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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) | Index Medicus
Journal Article
Journal Article
Journal Article
Annual Review of Biochemistry, ISSN 0066-4154, 6/2017, Volume 86, Issue 1, pp. 21 - 26
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 01/2017, Volume 114, Issue 3, pp. 574 - 579
Alzheimer's disease (AD) and other neurodegenerative disorders are associated with the cytoplasmic aggregation of microtubule-associated protein tau. Recent... 
Immunoreceptors | Antibodies | Tau | Neurodegeneration | Intracellular immunity | PROTEIN-TAU | ISOFORMS | PHOSPHORYLATION | MULTIDISCIPLINARY SCIENCES | neurodegeneration | tau | PATHOLOGY | FILAMENTS | IMMUNOTHERAPY | intracellular immunity | NEURONS | antibodies | immunoreceptors | NEUTRALIZATION | BRAIN | Protein Aggregates | Proteostasis Deficiencies - metabolism | tau Proteins - immunology | Humans | Receptors, Fc - metabolism | Antibodies, Neutralizing - metabolism | tau Proteins - metabolism | Nerve Degeneration - metabolism | tau Proteins - chemistry | Receptors, Fc - deficiency | Nerve Degeneration - prevention & control | Protein Aggregation, Pathological - prevention & control | Ribonucleoproteins - genetics | Neurons - metabolism | Protein Aggregation, Pathological - immunology | Ribonucleoproteins - deficiency | Mice, Inbred C57BL | Cells, Cultured | Neurons - immunology | Nerve Degeneration - immunology | Ribonucleoproteins - metabolism | Mice, Knockout | Proteostasis Deficiencies - prevention & control | Animals | Cytosol - metabolism | Receptors, Fc - genetics | Mice | Proteasome Endopeptidase Complex - metabolism | In Vitro Techniques | Protein Aggregation, Pathological - metabolism | Physiological aspects | Protein folding | Alzheimer's disease | Health aspects | Proteins | Fluorescence | Pathogens | Alzheimers disease | Morphology | Immune system | Index Medicus | Biological Sciences
Journal Article
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 02/2016, Volume 291, Issue 9, pp. 4374 - 4385
Although trace levels of phosphorylated alpha-synuclein (alpha-syn) are detectable in normal brains, nearly all alpha-syn accumulated within Lewy bodies in... 
MULTIPLE SYSTEM ATROPHY | INCLUSION FORMATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | DISEASE-LINKED MUTATIONS | LEWY BODY DISEASE | MEDIATED PHOSPHORYLATION | SER-129 PHOSPHORYLATION | PARKINSONS-DISEASE | TRANSGENIC MICE | CELL-DEATH | OLIGODENDROGLIAL CELLS | Phosphorylation | Mesencephalon - cytology | Dopaminergic Neurons - pathology | Mesencephalon - metabolism | Humans | Synaptosomes - metabolism | Recombinant Fusion Proteins - metabolism | Dopaminergic Neurons - cytology | Endocytosis | Synaptosomes - pathology | Protein Aggregation, Pathological - pathology | Dopaminergic Neurons - metabolism | Parkinson Disease - metabolism | alpha-Synuclein - genetics | Protein Aggregation, Pathological - genetics | Protein-Serine-Threonine Kinases - metabolism | Mesencephalon - pathology | Animals, Newborn | Recombinant Proteins - metabolism | Cell Line | Parkinson Disease - pathology | Cells, Cultured | Protein-Serine-Threonine Kinases - genetics | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Parkinson Disease - genetics | Serine - metabolism | Protein Folding | alpha-Synuclein - chemistry | Animals | Recombinant Fusion Proteins - genetics | Mice | Protein Processing, Post-Translational | Mutation | alpha-Synuclein - metabolism | Protein Aggregation, Pathological - metabolism | Amino Acid Substitution | Index Medicus | post-translational modification (PTM) | Molecular Bases of Disease | fibril | protein misfolding | Parkinson disease | endocytosis | protein self-assembly | protein kinase | vesicles
Journal Article