Fused in Sarcoma: Properties, Self-Assembly and Correlation with Neurodegenerative Diseases.
Chen, Chen; Ding, Xiufang; Akram, Nimrah; Xue, Song; Luo, Shi-Zhong.
; 24(8)2019 Apr 24.
Artigo em Inglês | MEDLINE | ID: mdl-31022909
A Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation.
The Solution Structure of FUS Bound to RNA Reveals a Bipartite Mode of RNA Recognition with Both Sequence and Shape Specificity.
A comparative clinical, pathological, biochemical and genetic study of fused in sarcoma proteinopathies.
Altered mRNP granule dynamics in FTLD pathogenesis.
A new subtype of frontotemporal lobar degeneration with FUS pathology.
Structure of FUS Protein Fibrils and Its Relevance to Self-Assembly and Phase Separation of Low-Complexity Domains.
Activity-dependent FUS dysregulation disrupts synaptic homeostasis.
Phosphorylation-regulated binding of RNA polymerase II to fibrous polymers of low-complexity domains.
Modelling FUSopathies: focus on protein aggregation.
Phosphorylation of the FUS low-complexity domain disrupts phase separation, aggregation, and toxicity.