Triad of TDP43 control in neurodegeneration: autoregulation, localization and aggregation
Cytoplasmic aggregation of TAR DNA-binding protein 43 (TDP43; also known as TARDBP
or TDP-43) is a key pathological feature of several neurodegenerative diseases, including …
or TDP-43) is a key pathological feature of several neurodegenerative diseases, including …
RNA-binding proteins with prion-like domains in health and disease
AF Harrison, J Shorter - Biochemical Journal, 2017 - portlandpress.com
Approximately 70 human RNA-binding proteins (RBPs) contain a prion-like domain (PrLD).
PrLDs are low-complexity domains that possess a similar amino acid composition to prion …
PrLDs are low-complexity domains that possess a similar amino acid composition to prion …
Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS
HJ Kim, NC Kim, YD Wang, EA Scarborough, J Moore… - Nature, 2013 - nature.com
Algorithms designed to identify canonical yeast prions predict that around 250 human
proteins, including several RNA-binding proteins associated with neurodegenerative …
proteins, including several RNA-binding proteins associated with neurodegenerative …
Protein aggregation in amyotrophic lateral sclerosis
Amyotrophic lateral sclerosis (ALS) is a neurodegenerative disease characterized by the
aggregation of ubiquitinated proteins in affected motor neurons. Recent studies have …
aggregation of ubiquitinated proteins in affected motor neurons. Recent studies have …
Exosome secretion is a key pathway for clearance of pathological TDP-43
Cytoplasmic TDP-43 aggregation is a pathological hallmark of amyotrophic lateral sclerosis
and frontotemporal lobar degeneration. Here we investigated the role of exosomes in the …
and frontotemporal lobar degeneration. Here we investigated the role of exosomes in the …
Characterizing the RNA targets and position-dependent splicing regulation by TDP-43
TDP-43 is a predominantly nuclear RNA-binding protein that forms inclusion bodies in
frontotemporal lobar degeneration (FTLD) and amyotrophic lateral sclerosis (ALS). The …
frontotemporal lobar degeneration (FTLD) and amyotrophic lateral sclerosis (ALS). The …
Ataxin-2 intermediate-length polyglutamine expansions are associated with increased risk for ALS
The causes of amyotrophic lateral sclerosis (ALS), a devastating human neurodegenerative
disease, are poorly understood, although the protein TDP-43 has been suggested to have a …
disease, are poorly understood, although the protein TDP-43 has been suggested to have a …
[HTML][HTML] Loss of TAX1BP1-directed autophagy results in protein aggregate accumulation in the brain
SA Sarraf, HV Shah, G Kanfer, AM Pickrell… - Molecular Cell, 2020 - cell.com
Protein aggregates disrupt cellular homeostasis, causing toxicity linked to
neurodegeneration. Selective autophagic elimination of aggregates is critical to protein …
neurodegeneration. Selective autophagic elimination of aggregates is critical to protein …
The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease
Prions are self-templating protein conformers that are naturally transmitted between
individuals and promote phenotypic change. In yeast, prion-encoded phenotypes can be …
individuals and promote phenotypic change. In yeast, prion-encoded phenotypes can be …
TDP-43 and FUS in amyotrophic lateral sclerosis and frontotemporal dementia
Abnormal intracellular protein aggregates comprise a key characteristic in most
neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS) and …
neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS) and …