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

The unfolded protein response in familial amyotrophic lateral sclerosis

15 Dec 2010

Abstract excerpt

Mutant superoxide dismutase type 1 (MTSOD1) is thought to cause ∼20% of cases of familial amyotrophic lateral sclerosis (FALS) because it misfolds and aggregates. Previous studies have shown that MTSOD1 accumulates inside the endoplasmic reticulum (ER) and activates the unfolded protein response (UPR), suggesting that ER stress is involved in the pathogenesis of FALS. We used a genetic approach to investigate the...

Read the complete abstract on PubMed

Topics

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

Share to Amyotrophic Lateral Sclerosis Research
Share to Endoplasmic Reticulum Stress and Disease
Share to Parkinson's Disease Mechanisms and Treatments

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 21159797
DOI: 10.1093/hmg/ddq546

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

The unfolded protein response in familial amyotrophic lateral sclerosisPMID 21159797Read ↗

ER Stress and UPR in Familial Amyotrophic Lateral SclerosisSemantic proximity Read ↗

An enhanced integrated stress response ameliorates mutant SOD1-induced ALSSemantic proximity Read ↗

Stress signaling from the endoplasmic reticulum: A central player in the pathogenesis of amyotrophic lateral sclerosisSemantic proximity Read ↗

Tauopathy-associated PERK alleles are functional hypomorphs that increase neuronal vulnerability to ER stress.Semantic proximity Read ↗

PERK-opathies: An Endoplasmic Reticulum Stress Mechanism Underlying NeurodegenerationSemantic proximity Read ↗

Fine tuning of the unfolded protein response by ISRIB improves neuronal survival in a model of amyotrophic lateral sclerosis.Semantic proximity Read ↗

The PERK pathway: beneficial or detrimental for neurodegenerative diseases and tumor growth and cancerSemantic proximity Read ↗

PERK modulation, with GSK2606414, Sephin1 or salubrinal, failed to produce therapeutic benefits in the SOD1G93A mouse model of ALSSemantic proximity Read ↗

Fine‐tuning PERK signaling for neuroprotectionSemantic proximity Read ↗

The Role of PERK in Understanding Development of Neurodegenerative Diseases.Semantic proximity Read ↗

Wild-type SOD1 overexpression accelerates disease onset of a G85R SOD1 mouseSemantic proximity Read ↗

Familial amyotrophic lateral sclerosis (FALS)-linked SOD1 mutation accelerates neuronal cell death by activating cleavage of caspase-4 under ER stress in an in vitro model of FALS.Semantic proximity Read ↗

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