Fused in sarcoma (FUS) in DNA repair: tango with poly (ADP-ribose) polymerase 1 and compartmentalisation of damaged DNA
MV Sukhanova, AS Singatulina, D Pastré… - International Journal of …, 2020 - mdpi.com
The fused in sarcoma (FUS) protein combines prion-like properties with a multifunctional
DNA/RNA-binding domain and has functions spanning the regulation of RNA metabolism …
DNA/RNA-binding domain and has functions spanning the regulation of RNA metabolism …
Amyotrophic lateral sclerosis: proteins, proteostasis, prions, and promises
Amyotrophic lateral sclerosis (ALS) is characterized by the progressive degeneration of the
motor neurons that innervate muscle, resulting in gradual paralysis and culminating in the …
motor neurons that innervate muscle, resulting in gradual paralysis and culminating in the …
FUS recognizes G quadruplex structures within neuronal mRNAs
JA Imperatore, DS McAninch… - Frontiers in Molecular …, 2020 - frontiersin.org
Fused in sarcoma (FUS), identified as the heterogeneous nuclear ribonuclear protein P2, is
expressed in neuronal and non-neuronal tissue, and among other functions, has been …
expressed in neuronal and non-neuronal tissue, and among other functions, has been …
FUS contributes to mTOR-dependent inhibition of translation
M Sévigny, IB Julien, JP Venkatasubramani… - Journal of Biological …, 2020 - ASBMB
The amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD)–linked RNA-
binding protein called FUS (fused in sarcoma) has been implicated in several aspects of …
binding protein called FUS (fused in sarcoma) has been implicated in several aspects of …
[HTML][HTML] Karyopherins and condensates
Several aggregation-prone RNA-binding proteins, including FUS, EWS, TAF15, hnRNP A1,
hnRNP A2, and TDP-43, are mutated in neurodegenerative diseases. The nuclear …
hnRNP A2, and TDP-43, are mutated in neurodegenerative diseases. The nuclear …
Application of yeast to studying amyloid and prion diseases
Amyloids are fibrous cross-β protein aggregates that are capable of proliferation via
nucleated polymerization. Amyloid conformation likely represents an ancient protein fold …
nucleated polymerization. Amyloid conformation likely represents an ancient protein fold …
Amyotrophic Lateral Sclerosis Modifiers in Drosophila Reveal the Phospholipase D Pathway as a Potential Therapeutic Target
Amyotrophic lateral sclerosis (ALS) is a devastating neurodegenerative disorder lacking
effective treatments. ALS pathology is linked to mutations in several different genes …
effective treatments. ALS pathology is linked to mutations in several different genes …
The prion-like nature of amyotrophic lateral sclerosis
The misfolding, aggregation, and deposition of specific proteins is the key hallmark of most
progressive neurodegenerative disorders such as Alzheimer's disease, Parkinson's disease …
progressive neurodegenerative disorders such as Alzheimer's disease, Parkinson's disease …
Targeted next-generation sequencing study in familial ALS-FTD Portuguese patients negative for C9orf72 HRE
M Gromicho, AM Coutinho, AC Pronto-Laborinho… - Journal of …, 2020 - Springer
Amyotrophic lateral sclerosis (ALS) is a neurodegenerative disease with clinical and
etiological heterogeneity and a complex genetic contribution. Clinical, neuropathological …
etiological heterogeneity and a complex genetic contribution. Clinical, neuropathological …
[图书][B] Retromer deficiency in amyotrophic lateral sclerosis
EJ Pérez-Torres - 2020 - search.proquest.com
The retromer is a protein complex whose function is to mediate the recycling of proteins from
the endosome to either the plasma membrane or the trans-Golgi network. A deficit in …
the endosome to either the plasma membrane or the trans-Golgi network. A deficit in …