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

SOD1A4V aggregation alters ubiquitin homeostasis in a cell model of ALS.

Journal of cell science - 12 Jun 2018

Farrawell Natalie E, Lambert-Smith Isabella, Mitchell Kristen, McKenna Jessie, McAlary Luke, Ciryam Prajwal, Vine Kara L, Saunders Darren N, Yerbury Justin J

Abstract excerpt

A hallmark of amyotrophic lateral sclerosis (ALS) pathology is the accumulation of ubiquitylated protein inclusions within motor neurons. Recent studies suggest the sequestration of ubiquitin (Ub) into inclusions reduces the availability of free Ub, which is essential for cellular function and survival. However, the dynamics of the Ub landscape in ALS have not yet been described. Here, we show that Ub homeostasis...

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 Line, Tumor

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Homeostasis

Share to Proteasome Endopeptidase Complex

Share to Protein Folding

Share to Superoxide Dismutase-1

Share to Ubiquitin

Source

Open in PubMed Open full text

Identifiers

PMID: 29748379
DOI: 10.1242/jcs.209122
PMCID: PMC6919637

Genes

SOD1

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

SOD1A4V aggregation alters ubiquitin homeostasis in a cell model of ALS.PMID 29748379Read ↗

Analysis of proteome-wide degradation dynamics in ALS SOD1 iPSC-derived patient neurons reveals disrupted VCP homeostasis.Semantic proximity Read ↗

UBA1: At the Crossroads of Ubiquitin Homeostasis and NeurodegenerationSemantic proximity Read ↗

Ubiquitin homeostasis disruption, a common cause of proteostasis collapse in amyotrophic lateral sclerosis?Semantic proximity Read ↗

Aggregation of ubiquitin and a mutant ALS-linked SOD1 protein correlate with disease progression and fragmentation of the Golgi apparatusSemantic proximity Read ↗

Molecular mechanisms underlying p62-dependent secretion of the Alzheimer-associated ubiquitin variant, UBB <sup>+1</sup>Semantic proximity Read ↗

Protein misfolding in the late-onset neurodegenerative diseases: common themes and the unique case of amyotrophic lateral sclerosis.Semantic proximity Read ↗

Functional implication of ubiquitinating and deubiquitinating mechanisms in TDP-43 proteinopathiesSemantic proximity Read ↗

Structure-function relationship of alpha-synuclein fibrillar polymorphs derived from distinct synucleinopathiesSemantic proximity Read ↗

High-content analysis of proteostasis capacity in cellular models of amyotrophic lateral sclerosis (ALS)Semantic proximity Read ↗

Disease-Associated Mutant Ubiquitin Causes Proteasomal Impairment and Enhances the Toxicity of Protein AggregatesSemantic proximity Read ↗

UBQLN2 in neurodegenerative disease: mechanistic insights and emerging therapeutic potential.Semantic proximity Read ↗

Ubiquitin, cellular inclusions and their role in neurodegeneration.Semantic proximity Read ↗

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