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Proceedings of the National Academy of Sciences - PNAS, ISSN 1091-6490, 12/2016, Volume 113, Issue 50, pp. E8187 - E8196
...) tau prions, were used to infect HEK293T cells expressing 3R tau fused to yellow fluorescent protein (YFP... 
Pick's disease | Tauopathies | Argyrophilic grain disease | Progressive supranuclear palsy | Corticobasal degeneration | Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | Up-Regulation | Chronic Traumatic Encephalopathy - metabolism | Humans | Bacterial Proteins - chemistry | tau Proteins - metabolism | Pick Disease of the Brain - genetics | Recombinant Fusion Proteins - metabolism | tau Proteins - chemistry | Protein Isoforms - metabolism | tau Proteins - genetics | Chronic Traumatic Encephalopathy - genetics | HEK293 Cells | Luminescent Proteins - chemistry | Pick Disease of the Brain - metabolism | Supranuclear Palsy, Progressive - genetics | Cell Line | Bacterial Proteins - genetics | Recombinant Fusion Proteins - chemistry | Alzheimer Disease - metabolism | Recombinant Fusion Proteins - genetics | Supranuclear Palsy, Progressive - metabolism | Bacterial Proteins - metabolism | Luminescent Proteins - genetics | Mutation | Alzheimer Disease - genetics | Luminescent Proteins - metabolism | Protein Isoforms - genetics | Physiological aspects | Alzheimer's disease | Health aspects | Prions | Encephalopathy | Proteins | Brain | Alzheimers disease | Cells | Index Medicus | Biological Sciences | PNAS Plus | corticobasal degeneration | tauopathies | argyrophilic grain disease | Pick’s disease | progressive supranuclear palsy
Journal Article
Journal Article
Journal Article
Biochemical journal, ISSN 1470-8728, 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... 
Life Sciences & Biomedicine | Biochemistry & Molecular Biology | Science & Technology | 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 | Index Medicus
Journal Article
Nature (London), ISSN 1476-4687, 05/2012, Volume 485, Issue 7399, pp. 507 - 511
.... Many of these disorders, including Alzheimer's, Parkinson's and prion diseases, are associated with the accumulation of misfolded disease-specific proteins... 
Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | Neurons - pathology | Neuroprotective Agents | Phosphorylation | Prions - genetics | Eukaryotic Initiation Factor-2 - chemistry | Neurodegenerative Diseases - etiology | PrPSc Proteins - analysis | Synapses - pathology | Thiourea - pharmacology | Phosphoproteins - metabolism | Repressor Proteins - analysis | PrPSc Proteins - metabolism | Synapses - metabolism | Phosphoproteins - analysis | Protein Folding - drug effects | Protein Phosphatase 1 - genetics | Eukaryotic Initiation Factor-2 - metabolism | Synaptic Transmission - drug effects | Cell Death - drug effects | PrPSc Proteins - toxicity | Neurons - drug effects | Repressor Proteins - metabolism | Prions - metabolism | Synapses - drug effects | Repressor Proteins - chemistry | Neurodegenerative Diseases - pathology | Mice, Inbred C57BL | Kaplan-Meier Estimate | Hippocampus - pathology | Prion Diseases - pathology | Neurodegenerative Diseases - metabolism | Hippocampus - cytology | Cinnamates - pharmacology | Eukaryotic Initiation Factor-2 - analysis | Hippocampus - metabolism | Protein Phosphatase 1 - metabolism | Animals | Prions - biosynthesis | Protein Biosynthesis - drug effects | Mice | Unfolded Protein Response - physiology | Thiourea - analogs & derivatives | Index Medicus
Journal Article