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

ALS-linked mutations impair UBQLN2 stress-induced biomolecular condensate assembly in cells.

Journal of neurochemistry - 1 Oct 2021

Riley Julia F, Fioramonti Peter J, Rusnock Amber K, Hehnly Heidi, Castañeda Carlos A

Abstract excerpt

Mutations in ubiquilin-2 (UBQLN2), a ubiquitin-binding shuttle protein involved in several protein quality control processes, can lead to amyotrophic lateral sclerosis (ALS). We previously found that wild-type UBQLN2 forms dynamic, membraneless biomolecular condensates upon cellular stress, and undergoes liquid-liquid phase separation in vitro. However, the impact of ALS-linked mutations on UBQLN2 condensate...

Read the complete abstract on PubMed

Topics

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

Share to Adaptor Proteins, Signal Transducing
Share to Amyotrophic Lateral Sclerosis

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Autophagy-Related Proteins

Share to Cell Line

Share to Mutation

Share to Optical Imaging

Share to Oxidative Stress

Source

Open in PubMed Open full text

Identifiers

PMID: 34129687
DOI: 10.1111/jnc.15453
PMCID: PMC8667623

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

ALS-linked mutations impair UBQLN2 stress-induced biomolecular condensate assembly in cells.PMID 34129687Read ↗

ALS-linked mutations impair UBQLN2 stress-induced biomolecular condensate assembly in cellsSemantic proximity Read ↗

Short N-terminal disordered regions and the proline-rich domain are major regulators of phase transitions for full-length UBQLN1, UBQLN2 and UBQLN4Semantic proximity Read ↗

A Spectrophotometric Turbidity Assay to Study Liquid-Liquid Phase Separation of UBQLN2 In Vitro.Semantic proximity Read ↗

Mapping high resolution, multidimensional phase diagrams of physiological protein condensatesSemantic proximity Read ↗

Pathogenic mutations in UBQLN2 exhibit diverse aggregation propensity and neurotoxicity.Semantic proximity Read ↗

Small molecule modulation of a redox-sensitive stress granule protein dissolves stress granules with beneficial outcomes for familial amyotrophic lateral sclerosis modelsSemantic proximity Read ↗

Compositional control of FUS condensate ageing through aggregation-prone interaction networksSemantic proximity Read ↗

MLF2 modulates phase separated nuclear envelope condensates that provoke dual proteotoxicitySemantic proximity Read ↗

The implications of physiological biomolecular condensates in amyotrophic lateral sclerosis.Semantic proximity Read ↗

A Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation.Semantic proximity Read ↗

HspB8 prevents aberrant phase transitions of FUS by chaperoning its folded RNA-binding domain.Semantic proximity Read ↗

Stress Granule Homeostasis, Aberrant Phase Transition, and Amyotrophic Lateral Sclerosis.Semantic proximity Read ↗

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