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Cell, ISSN 0092-8674, 06/2013, Volume 153, Issue 7, p. 1461
Summary Stress granules and P bodies are conserved cytoplasmic aggregates of nontranslating messenger ribonucleoprotein complexes (mRNPs) implicated in the... 
Journal Article
Cell, ISSN 0092-8674, 10/2016, Volume 167, Issue 3, pp. 774 - 788.e17
Journal Article
Molecular Cell, ISSN 1097-2765, 03/2017, 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... 
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
Journal Article
Molecular Cell, ISSN 1097-2765, 03/2018, Volume 69, Issue 6, pp. 965 - 978.e6
Under stress, certain eukaryotic proteins and RNA assemble to form membraneless organelles known as stress granules. The most well-studied stress granule... 
LLPS | Ubiquilin-2 | multivalent interactions | liquid-liquid phase separation | stress granules | protein quality control | ligand-induced phase transition | NMR spectroscopy | amyotrophic lateral sclerosis | ubiquitin | INTRINSICALLY DISORDERED PROTEINS | DOMAIN | LINKED MUTATIONS | N-15 RELAXATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | ALS | ENDOPLASMIC-RETICULUM | SECONDARY STRUCTURE | FAMILY PROTEINS | AUTOPHAGY | STRESS GRANULES | CELL BIOLOGY | Ubiquitins - genetics | Humans | Cell Cycle Proteins - metabolism | Stress, Physiological | Models, Molecular | Ubiquitins - chemistry | Structure-Activity Relationship | Intrinsically Disordered Proteins - genetics | Protein Aggregation, Pathological | Protein Folding | Cell Cycle Proteins - chemistry | Intrinsically Disordered Proteins - chemistry | Cytoplasmic Granules - metabolism | Cell Cycle Proteins - genetics | Protein Binding | Protein Domains | Female | Protein Conformation | HeLa Cells | Proteasome Endopeptidase Complex - metabolism | Binding Sites | Ubiquitins - metabolism | Intrinsically Disordered Proteins - metabolism | Ubiquitin | Oligomers | Medical colleges | RNA | Developmental biology | Physiological aspects | Nuclear magnetic resonance spectroscopy | Liquid crystal displays | Molecular biology | Binding proteins | Protein binding | liquid- liquid phase separation (LLPS) | amyotrophic lateral sclerosis (ALS)
Journal Article
Neuron, ISSN 0896-6273, 04/2013, Volume 78, Issue 1, pp. 65 - 80
Mutations in VCP cause multisystem degeneration impacting the nervous system, muscle, and/or bone. Patients may present with ALS, Parkinsonism, frontotemporal... 
PATHOGENESIS | PARKIN | VALOSIN-CONTAINING-PROTEIN | INCLUSION-BODY MYOPATHY | DROSOPHILA MODEL | FRONTOTEMPORAL DEMENTIA | PAGETS-DISEASE | BONE | NEUROSCIENCES | P97 | DEGENERATION | Embryo, Mammalian | Humans | Ganglia, Spinal - cytology | Drosophila Proteins - metabolism | HSP72 Heat-Shock Proteins - genetics | Protein Tyrosine Phosphatases - genetics | Neurons - ultrastructure | Time Factors | Carbonyl Cyanide m-Chlorophenyl Hydrazone - pharmacology | Neuromuscular Junction - genetics | Neurons - metabolism | Protein-Serine-Threonine Kinases - metabolism | Mitochondrial Membrane Transport Proteins - metabolism | Cell Cycle Proteins - metabolism | Enzyme Inhibitors - pharmacology | Ubiquitin-Protein Ligases - metabolism | Adenosine Triphosphatases - metabolism | Mutation - genetics | Leupeptins - pharmacology | GTP Phosphohydrolases - metabolism | Luminescent Proteins - genetics | Adenosine Triphosphatases - genetics | Ubiquitin-Protein Ligases - genetics | RNA, Small Interfering - metabolism | Immunoprecipitation | Neuromuscular Junction - metabolism | Valosin Containing Protein | Mitochondria - ultrastructure | Transfection | Mitochondria - genetics | Proton Ionophores - pharmacology | Cell Cycle Proteins - genetics | Microscopy, Electron, Transmission | Animals, Genetically Modified | Gene Expression Regulation - genetics | Drosophila | RNA, Small Interfering - pharmacology | Cells, Cultured | Protein-Serine-Threonine Kinases - genetics | Nuclear Proteins - metabolism | Mitochondria - metabolism | Mitochondria - drug effects | Transcription Factors - genetics | Transcription Factors - metabolism | Animals | Proteins - metabolism | Drosophila Proteins - genetics | In Vitro Techniques | Ubiquitination - genetics | Luminescent Proteins - metabolism | Ubiquitin | Analysis | Genomics | Quality control | Amyotrophic lateral sclerosis | Genetic aspects | Mitochondrial DNA | Dementia | Neurons | Parkinsons disease | Biosynthesis | Digital cameras | Kinases | DNA repair | Proteins | Mitochondria | Brain research | Insects | Microscopy | Morphology | Mutation
Journal Article
The EMBO Journal, ISSN 0261-4189, 06/2016, Volume 35, Issue 12, pp. 1254 - 1275
Journal Article
Cell, ISSN 0092-8674, 6/2013, Volume 153, Issue 7, pp. 1461 - 1474
Stress granules and P-bodies are conserved cytoplasmic aggregates of non-translating mRNPs implicated in the regulation of mRNA translation and decay, and are... 
Journal Article
Human Molecular Genetics, ISSN 0964-6906, 03/2016, Volume 25, Issue 5, pp. 936 - 950
Adult-onset inherited myopathies with similar pathological features, including hereditary inclusion body myopathy (hIBM) and limb-girdle muscular dystrophy... 
RNA-PROCESSING PROTEIN | PRION-LIKE DOMAINS | BIOCHEMISTRY & MOLECULAR BIOLOGY | BINDING PROTEINS | GENETICS & HEREDITY | MOLECULAR CHAPERONE | GIRDLE MUSCULAR-DYSTROPHY | AMYOTROPHIC-LATERAL-SCLEROSIS | MUTATIONS | STRESS GRANULES | AGGREGATION | MULTIPLE ALIGNMENT | RNA-Binding Proteins - genetics | Molecular Chaperones - metabolism | Humans | Myositis, Inclusion Body - congenital | Molecular Sequence Data | Contracture - genetics | Drosophila Proteins - metabolism | Drosophila melanogaster - genetics | Muscles - pathology | DNA-Binding Proteins - metabolism | Drosophila melanogaster - metabolism | Muscular Dystrophies, Limb-Girdle - genetics | Myositis, Inclusion Body - pathology | Adult | Muscles - metabolism | Muscular Dystrophies, Limb-Girdle - pathology | Heterogeneous-Nuclear Ribonucleoprotein Group A-B - genetics | Disease Models, Animal | Amino Acid Sequence | HSP40 Heat-Shock Proteins - metabolism | HSP40 Heat-Shock Proteins - genetics | Signal Transduction | Ophthalmoplegia - pathology | Contracture - pathology | Gene Expression Regulation | Molecular Chaperones - genetics | Heterogeneous-Nuclear Ribonucleoproteins - metabolism | Heterogeneous-Nuclear Ribonucleoprotein Group A-B - metabolism | DNA-Binding Proteins - genetics | Myositis, Inclusion Body - genetics | Nerve Tissue Proteins - genetics | Heterogeneous-Nuclear Ribonucleoproteins - genetics | Nerve Tissue Proteins - metabolism | Sequence Homology, Amino Acid | Contracture - metabolism | Contracture - congenital | Phenotype | Sequence Alignment | Animals | Muscular Dystrophies, Limb-Girdle - metabolism | Age of Onset | Protein Binding | Myositis, Inclusion Body - metabolism | Ophthalmoplegia - genetics | Drosophila Proteins - genetics | Mutation | RNA-Binding Proteins - metabolism | Ophthalmoplegia - metabolism
Journal Article
Human Molecular Genetics, ISSN 0964-6906, 03/2016, Volume 25, Issue 5, pp. 936 - 950
Journal Article
EMBO Journal, ISSN 0261-4189, 08/2016, Volume 35, Issue 15, p. 1628
  Intramembrane proteases execute fundamental biological processes ranging from crucial signaling events to general membrane proteostasis. Despite the... 
Alzheimers disease | Binding sites | Mutation
Journal Article
Molecular and Cellular Biochemistry, ISSN 0300-8177, 10/2011, Volume 356, Issue 1, pp. 261 - 267
Journal Article