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Cellular and molecular life sciences : CMLS, ISSN 1420-9071, 2016, Volume 74, Issue 7, pp. 1297 - 1318
Five structurally and functionally different proteins, an enzyme superoxide dismutase 1 (SOD1... 
Biomedicine, general | Biochemistry, general | Protein–protein interactions | FUS | Amyotrophic lateral sclerosis | Cell Biology | SOD1 | Life Sciences | Life Sciences, general | Posttranslational modifications | Neurodegeneration | Intrinsically disordered proteins | TDP-43 | Protein function | Binding-induced folding | Protein structure | Polymorphism | BIOCHEMISTRY & MOLECULAR BIOLOGY | FRONTOTEMPORAL LOBAR DEGENERATION | BINDING PROTEIN | MOLECULAR INTERACTION DATABASE | Protein-protein interactions | CU,ZN SUPEROXIDE-DISMUTASE | CELL BIOLOGY | NATIVELY UNFOLDED PROTEINS | C9ORF72 HEXANUCLEOTIDE REPEAT | PATHOLOGICAL TDP-43 | ANTISENSE TRANSCRIPTS | MUTANT SOD1 | STRESS GRANULES | Amyotrophic Lateral Sclerosis - physiopathology | Humans | DNA-Binding Proteins - metabolism | RNA-Binding Protein FUS - chemistry | Profilins - genetics | Databases, Protein | Superoxide Dismutase-1 - metabolism | C9orf72 Protein | Protein Structure, Tertiary | Amino Acid Sequence | Amyotrophic Lateral Sclerosis - genetics | RNA-Binding Protein FUS - genetics | RNA-Binding Protein FUS - metabolism | DNA-Binding Proteins - genetics | DNA-Binding Proteins - chemistry | Superoxide Dismutase-1 - chemistry | Proteins - genetics | Algorithms | Proteins - metabolism | Intrinsically Disordered Proteins - chemistry | Profilins - chemistry | Amyotrophic Lateral Sclerosis - metabolism | Superoxide Dismutase-1 - genetics | Mutation | Proteins - chemistry | Profilins - metabolism | Intrinsically Disordered Proteins - metabolism | Enzymes | Medical colleges | RNA | Analysis | Superoxide | Muscle proteins | Alzheimer's disease | Protein binding | RNA-protein interactions | Pathogenesis | Binding sites
Journal Article
Journal Article
Molecular cell, ISSN 1097-2765, 2017, Volume 67, Issue 3, pp. 387 - 399.e5
... (DNAPKc, Ku70, and Ku80) and paraspeckle proteins (SFPQ, NONO, PSPC1, RBM14, and MATRIN3... 
HEXIM1 | DNA-PK | innate immune response | herpesvirus | paraspeckles | cGAS | NEAT1 | interferon stimulatory DNA | DEFENSE | PROTEIN | INHIBITION | BIOCHEMISTRY & MOLECULAR BIOLOGY | TRANSCRIPTION | SENSOR | POLYMERASE-II | 7SK RNA | BINDING | GMP-AMP SYNTHASE | P-TEFB | CELL BIOLOGY | Human Umbilical Vein Endothelial Cells - metabolism | Humans | Octamer Transcription Factors - immunology | Intracellular Signaling Peptides and Proteins - metabolism | Herpesvirus 8, Human - immunology | RNA, Long Noncoding - immunology | PTB-Associated Splicing Factor - genetics | RNA Interference | Calcium-Binding Proteins - immunology | Octamer Transcription Factors - genetics | Nucleotidyltransferases - metabolism | Intracellular Signaling Peptides and Proteins - genetics | Signal Transduction | Membrane Proteins - genetics | RNA-Binding Proteins - immunology | PTB-Associated Splicing Factor - metabolism | Nuclear Matrix-Associated Proteins - metabolism | PTB-Associated Splicing Factor - immunology | DNA - metabolism | Host-Pathogen Interactions | Nuclear Matrix-Associated Proteins - genetics | HeLa Cells | RNA-Binding Proteins - metabolism | Calcium-Binding Proteins - genetics | RNA-Binding Proteins - genetics | Multiprotein Complexes | Human Umbilical Vein Endothelial Cells - immunology | Intracellular Signaling Peptides and Proteins - immunology | Human Umbilical Vein Endothelial Cells - virology | Interferon Regulatory Factor-3 - genetics | Ku Autoantigen - genetics | Transfection | HEK293 Cells | Membrane Proteins - metabolism | Nuclear Proteins - genetics | Octamer Transcription Factors - metabolism | Interferon Regulatory Factor-3 - immunology | Calcium-Binding Proteins - metabolism | DNA - immunology | Nuclear Matrix-Associated Proteins - immunology | Ku Autoantigen - immunology | Membrane Proteins - immunology | Nuclear Proteins - metabolism | Ku Autoantigen - metabolism | RNA, Long Noncoding - genetics | Immunity, Innate | Nuclear Proteins - immunology | DNA - genetics | Interferon Regulatory Factor-3 - metabolism | Nucleotidyltransferases - genetics | Protein Binding | Nucleotidyltransferases - immunology | RNA, Long Noncoding - metabolism | RNA sequencing | Immune response | RNA | DNA | Genetic research | Interferon | Biological response modifiers | Mass spectrometry | Human Umbilical Vein Endothelial Cells | Nuclear Matrix-Associated Proteins | Herpesvirus 8, Human | RNA-Binding Proteins | Life Sciences | Interferon Regulatory Factor-3 | Genetics | Calcium-Binding Proteins | Intracellular Signaling Peptides and Proteins | PTB-Associated Splicing Factor | Nuclear Proteins | Membrane Proteins | Nucleotidyltransferases | Ku Autoantigen | Octamer Transcription Factors | RNA, Long Noncoding
Journal Article
Cellular and molecular life sciences : CMLS, ISSN 1420-9071, 2013, Volume 71, Issue 8, pp. 1477 - 1504
Journal Article
Journal Article
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... 
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 | 60 APPLIED LIFE SCIENCES | Neuroscience | Protein Biosynthesis & Quality Control
Journal Article
Trends in biochemical sciences (Amsterdam. Regular ed.), ISSN 0968-0004, 2012, Volume 37, Issue 6, pp. 237 - 247
Journal Article
Cell (Cambridge), ISSN 0092-8674, 2006, Volume 125, Issue 5, pp. 873 - 886
.... This silencing depends on a functional RNAi pathway, requires the heterochromatin proteins, Swi6/HP1, Clr4/Suv39h, and Sir2, and is accompanied by the generation of ura4... 
H3 LYSINE-9 METHYLATION | DOUBLE-STRANDED-RNA | FISSION YEAST | EPIGENETIC CONTROL | HISTONE H3 | BIOCHEMISTRY & MOLECULAR BIOLOGY | INTERFERENCE | MECHANISMS | CHROMOSOME SEGREGATION | POLYMERASE-II | SCHIZOSACCHAROMYCES-POMBE | CELL BIOLOGY | RNA, Small Interfering - genetics | RNA-Binding Proteins - genetics |