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1999, Methods in enzymology, ISBN 0121822109, Volume 309, 412, 413., 3 v.
This volume includes a core of methodologies to attack the unique experimental problems presented by protein misassembly... 
Prions | Amyloid | Amyloid beta-protein | Proteins
Book
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