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Nature Chemical Biology, ISSN 1552-4450, 03/2008, Volume 4, Issue 3, pp. 197 - 199
Many amyloid inhibitors resemble molecules that form chemical aggregates, which are known to inhibit many proteins. Eight known chemical aggregators inhibited... 
FIBRIL FORMATION | YEAST | MECHANISM | BIOCHEMISTRY & MOLECULAR BIOLOGY | DISEASE | PROMISCUOUS INHIBITORS | NEUROTOXICITY | Molecular Weight | Detergents - chemistry | Microscopy, Electron, Transmission - methods | Phthalimides - chemistry | Structure-Activity Relationship | Benzopyrans - chemistry | Saccharomyces cerevisiae - metabolism | Clioquinol - chemistry | Phthalimides - pharmacology | Flavanones - chemistry | Sensitivity and Specificity | Acetophenones - pharmacology | Molecular Structure | Prions - pharmacokinetics | beta-Lactamase Inhibitors | Benzopyrans - pharmacology | Saccharomyces cerevisiae Proteins - pharmacokinetics | Recombinant Proteins - metabolism | Prions - metabolism | Recombinant Proteins - antagonists & inhibitors | Phenolphthaleins - chemistry | Saccharomyces cerevisiae Proteins - antagonists & inhibitors | Congo Red - pharmacology | Flavanones - pharmacology | Recombinant Proteins - chemistry | Prions - chemistry | Clioquinol - pharmacology | Prions - antagonists & inhibitors | Saccharomyces cerevisiae - chemistry | Particle Size | Phenolphthaleins - pharmacology | beta-Lactamases - chemistry | Animals | Acetophenones - chemistry | Peptide Termination Factors | Mice | Congo Red - chemistry | Saccharomyces cerevisiae Proteins - chemistry | Proteins | Biochemistry | Inhibitor drugs | Molecular biology | Prions | Index Medicus
Journal Article
Science, ISSN 0036-8075, 12/2007, Volume 318, Issue 5858, pp. 1900 - 1903
Journal Article
Journal of Molecular Biology, ISSN 0022-2836, 2008, Volume 380, Issue 2, pp. 425 - 436
Journal Article
Cell, ISSN 0092-8674, 04/2018, Volume 173, Issue 3, pp. 677 - 692.e20
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
PLoS ONE, ISSN 1932-6203, 09/2009, Volume 4, Issue 9, pp. e7052 - e7052
Neurodegenerative disorders share common features comprising aggregation of misfolded proteins, failure of the ubiquitin-proteasome system, and increased... 
BIOLOGY | Protein Structure, Tertiary | Protein Structure, Secondary | Microscopy, Electron, Transmission - methods | Solvents - chemistry | Humans | Molecular Conformation | Chelating Agents - chemistry | Ubiquitin - chemistry | Ubiquitin - metabolism | Spectroscopy, Fourier Transform Infrared | Copper - chemistry | Alzheimer Disease - metabolism | Copper - metabolism | Microscopy, Atomic Force | Protein Binding | Cell Membrane - metabolism | Proteasome Endopeptidase Complex - metabolism | Electrochemistry - methods | Oligomers | Ubiquitin | Development and progression | Nervous system diseases | Analysis | Electric properties | Brain | Atomic force microscopy | Parkinson's disease | Aluminum | Disorders | Conglomerates | Sclerosis | Risk factors | Proteins | Ring structures | Particle physics | Dichroism | Chelation | Copper | Alzheimer's disease | Movement disorders | Cadmium | Dielectric constant | Trifluoroethanol | Neurodegenerative diseases | Infrared spectra | Electron microscopy | Fatty acids | Substrates | Circular dichroism | Studies | Aggregates | Proteasomes | Dismantling | Parkinsons disease | Chain branching | Lipids | Agglomeration | Infrared analysis | Protein folding | Spectrum analysis | Amyloid | Incubation | Gel electrophoresis | Health risks | Particulates | Amyotrophic lateral sclerosis | Clustering | Phosphocholine | Zinc | Coalescing | Transmission electron microscopy | N-Terminus | Nickel | Dimers | Liposomes | Alzheimers disease | Coalescence | Index Medicus
Journal Article
Molecular Cell, ISSN 1097-2765, 10/2015, Volume 60, Issue 2, pp. 231 - 241
Phase-separated states of proteins underlie ribonucleoprotein (RNP) granules and nuclear RNA-binding protein assemblies that may nucleate protein inclusions... 
CELL-FREE FORMATION | PROTEIN | PHOSPHORYLATION | PRION-LIKE DOMAINS | PHASE-TRANSITIONS | TDP-43 | BIOCHEMISTRY & MOLECULAR BIOLOGY | ALS | FUS/TLS | ARGININE METHYLATION | ALPHA-SYNUCLEIN | CELL BIOLOGY | RNA-Binding Proteins - genetics | Humans | Molecular Sequence Data | RNA Polymerase II - metabolism | Cytoplasmic Granules - chemistry | Phase Transition | RNA-Binding Protein FUS - chemistry | Molecular Mimicry | Cytoplasmic Granules - metabolism | Escherichia coli - metabolism | Binding Sites | RNA Polymerase II - chemistry | RNA - metabolism | Protein Structure, Tertiary | Recombinant Proteins - metabolism | Prions - metabolism | Gene Expression | Rheology | RNA-Binding Proteins - chemistry | RNA-Binding Protein FUS - genetics | Recombinant Proteins - chemistry | RNA-Binding Protein FUS - metabolism | Recombinant Proteins - genetics | Prions - chemistry | RNA - chemistry | Intrinsically Disordered Proteins - genetics | Amino Acid Motifs | Escherichia coli - genetics | Intrinsically Disordered Proteins - chemistry | Protein Binding | RNA Polymerase II - genetics | RNA-Binding Proteins - metabolism | Intrinsically Disordered Proteins - metabolism | Proteins | Nervous system diseases | Sarcoma | RNA | Physiological aspects | Fluorescence | Nuclear magnetic resonance spectroscopy | Molecular biology | Fluorescence microscopy | Cells | Protein binding | Analysis | Index Medicus
Journal Article