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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
Molecular cell, ISSN 1097-2765, 2017, Volume 65, Issue 6, pp. 1044 - 1055.e5
Liquid-liquid phase separation (LLPS) of RNA-binding proteins plays an important role in the formation of multiple membrane-less organelles involved in RNA metabolism, including stress granules... 
LLPS | hnRNP | intrinsically disordered protein | FUS | protein aggregation | low complexity domain | prion-like domain | phase transition | amyotrophic lateral sclerosis | frontotemporal lobar degeneration | RNA-BINDING PROTEINS | NEURODEGENERATIVE DISEASE | IN-VITRO | PRION-LIKE DOMAINS | BIOCHEMISTRY & MOLECULAR BIOLOGY | ALS | LIQUID DROPLETS | C-TERMINAL DOMAIN | HEXANUCLEOTIDE REPEAT | GGGGCC REPEAT | NUCLEOCYTOPLASMIC TRANSPORT | CELL BIOLOGY | Phosphorylation | Humans | Poly-ADP-Ribose Binding Proteins | RNA Helicases | Transfection | Time Factors | Cytoplasmic Granules - metabolism | Eukaryotic Initiation Factor-2 - metabolism | Protein Domains | C9orf72 Protein | Dipeptides - metabolism | Lipid Droplets - metabolism | RNA Recognition Motif Proteins | RNA - metabolism | Cytoplasmic Granules - pathology | Amyotrophic Lateral Sclerosis - genetics | Dipeptides - chemistry | Arginine - chemistry | Carrier Proteins - genetics | Amyotrophic Lateral Sclerosis - pathology | DNA Helicases | Carrier Proteins - metabolism | Proteins - metabolism | Intrinsically Disordered Proteins - chemistry | Eukaryotic Initiation Factor-2 - genetics | Amyotrophic Lateral Sclerosis - metabolism | HeLa Cells | Proteins - chemistry | Arginine - metabolism | Intrinsically Disordered Proteins - metabolism | Physiological aspects | Amino acids | Neurosciences | RNA | Binding proteins | Protein binding | Arginine | Glutamine
Journal Article
EMBO Molecular Medicine, ISSN 1757-4676, 01/2018, Volume 10, Issue 1, pp. 48 - 62
... spectrum. In addition to their clinical overlap, most cases of ALS and FTD display pathological accumulation of TAR‐DNA binding protein (TDP‐43), a ubiquitously... 
neurodegeneration | mass spectrometry | C9orf72 expansion mutation | protein co‐expression | TDP‐43 | TDP-43 | protein co-expression | NEURODEGENERATIVE DISEASE | MEDICINE, RESEARCH & EXPERIMENTAL | DIAGNOSIS | DEMENTIA | FRONTOTEMPORAL LOBAR DEGENERATION | C9ORF72 | COEXPRESSION | BEHAVIORAL VARIANT | LATERAL-SCLEROSIS | PROTEINS | HEXANUCLEOTIDE REPEAT | C9orf72 Protein - genetics | Frontotemporal Dementia - genetics | Proteome - genetics | Amyotrophic Lateral Sclerosis - genetics | Humans | Gene Expression Regulation | Male | DNA-Binding Proteins - genetics | Gene Regulatory Networks | Protein Interaction Maps | Brain - metabolism | DNA-Binding Proteins - metabolism | Frontotemporal Dementia - metabolism | Amyotrophic Lateral Sclerosis - pathology | Proteolysis | Amyotrophic Lateral Sclerosis - metabolism | Proteomics | Brain - pathology | Female | C9orf72 Protein - metabolism | Protein Processing, Post-Translational | Mutation | Proteome - metabolism | Frontotemporal Dementia - pathology | Brain | Nervous system diseases | Phenotype | Disease transmission | RNA | Genetic research | Genetic aspects | Binding proteins | Mass spectrometry | Protein-protein interactions | Dementia | Protein binding | Disease | Neurodegenerative diseases | Cortex | Cognitive ability | Amyotrophic lateral sclerosis | Mass spectroscopy | Inflammation | Ribonucleic acid--RNA | Microglia | Proteins | Pathology | RNA-binding protein | Synaptic transmission | Dementia disorders | Frontotemporal dementia | Protein interaction | Neuroscience | Post-translational Modifications, Proteolysis & Proteomics
Journal Article
Journal Article
Nature communications, ISSN 2041-1723, 2018, Volume 9, Issue 1, pp. 2794 - 18
Journal Article
Acta neuropathologica, ISSN 0001-6322, 2016, Volume 132, Issue 2, pp. 175 - 196
Journal Article
Nature genetics, ISSN 1546-1718, 2018, Volume 50, Issue 4, pp. 603 - 612
Journal Article