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Experimental & molecular medicine, ISSN 2092-6413, 2015, Volume 47, Issue 3, pp. e147 - e147
Mammalian cells remove misfolded proteins using various proteolytic systems, including the ubiquitin (Ub)-proteasome system (UPS), chaperone mediated autophagy... 
MEDICINE, RESEARCH & EXPERIMENTAL | UBIQUITIN-PROTEASOME SYSTEM | CHAPERONE-MEDIATED AUTOPHAGY | ALPHA-SYNUCLEIN AGGREGATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | QUALITY CONTROL DEGRADATION | CENTRAL-NERVOUS-SYSTEM | AMYOTROPHIC-LATERAL-SCLEROSIS | SOD1 TRANSGENIC MICE | ENDOPLASMIC-RETICULUM STRESS | END RULE PATHWAY | PARKINSONS-DISEASE | Proteostasis Deficiencies - metabolism | Humans | Ubiquitin - metabolism | tau Proteins - metabolism | Parkinson Disease - drug therapy | Molecular Targeted Therapy | Neurodegenerative Diseases - drug therapy | Amyotrophic Lateral Sclerosis - drug therapy | Autophagy - drug effects | DNA-Binding Proteins - metabolism | PrPSc Proteins - metabolism | Lysosomes - metabolism | Proteolysis | Amyloid beta-Peptides - metabolism | Parkinson Disease - metabolism | Huntington Disease - drug therapy | Superoxide Dismutase - metabolism | Prion Diseases - drug therapy | Alzheimer Disease - drug therapy | Neurodegenerative Diseases - metabolism | Huntington Disease - metabolism | Nerve Tissue Proteins - genetics | Nerve Tissue Proteins - metabolism | Huntingtin Protein | Animals | Alzheimer Disease - metabolism | Amyotrophic Lateral Sclerosis - metabolism | Huntington Disease - genetics | Mutation | Proteasome Endopeptidase Complex - metabolism | alpha-Synuclein - metabolism | Prion Diseases - metabolism | Review
Journal Article
Nature (London), ISSN 1476-4687, 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
Journal Article
Biochemical journal, ISSN 1470-8728, 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
British journal of pharmacology, ISSN 0007-1188, 2009, Volume 146, Issue 8, pp. 1041 - 1059
Journal Article
Journal Article