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

Defective Proteasome Delivery of Polyubiquitinated Proteins by Ubiquilin-2 Proteins Containing ALS Mutations.

PloS one - 1 Jan 2015

Chang Lydia, Monteiro Mervyn J

Abstract excerpt

Ubiquilin proteins facilitate delivery of ubiquitinated proteins to the proteasome for degradation. Interest in the proteins has been heightened by the discovery that gene mutations in UBQLN2 cause dominant inheritance of amyotrophic lateral sclerosis (ALS). However, the mechanisms by which the mutations cause ALS are not known. Here we report on the underlying defect of ubiquilin-2 proteins containing ALS-linked...

Read the complete abstract on PubMed

Topics

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

Share to Autophagy-Related Proteins
Share to Immunoprecipitation
Share to Inclusion Bodies

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Proteasome Endopeptidase Complex

Share to Proteolysis

Share to Proto-Oncogene Proteins c-myc

Share to Ubiquitination

Share to Ubiquitins

Source

Open in PubMed Open full text

Identifiers

PMID: 26075709
DOI: 10.1371/journal.pone.0130162
PMCID: PMC4468220

Genes

UBQLN2

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

Defective Proteasome Delivery of Polyubiquitinated Proteins by Ubiquilin-2 Proteins Containing ALS Mutations.PMID 26075709Read ↗

Disturbance of proteasomal and autophagic protein degradation pathways by amyotrophic lateral sclerosis-linked mutations in ubiquilin 2.Semantic proximity Read ↗

Global proteomics of Ubqln2-based murine models of ALSSemantic proximity Read ↗

Wild-type and pathogenic forms of ubiquilin 2 differentially modulate components of the autophagy-lysosome pathways.Semantic proximity Read ↗

Studies of the role of ubiquitination in the interaction of ubiquilin with the loop and carboxyl terminal regions of presenilin-2.Semantic proximity Read ↗

Structure, dynamics and functions of UBQLNs: at the crossroads of protein quality control machinery.Semantic proximity Read ↗

Ubiquilin 2: A component of the ubiquitin–proteasome system with an emerging role in neurodegenerationSemantic proximity Read ↗

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

Global proteomics of <i>Ubqln</i> 2-based murine models of ALSSemantic proximity Read ↗

ALS-linked mutations in ubiquilin-2 or hnRNPA1 reduce interaction between ubiquilin-2 and hnRNPA1.Semantic proximity Read ↗

UBQLN proteins in health and disease with a focus on UBQLN2 in ALS/FTD.Semantic proximity Read ↗

E3 ligase recruitment by UBQLN2 protects substrates from proteasomal degradationSemantic proximity Read ↗

Pathogenic mutation of UBQLN2 impairs its interaction with UBXD8 and disrupts endoplasmic reticulum-associated protein degradation.Semantic proximity Read ↗

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