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Journal Article
Journal Article
The FEBS journal, ISSN 1742-464X, 2013, Volume 280, Issue 18, pp. 4348 - 4370
Stress granules (SGs) are cytoplasmic foci that rapidly form when cells are exposed to stress... 
FUS | FTLD | ALS | neurodegeneration | stress granules | TLS | RNA‐binding proteins | TDP‐43 | TDP-43 | RNA-binding proteins | BIOCHEMISTRY & MOLECULAR BIOLOGY | GLOBAL BRAIN ISCHEMIA | AMYOTROPHIC-LATERAL-SCLEROSIS | MESSENGER-RNA STABILITY | FRONTOTEMPORAL LOBAR DEGENERATION | LENGTH POLYGLUTAMINE EXPANSIONS | CHRONIC TRAUMATIC ENCEPHALOPATHY | MOTOR-NEURON PROTEIN | INTERNAL RIBOSOME ENTRY | SPINAL MUSCULAR-ATROPHY | HIPPOCAMPAL CORNU AMMONIS-1 | Biomarkers - metabolism | Protein Structure, Tertiary | Frontotemporal Lobar Degeneration - pathology | Cytoplasmic Granules - pathology | Signal Transduction | Amyotrophic Lateral Sclerosis - genetics | Heat-Shock Proteins - metabolism | Humans | RNA, Messenger - genetics | Gene Expression Regulation | Stress, Physiological | RNA-Binding Protein FUS - genetics | RNA-Binding Protein FUS - metabolism | DNA-Binding Proteins - genetics | RNA, Messenger - metabolism | Protein Folding | DNA-Binding Proteins - metabolism | Heat-Shock Proteins - genetics | Amyotrophic Lateral Sclerosis - pathology | Frontotemporal Lobar Degeneration - metabolism | Cytoplasmic Granules - metabolism | Amyotrophic Lateral Sclerosis - metabolism | Cytoplasmic Granules - genetics | Frontotemporal Lobar Degeneration - genetics | Sarcoma | Binding proteins | DNA | Protein binding | Proteins | Stress response | Neurodegeneration | Deoxyribonucleic acid--DNA | Index Medicus
Journal Article
Molecular cell, ISSN 1097-2765, 2015, Volume 60, Issue 2, pp. 231 - 241
Phase-separated states of proteins underlie ribonucleoprotein (RNP) granules and nuclear RNA-binding protein assemblies that may nucleate protein inclusions associated with neurodegenerative diseases... 
CELL-FREE FORMATION | PROTEIN | PHOSPHORYLATION | PRION-LIKE DOMAINS | PHASE-TRANSITIONS | TDP-43 | BIOCHEMISTRY & MOLECULAR BIOLOGY | ALS | FUS/TLS | ARGININE METHYLATION | ALPHA-SYNUCLEIN | CELL BIOLOGY | RNA-Binding Proteins - genetics | Humans | Molecular Sequence Data | RNA Polymerase II - metabolism | Cytoplasmic Granules - chemistry | Phase Transition | RNA-Binding Protein FUS - chemistry | Molecular Mimicry | Cytoplasmic Granules - metabolism | Escherichia coli - metabolism | Binding Sites | RNA Polymerase II - chemistry | RNA - metabolism | Protein Structure, Tertiary | Recombinant Proteins - metabolism | Prions - metabolism | Gene Expression | Rheology | RNA-Binding Proteins - chemistry | RNA-Binding Protein FUS - genetics | Recombinant Proteins - chemistry | RNA-Binding Protein FUS - metabolism | Recombinant Proteins - genetics | Prions - chemistry | RNA - chemistry | Intrinsically Disordered Proteins - genetics | Amino Acid Motifs | Escherichia coli - genetics | Intrinsically Disordered Proteins - chemistry | Protein Binding | RNA Polymerase II - genetics | RNA-Binding Proteins - metabolism | Intrinsically Disordered Proteins - metabolism | Proteins | Nervous system diseases | Sarcoma | RNA | Physiological aspects | Fluorescence | Nuclear magnetic resonance spectroscopy | Molecular biology | Fluorescence microscopy | Cells | Protein binding | Analysis
Journal Article