Associated Papers
Multiplex neurodegeneration proteotoxicity platform reveals DNAJB6 promotes non-toxic FUS condensate gelation and inhibits neurotoxicity.
Resnick SJ et al.
Nature Communications, 2025
Pathology of three ALS patients with FUS variants, including one likely benign Q23L variant lacking FUS inclusions.
Stenvall E et al.
Human Molecular Genetics, 2025
ATP as a Key Modulator of Fused-in-sarcoma Phase Separation and Aggregation: Insights into Amyotrophic Lateral Sclerosis Pathogenesis.
Kitamura K et al.
Journal of Molecular Biology, 2025
Single-cell RNA-sequencing reveals early mitochondrial dysfunction unique to motor neurons shared across FUS- and TARDBP-ALS.
Schweingruber C et al.
Nature Communications, 2025
Exploring Protein Misfolding in Amyotrophic Lateral Sclerosis: Structural and Functional Insights.
Ivantsik O et al.
Biomedicines, 2025
Single-point mutations in disordered proteins: Linking sequence, ensemble, and function.
Flores E et al.
Current Opinion in Structural Biology, 2025
Multi-scale in silico analysis of the phase separation behavior of FUS mutants.
Fernando KS et al.
Journal of Materials Chemistry. B, 2024
Decoding Missense Variants by Incorporating Phase Separation via Machine Learning.
Feng M et al.
Nature Communications, 2024
Frontotemporal dementia-like disease progression elicited by seeded aggregation and spread of FUS.
Vazquez-Sanchez S et al.
Molecular Neurodegeneration, 2024
Frontotemporal dementia-like disease progression elicited by seeded aggregation and spread of FUS.
Vazquez-Sanchez S et al.
Biorxiv : the Preprint Server for Biology, 2024
An aberrant fused in sarcoma liquid droplet of amyotrophic lateral sclerosis pathological variant, R495X, accelerates liquid-solid phase transition.
Shiramasa Y et al.
Scientific Reports, 2024
The implications of physiological biomolecular condensates in amyotrophic lateral sclerosis.
Fakim H et al.
Seminars in Cell & Developmental Biology, 2024
FUS gene mutation in amyotrophic lateral sclerosis: a new case report and systematic review.
Xiao X et al.
Amyotrophic Lateral Sclerosis & Frontotemporal Degeneration, 2024
Regulation of RNG105/caprin1 dynamics by pathogenic cytoplasmic FUS and TDP-43 in neuronal RNA granules modulates synaptic loss.
Horio T et al.
Heliyon, 2023
Nucleation and dissolution mechanism underlying amyotrophic lateral sclerosis/frontotemporal lobar dementia-linked fused in sarcoma condensates.
Djaja NA et al.
Iscience, 2023
Mutated FUS in familial amyotrophic lateral sclerosis involves multiple hnRNPs in the formation of neuronal cytoplasmic inclusions.
Honda H et al.
Journal of Neuropathology and Experimental Neurology, 2023
Characterising the Genetic Landscape of Amyotrophic Lateral Sclerosis: A Catalogue and Assessment of Over 1,000 Published Genetic Variants.
McCann EP et al.
Journal of Neuromuscular Diseases, 2023
Phase separation and pathologic transitions of RNP condensates in neurons: implications for amyotrophic lateral sclerosis, frontotemporal dementia and other neurodegenerative disorders.
Naskar A et al.
Frontiers in Molecular Neuroscience, 2023
Mechanism underlying liquid-to-solid phase transition in fused in sarcoma liquid droplets.
Li S et al.
Physical Chemistry Chemical Physics : Pccp, 2022
Hsp70 exhibits a liquid-liquid phase separation ability and chaperones condensed FUS against amyloid aggregation.
Li Y et al.
Iscience, 2022
Phase-Separated Subcellular Compartmentation and Related Human Diseases.
Zhang L et al.
International Journal of Molecular Sciences, 2022
Poly(ADP-ribose) drives condensation of FUS via a transient interaction.
Rhine K et al.
Molecular Cell, 2022
The low-complexity domain of the FUS RNA binding protein self-assembles via the mutually exclusive use of two distinct cross-β cores.
Kato M et al.
Proceedings of the National Academy of Sciences of the United States of America, 2021
HspB8 prevents aberrant phase transitions of FUS by chaperoning its folded RNA-binding domain.
Boczek EE et al.
Elife, 2021
RNA modulates physiological and neuropathological protein phase transitions.
Mann JR et al.
Neuron, 2021
Phenotypic diversity in ALS and the role of poly-conformational protein misfolding.
Ayers JI et al.
Acta Neuropathologica, 2021
Proteostatic imbalance and protein spreading in amyotrophic lateral sclerosis.
Cicardi ME et al.
The Embo Journal, 2021
The FUS gene is dual-coding with both proteins contributing to FUS-mediated toxicity.
Brunet MA et al.
Embo Reports, 2021
Probing the influence of mutations on FUS condensates, one molecule at a time.
Chattopadhyay K
Communications Biology, 2021
Aberrant Phase Separation of FUS Leads to Lysosome Sequestering and Acidification.
Trnka F et al.
Frontiers in Cell and Developmental Biology, 2021
Rare CYLD Variants in Chinese Patients With Amyotrophic Lateral Sclerosis.
Gu X et al.
Frontiers in Genetics, 2021
Stress granule subtypes: an emerging link to neurodegeneration.
Advani VM et al.
Cellular and Molecular Life Sciences : Cmls, 2020
ALS/FTLD-Linked Mutations in FUS Glycine Residues Cause Accelerated Gelation and Reduced Interactions with Wild-Type FUS.
Rhine K et al.
Molecular Cell, 2020
A Systematic and Comprehensive Review on Disease-Causing Genes in Amyotrophic Lateral Sclerosis.
Srinivasan E et al.
Journal of Molecular Neuroscience : Mn, 2020
A de novo c.1509dupA:p.R503fs mutation of FUS: report of a girl with sporadic juvenile amyotrophic lateral sclerosis.
Chen L et al.
Amyotrophic Lateral Sclerosis & Frontotemporal Degeneration, 2020
The Occurrence of FUS Mutations in Pediatric Amyotrophic Lateral Sclerosis: A Case Report and Review of the Literature.
Picher-Martel V et al.
Journal of Child Neurology, 2020
[Molecular mechanism of amyotrophic lateral sclerosis (ALS) from the viewpoint of the formation and degeneration of transactive response DNA-binding protein 43 kDa (TDP-43) inclusions].
Kasahara S et al.
Rinsho Shinkeigaku = Clinical Neurology, 2020
Loss of Dynamic RNA Interaction and Aberrant Phase Separation Induced by Two Distinct Types of ALS/FTD-Linked FUS Mutations.
Niaki AG et al.
Molecular Cell, 2020
Fused in Sarcoma: Properties, Self-Assembly and Correlation with Neurodegenerative Diseases.
Chen C et al.
Molecules (basel, Switzerland), 2019
Disruption of protein function by pathogenic mutations: common and uncommon mechanisms 1.
Taipale M
Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire, 2019
Prion-Like Propagation of Protein Misfolding and Aggregation in Amyotrophic Lateral Sclerosis.
McAlary L et al.
Frontiers in Molecular Neuroscience, 2019
The neurodegenerative diseases ALS and SMA are linked at the molecular level via the ASC-1 complex.
Chi B et al.
Nucleic Acids Research, 2018
Liquidizing FUS via prion-like domain phosphorylation.
Shorter J
The Embo Journal, 2017
An aberrant phase transition of stress granules triggered by misfolded protein and prevented by chaperone function.
Mateju D et al.
The Embo Journal, 2017
Aggregation of FET Proteins as a Pathological Change in Amyotrophic Lateral Sclerosis.
Furukawa Y et al.
Advances in Experimental Medicine and Biology, 2017
A Surveillance Function of the HSPB8-BAG3-HSP70 Chaperone Complex Ensures Stress Granule Integrity and Dynamism.
Ganassi M et al.
Molecular Cell, 2016
ALS/FTD Mutation-Induced Phase Transition of FUS Liquid Droplets and Reversible Hydrogels into Irreversible Hydrogels Impairs RNP Granule Function.
Murakami T et al.
Neuron, 2015