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Journal Article
Molecular cell, ISSN 1097-2765, 2018, Volume 70, Issue 4, pp. 588 - 601.e6
Huntington’s disease is caused by an abnormally long polyglutamine tract in the huntingtin protein. This leads to the generation and deposition of N-terminal... 
huntingtin exon1 | aggregation | phase transition | polyQ | electron tomography | fluorescence microscopy | P-BODIES | FLANKING SEQUENCES | PROTEIN | NEURONAL DEATH | BIOCHEMISTRY & MOLECULAR BIOLOGY | IN-VIVO | MUTANT HUNTINGTIN | POLYGLUTAMINE AGGREGATION | STRESS GRANULES | TRANSGENIC MICE | YEAST-CELLS | CELL BIOLOGY | Proteins | Analysis | Proline | Fluorescence | Molecular biology | Fluorescence microscopy | Cells
Journal Article
Genetics (Austin), ISSN 1943-2631, 2012, Volume 190, Issue 2, pp. 581 - 600
Journal Article
Journal Article
Molecular cell, ISSN 1097-2765, 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)
Journal Article
The Journal of biological chemistry, ISSN 1083-351X, 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 | post-translational modification (PTM) | Molecular Bases of Disease | fibril | protein misfolding | Parkinson disease | endocytosis | protein self-assembly | protein kinase | vesicles
Journal Article
Journal Article
PLoS genetics, ISSN 1553-7404, 2018, Volume 14, Issue 7, p. e1007517
.... We developed a genetic screen in yeast that allowed us to explore the sequence features that promote degradation versus aggregation of a model glutamine/asparagine (Q/N... 
EXPOSED HYDROPHOBICITY | SUBSTRATE-SPECIFICITY | GENETICS & HEREDITY | QUALITY-CONTROL DEGRADATION | ALS | AMYOTROPHIC-LATERAL-SCLEROSIS | MUTATIONS | FRONTOTEMPORAL LOBAR DEGENERATION | CHAPERONE | SACCHAROMYCES-CEREVISIAE | YEAST PRION | Prions - metabolism | Neurodegenerative Diseases - pathology | Prions - genetics | Peptide Termination Factors - genetics | Humans | Glutamine - metabolism | Heterogeneous-Nuclear Ribonucleoprotein Group A-B - metabolism | Neurodegenerative Diseases - genetics | Amino Acid Sequence - genetics | Saccharomyces cerevisiae Proteins - genetics | Peptide Termination Factors - metabolism | Protein Domains - genetics | Protein Aggregation, Pathological - pathology | Proteolysis | Asparagine - metabolism | Glutamine - genetics | Saccharomyces cerevisiae Proteins - metabolism | Heterogeneous-Nuclear Ribonucleoprotein Group A-B - genetics | Protein Aggregation, Pathological - genetics | Asparagine - genetics | Protein research | Nucleotide sequence | Protein folding | Prions | Genetic research | Genetic aspects | Research | Nervous system diseases | Analysis | Quality control | Control systems | Glycine | Genetic screening | Quality management | Biodegradation | Yeast | Disease | Neurodegenerative diseases | Amino acids | Biochemistry | Mammals | Proteins | Algorithms | Asparagine | Mutation | Molecular biology | Prion protein | Protein interaction | Glutamine
Journal Article