[HTML][HTML] Phase separation and neurodegenerative diseases: a disturbance in the force
A Zbinden, M Pérez-Berlanga, P De Rossi… - Developmental cell, 2020 - cell.com
Protein aggregation is the main hallmark of neurodegenerative diseases. Many proteins
found in pathological inclusions are known to undergo liquid-liquid phase separation, a …
found in pathological inclusions are known to undergo liquid-liquid phase separation, a …
Molecular mechanisms of TDP-43 misfolding and pathology in amyotrophic lateral sclerosis
A Prasad, V Bharathi, V Sivalingam… - Frontiers in molecular …, 2019 - frontiersin.org
TAR DNA binding protein 43 (TDP-43) is a versatile RNA/DNA binding protein involved in
RNA-related metabolism. Hyper-phosphorylated and ubiquitinated TDP-43 deposits act as …
RNA-related metabolism. Hyper-phosphorylated and ubiquitinated TDP-43 deposits act as …
Molecular interactions underlying liquid− liquid phase separation of the FUS low-complexity domain
The low-complexity domain of the RNA-binding protein FUS (FUS LC) mediates liquid−
liquid phase separation (LLPS), but the interactions between the repetitive SYGQ-rich …
liquid phase separation (LLPS), but the interactions between the repetitive SYGQ-rich …
The molecular language of membraneless organelles
Eukaryotic cells organize their intracellular components into organelles that can be
membrane-bound or membraneless. A large number of membraneless organelles, including …
membrane-bound or membraneless. A large number of membraneless organelles, including …
FUS and TDP-43 phases in health and disease
The distinct prion-like domains (PrLDs) of FUS and TDP-43, modulate phase transitions that
result in condensates with a range of material states. These assemblies are implicated in …
result in condensates with a range of material states. These assemblies are implicated in …
[HTML][HTML] Phase separation of FUS is suppressed by its nuclear import receptor and arginine methylation
M Hofweber, S Hutten, B Bourgeois, E Spreitzer… - Cell, 2018 - cell.com
Cytoplasmic FUS aggregates are a pathological hallmark in a subset of patients with
frontotemporal dementia (FTD) or amyotrophic lateral sclerosis (ALS). A key step that is …
frontotemporal dementia (FTD) or amyotrophic lateral sclerosis (ALS). A key step that is …
Phosphorylation of the FUS low‐complexity domain disrupts phase separation, aggregation, and toxicity
Neuronal inclusions of aggregated RNA‐binding protein fused in sarcoma (FUS) are
hallmarks of ALS and frontotemporal dementia subtypes. Intriguingly, FUS's nearly …
hallmarks of ALS and frontotemporal dementia subtypes. Intriguingly, FUS's nearly …
Cytoplasmic TDP-43 de-mixing independent of stress granules drives inhibition of nuclear import, loss of nuclear TDP-43, and cell death
While cytoplasmic aggregation of TDP-43 is a pathological hallmark of amyotrophic lateral
sclerosis and frontotemporal dementia, how aggregates form and what drives its nuclear …
sclerosis and frontotemporal dementia, how aggregates form and what drives its nuclear …
Nuclear-import receptors reverse aberrant phase transitions of RNA-binding proteins with prion-like domains
RNA-binding proteins (RBPs) with prion-like domains (PrLDs) phase transition to functional
liquids, which can mature into aberrant hydrogels composed of pathological fibrils that …
liquids, which can mature into aberrant hydrogels composed of pathological fibrils that …
Poly (ADP-ribose) prevents pathological phase separation of TDP-43 by promoting liquid demixing and stress granule localization
In amyotrophic lateral sclerosis (ALS) and frontotemporal degeneration (FTD), cytoplasmic
aggregates of hyperphosphorylated TDP-43 accumulate and colocalize with some stress …
aggregates of hyperphosphorylated TDP-43 accumulate and colocalize with some stress …