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The EMBO Journal, ISSN 0261-4189, 10/2017, Volume 36, Issue 20, pp. 2951 - 2967
Neuronal inclusions of aggregated RNA ‐binding protein fused in sarcoma ( FUS ) are hallmarks of ALS and frontotemporal dementia subtypes. Intriguingly, FUS 's... 
frontotemporal dementia | prion | intrinsically disordered protein | ribonucleoprotein granule | amyotrophic lateral sclerosis | NEURODEGENERATIVE DISEASE | PRION-LIKE DOMAINS | BIOCHEMISTRY & MOLECULAR BIOLOGY | DISORDERED PROTEINS | AMYOTROPHIC-LATERAL-SCLEROSIS | WILD-TYPE FUS | CELL BIOLOGY | RNA-BINDING PROTEINS | CELL-FREE FORMATION | MOTOR-NEURON DEGENERATION | C-TERMINAL DOMAIN | STRESS GRANULES | RNA-Binding Protein FUS - chemistry | Cell Line | Amyotrophic Lateral Sclerosis - pathology | Phosphorylation | Magnetic Resonance Spectroscopy | Humans | Protein Conformation | Protein Processing, Post-Translational | RNA-Binding Protein FUS - metabolism | Protein Aggregation, Pathological | Frontotemporal Dementia - pathology | Cell culture | Salts | Yeast | Nuclear magnetic resonance--NMR | Self-association | Toxicity | DNA damage | Cytotoxicity | Agglomeration | Kinases | Complexity | Magnetic resonance spectroscopy | Proteins | FUS protein | Neurotoxicity | Post-translation | Dementia disorders | Deoxyribonucleic acid--DNA | Spectroscopy | Sarcoma | Therapeutic applications | Amyotrophic lateral sclerosis | Pharmacology | Ribonucleic acid--RNA | RNA-binding protein | DNA-dependent protein kinase | Phase separation | Frontotemporal dementia | Protein interaction | Index Medicus | 60 APPLIED LIFE SCIENCES | Neuroscience | Protein Biosynthesis & Quality Control
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