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

Interaction of amyotrophic lateral sclerosis (ALS)-related mutant copper-zinc superoxide dismutase with the dynein-dynactin complex contributes to inclusion formation.

The Journal of biological chemistry - 15 Aug 2008

Ström Anna-Lena, Shi Ping, Zhang Fujian, Gal Jozsef, Kilty Renee, Hayward Lawrence J, Zhu Haining

Abstract excerpt

An important consequence of protein misfolding related to neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS), is the formation of proteinaceous inclusions or aggregates within the central nervous system. We have previously shown that several familial ALS-linked copper-zinc superoxide dismutase (SOD1) mutants (A4V, G85R, and G93A) interact and co-localize with the dynein-dynactin complex in...

Read the complete abstract on PubMed

Topics

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

Share to Dynactin Complex
Share to Dyneins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Genes, Reporter

Share to Microtubule-Associated Proteins

Share to Motor Neuron Disease

Share to Plasmids

Share to Protein Subunits

Share to Superoxide Dismutase

Source

Open in PubMed Open full text

Identifiers

PMID: 18515363
DOI: 10.1074/jbc.M800276200
PMCID: PMC2504878

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

Interaction of amyotrophic lateral sclerosis (ALS)-related mutant copper-zinc superoxide dismutase with the dynein-dynactin complex contributes to inclusion formation.PMID 18515363Read ↗

Interaction between familial amyotrophic lateral sclerosis (ALS)-linked SOD1 mutants and the dynein complex.Semantic proximity Read ↗

Amyotrophic lateral sclerosis associated with mutations in the CuZn superoxide dismutase gene.Semantic proximity Read ↗

Aberrant dynein function promotes TDP-43 aggregation and upregulation of p62 in male mice harboring transgenic human TDP-43Semantic proximity Read ↗

Many roads lead to Rome? Multiple modes of Cu,Zn superoxide dismutase destabilization, misfolding and aggregation in amyotrophic lateral sclerosis.Semantic proximity Read ↗

Familial amyotrophic lateral sclerosis-linked mutant SOD1 aberrantly interacts with tubulin.Semantic proximity Read ↗

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

α-Synuclein coaggregation in familial amyotrophic lateral sclerosis with SOD1 gene mutation.Semantic proximity Read ↗

Aggregation of copper-zinc superoxide dismutase in familial and sporadic ALS.Semantic proximity Read ↗

TDP-43 physically interacts with amyotrophic lateral sclerosis-linked mutant CuZn superoxide dismutase.Semantic proximity Read ↗

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

UNRAVELING THE MECHANISMS INVOLVED IN MOTOR NEURON DEGENERATION IN ALSSemantic proximity Read ↗

SOD1-interacting proteins: Roles of aggregation cores and protein degradation systems.Semantic proximity Read ↗

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