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Journal Article
Proceedings of the National Academy of Sciences of the United States, ISSN 0027-8424, 12/2017, Volume 114, Issue 50, p. 13176
[alpha]-Synuclein accumulation is a pathological hallmark of Parkinson's disease (PD). Ubiquitinated [alpha]-synuclein is targeted to proteasomal or lysosomal... 
Proteins | Ubiquitin-proteasome system | Properties | Methods | Ubiquitin | Parkinson's disease | Neurodegenerative diseases | Substantia nigra | Parkinsons disease | Lysosomes | Agglomeration | Synuclein | Cells | Accumulation | Lewy bodies | Mutants | Degradation | SUMO protein | Ubiquitination | Proteasomes | Mutation | Movement disorders
Journal Article
2015, Methods in molecular biology, ISBN 149392978X, Volume 1345
This detailed volume focuses on methods for the characterization of aggregation processes that lead to the formation of amyloid fibrils and amyloid oligomers... 
Proteins | Protein Aggregates | Life sciences | Amyloid | Protein Aggregation, Pathological
Web Resource
Journal of Clinical Investigation, ISSN 0021-9738, 03/2014, Volume 124, Issue 3, pp. 1144 - 1157
Journal Article
Web Resource
Nature, ISSN 0028-0836, 07/2015, Volume 523, Issue 7562, pp. 607 - 611
The human lens is comprised largely of crystallin proteins assembled into a highly ordered, interactive macro-structure essential for lens transparency and... 
SELENITE-INDUCED CATARACTOGENESIS | MULTIDISCIPLINARY SCIENCES | MUTATION | PREVENTION | ALPHA-B-CRYSTALLIN | DOMINANT CONGENITAL CATARACT | HUMAN OXIDOSQUALENE CYCLASE | SEQUENCING DATA | CHINESE FAMILY | LENS | EXPRESSION | Crystallins - metabolism | Humans | Cataract - pathology | Molecular Sequence Data | Lanosterol - pharmacology | Male | Amyloid - chemistry | Amyloid - ultrastructure | Lens, Crystalline - pathology | Mutant Proteins - ultrastructure | Amyloid - metabolism | Protein Aggregation, Pathological - pathology | Base Sequence | Amyloid - drug effects | Adult | Female | Child | Crystallins - chemistry | Protein Aggregates - drug effects | Amino Acid Sequence | Cell Line | Crystallins - ultrastructure | Lanosterol - administration & dosage | Mutant Proteins - genetics | Lens, Crystalline - metabolism | Models, Molecular | Mutant Proteins - metabolism | Crystallins - genetics | Cataract - metabolism | Lanosterol - therapeutic use | Protein Aggregation, Pathological - drug therapy | Animals | Cataract - congenital | Pedigree | Mutant Proteins - chemistry | Dogs | Cataract - genetics | Cataract - drug therapy | Lens, Crystalline - drug effects | Proteins | Cataract | Physiological aspects | Development and progression | Genetic aspects | Research | Gene expression | Drug therapy | Cataracts | Studies | Older people | Mortality | Mutation | Cholesterol | Index Medicus
Journal Article
Scientific Reports, ISSN 2045-2322, 12/2017, Volume 7, Issue 1, pp. 13556 - 18
Tau pathology is associated with cognitive decline in Alzheimer's disease, and missense tau mutations cause frontotemporal dementia. Hyperphosphorylation and... 
PHOSPHORYLATION | MULTIDISCIPLINARY SCIENCES | TANGLES | PAIRED HELICAL FILAMENTS | NEURONS | TAUOPATHY | MUTATIONS | MODEL | DEFICITS | EXPRESSION | SEVERITY | Phosphorylation | Vinblastine | Neurodegenerative diseases | Cognitive ability | Forebrain | Proline | Pathology | Tau protein | Microtubules | Dementia disorders | Cytoskeleton | Mutation | Frontotemporal dementia | Dementia | Index Medicus
Journal Article
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