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Molecular Cell, ISSN 1097-2765, 10/2015, Volume 60, Issue 2, pp. 208 - 219
Eukaryotic cells possess numerous dynamic membrane-less organelles, RNP granules, enriched in RNA and RNA-binding proteins containing disordered regions. We... 
TRANSITION | EUKARYOTIC STRESS GRANULES | CELL-FREE FORMATION | PRION-LIKE DOMAINS | NUCLEOLI | BEHAVIOR | BIOCHEMISTRY & MOLECULAR BIOLOGY | REGIONS | BODIES | P GRANULES | AGGREGATION | CELL BIOLOGY | Organelles - chemistry | Fluorescence Recovery After Photobleaching | Humans | Polyethylene Glycols - chemistry | Amyloid - chemistry | Cytoplasmic Granules - chemistry | Molecular Mimicry | Amyloid - metabolism | Protein Aggregation, Pathological - pathology | Solutions | Cytoplasmic Granules - metabolism | Escherichia coli - metabolism | Heterogeneous-Nuclear Ribonucleoprotein Group A-B - genetics | Protein Aggregation, Pathological - genetics | RNA - metabolism | Sodium Chloride - chemistry | Protein Structure, Tertiary | Recombinant Proteins - metabolism | Amyloid - genetics | Gene Expression | Recombinant Proteins - chemistry | Heterogeneous-Nuclear Ribonucleoprotein Group A-B - metabolism | Recombinant Proteins - genetics | RNA - chemistry | Intrinsically Disordered Proteins - genetics | Heterogeneous Nuclear Ribonucleoprotein A1 | Heterogeneous-Nuclear Ribonucleoprotein Group A-B - chemistry | Escherichia coli - genetics | Intrinsically Disordered Proteins - chemistry | Protein Binding | Organelles - metabolism | Protein Aggregation, Pathological - metabolism | Intrinsically Disordered Proteins - metabolism | Fluorescence | Marine biology | Chemical properties | RNA | Binding proteins | Protein binding | Yuan (China)
Journal Article
Biochemical Journal, ISSN 0264-6021, 04/2017, Volume 474, Issue 8, pp. 1417 - 1438
Approximately 70 human RNA-binding proteins (RBPs) contain a prion-like domain (PrLD). PrLDs are low-complexity domains that possess a similar amino acid... 
EUKARYOTIC STRESS GRANULES | MUTANT FUS PROTEINS | MULTISYSTEM PROTEINOPATHY | BIOCHEMISTRY & MOLECULAR BIOLOGY | PHASE-TRANSITION | TARDBP MUTATIONS | HNRNP A1 | AMYOTROPHIC-LATERAL-SCLEROSIS | FRONTOTEMPORAL LOBAR DEGENERATION | HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEINS | NEURODEGENERATIVE DISEASES | Proteostasis Deficiencies - metabolism | RNA-Binding Proteins - genetics | TATA-Binding Protein Associated Factors - metabolism | Humans | Prion Proteins - metabolism | DNA-Binding Proteins - metabolism | Frontotemporal Dementia - metabolism | RNA-Binding Protein FUS - chemistry | TDP-43 Proteinopathies - genetics | Protein Domains | TDP-43 Proteinopathies - pathology | Prion Proteins - chemistry | Prion Proteins - genetics | Heterogeneous-Nuclear Ribonucleoprotein Group A-B - genetics | Frontotemporal Dementia - pathology | Calmodulin-Binding Proteins - genetics | Frontotemporal Dementia - genetics | Cytoplasmic Granules | Neurodegenerative Diseases - pathology | Amyotrophic Lateral Sclerosis - genetics | RNA-Binding Proteins - chemistry | TDP-43 Proteinopathies - metabolism | Proteostasis Deficiencies - pathology | RNA-Binding Protein FUS - genetics | Heterogeneous-Nuclear Ribonucleoprotein Group A-B - metabolism | Neurodegenerative Diseases - genetics | Calmodulin-Binding Proteins - chemistry | Calmodulin-Binding Proteins - metabolism | RNA-Binding Protein FUS - metabolism | Neurodegenerative Diseases - metabolism | TATA-Binding Protein Associated Factors - chemistry | DNA-Binding Proteins - genetics | TATA-Binding Protein Associated Factors - genetics | DNA-Binding Proteins - chemistry | Heterogeneous Nuclear Ribonucleoprotein A1 | Proteostasis Deficiencies - genetics | Amyotrophic Lateral Sclerosis - pathology | Heterogeneous-Nuclear Ribonucleoprotein Group A-B - chemistry | Amyotrophic Lateral Sclerosis - metabolism | Mutation | RNA-Binding Proteins - metabolism | RNA-Binding Protein EWS
Journal Article
Nature, ISSN 0028-0836, 03/2013, Volume 495, Issue 7442, pp. 467 - 473
Algorithms designed to identify canonical yeast prions predict that around 250 human proteins, including several RNA-binding proteins associated with... 
RNA-BINDING PROTEINS | DROSOPHILA MODEL | TDP-43 | MULTIDISCIPLINARY SCIENCES | FRONTOTEMPORAL DEMENTIA | VCP MUTATIONS | DISEASE | AMYOTROPHIC-LATERAL-SCLEROSIS | SACCHAROMYCES-CEREVISIAE | STRESS GRANULES | MULTIPLE ALIGNMENT | Prions - genetics | Humans | Molecular Sequence Data | Osteitis Deformans - metabolism | Male | Drosophila melanogaster - genetics | Osteitis Deformans - genetics | Drosophila melanogaster - metabolism | Frontotemporal Dementia - metabolism | Muscular Dystrophies, Limb-Girdle - genetics | Myositis, Inclusion Body - pathology | Female | Inclusion Bodies - metabolism | Muscular Dystrophies, Limb-Girdle - pathology | Heterogeneous-Nuclear Ribonucleoprotein Group A-B - genetics | Frontotemporal Dementia - pathology | RNA - metabolism | Frontotemporal Dementia - genetics | Amino Acid Sequence | Prions - metabolism | Peptide Termination Factors - genetics | Amyotrophic Lateral Sclerosis - genetics | Drosophila melanogaster - cytology | Mutant Proteins - genetics | Heterogeneous-Nuclear Ribonucleoprotein Group A-B - metabolism | Mutant Proteins - metabolism | Protein Structure, Tertiary - genetics | Prions - chemistry | Saccharomyces cerevisiae Proteins - genetics | Mutation - genetics | Myositis, Inclusion Body - genetics | Peptide Termination Factors - metabolism | Amyotrophic Lateral Sclerosis - pathology | Inclusion Bodies - genetics | Osteitis Deformans - pathology | Animals | Heterogeneous-Nuclear Ribonucleoprotein Group A-B - chemistry | Muscular Dystrophies, Limb-Girdle - metabolism | Mutant Proteins - chemistry | Amyotrophic Lateral Sclerosis - metabolism | Saccharomyces cerevisiae Proteins - metabolism | Inclusion Bodies - pathology | Myositis, Inclusion Body - metabolism | Mice | Peptide Termination Factors - chemistry | HeLa Cells | Saccharomyces cerevisiae Proteins - chemistry | Pathology | Insects | Genomics | Genetics | Software | Genomes | Mutation | Genetic testing | Patients
Journal Article
Cellular and Molecular Life Sciences, ISSN 1420-682X, 04/2009, Volume 66, Issue 7, pp. 1239 - 1256
Journal Article