMed Open full text

Identifiers

PMID: 16216923
DOI: 10.1083/jcb.200504050
PMCID: PMC2171239

Genes

SOD1

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural properties and neuronal toxicity of amyotrophic lateral sclerosis-associated Cu/Zn superoxide dismutase 1 aggregates.PMID 16216923Read ↗

Huntingtin and mutant SOD1 form aggregate structures with distinct molecular properties in human cells.Semantic proximity Read ↗

Dysregulation of the proteasome increases the toxicity of ALS-linked mutant SOD1.Semantic proximity Read ↗

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

Spinal cord homogenates from SOD1 familial amyotrophic lateral sclerosis induce SOD1 aggregation in living cells.Semantic proximity Read ↗

Dimerization, oligomerization, and aggregation of human amyotrophic lateral sclerosis copper/zinc superoxide dismutase 1 protein mutant forms in live cells.Semantic proximity Read ↗

Temporal control of acute protein aggregate turnover by UBE3C and NRF1-dependent proteasomal pathwaysSemantic proximity Read ↗

Nonamyloid aggregates arising from mature copper/zinc superoxide dismutases resemble those observed in amyotrophic lateral sclerosis.Semantic proximity Read ↗

Misfolded CuZnSOD and amyotrophic lateral sclerosis.Semantic proximity Read ↗

Cu/Zn superoxide dismutase mutants associated with amyotrophic lateral sclerosis show enhanced formation of aggregates in vitro.Semantic proximity Read ↗

Protein aggregation in amyotrophic lateral sclerosisSemantic proximity Read ↗

Superoxide dismutase 1 mutants related to amyotrophic lateral sclerosis induce endoplasmic stress in neuro2a cells.Semantic proximity Read ↗

Accumulation and clearance of alpha-synuclein aggregates demonstrated by time-lapse imaging.Semantic proximity Read ↗

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