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

Combating deleterious phase transitions in neurodegenerative disease.

Biochimica et biophysica acta. Molecular cell research - 1 Apr 2021

Darling April L, Shorter James

Abstract excerpt

Protein aggregation is a hallmark of neurodegenerative diseases. However, the mechanism that induces pathogenic aggregation is not well understood. Recently, it has emerged that several of the pathological proteins found in an aggregated or mislocalized state in neurodegenerative diseases are also able to undergo liquid-liquid phase separation (LLPS) under physiological conditions. Although these phase...

Read the complete abstract on PubMed

Topics

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

Share to Biophysical Phenomena
Share to Mutation
Share to Neurodegenerative Diseases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Protein Aggregates

Share to Protein Aggregation, Pathological

Source

Open in PubMed Open full text

Identifiers

PMID: 33549703
DOI: 10.1016/j.bbamcr.2021.118984
PMCID: PMC7965345

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

Combating deleterious phase transitions in neurodegenerative disease.PMID 33549703Read ↗

Disrupting pathologic phase transitions in neurodegenerationSemantic proximity Read ↗

The pathophysiology of neurodegenerative disease: Disturbing the balance between phase separation and irreversible aggregation.Semantic proximity Read ↗

Aberrant liquid-liquid phase separation and amyloid aggregation of proteins related to neurodegenerative diseasesSemantic proximity Read ↗

Liquid-liquid phase separation induces pathogenic tau conformations in vitro.Semantic proximity Read ↗

Parkinson's disease-specific α-Synuclein variants potentially drive Lewy body formation by engaging in promiscuous and non-functional interactions.Semantic proximity Read ↗

Tau liquid-liquid phase separation in neurodegenerative diseases.Semantic proximity Read ↗

Liquid-liquid phase separation regulates alpha-synuclein aggregate and mitophagy in Parkinson’s diseaseSemantic proximity Read ↗

Heterotypic droplet formation by pro-inflammatory S100A9 and neurodegenerative disease-related alpha-synucleinSemantic proximity Read ↗

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

Aberrant phase separation and cancer.Semantic proximity Read ↗

Role and therapeutic potential of liquid-liquid phase separation in amyotrophic lateral sclerosis.Semantic proximity Read ↗

Prion Protein Biology Through the Lens of Liquid-Liquid Phase Separation.Semantic proximity Read ↗

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