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PLoS ONE, ISSN 1932-6203, 09/2017, Volume 12, Issue 9, p. e0180905
Proteins associated with neurodegenerative diseases are highly pleiomorphic and may adopt an all-a-helical fold in one environment, assemble into all-beta-sheet or collapse into a coil in another... 
ALPHA-SYNUCLEIN OLIGOMERS | ATOMIC-FORCE MICROSCOPY | SOLID-STATE NMR | SODIUM DODECYL-SULFATE | MULTIDISCIPLINARY SCIENCES | PARTIALLY FOLDED STRUCTURE | PAIRED HELICAL FILAMENTS | AMYLOID-BETA-PROTEIN | C-TERMINAL THREONINE | INDUCED CONFORMATIONAL-CHANGES | HUMAN PRION PROTEIN | Protein Aggregates | Protein Structure, Secondary | Humans | Protein Multimerization | Models, Molecular | tau Proteins - metabolism | PrPSc Proteins - chemistry | Protein Folding | tau Proteins - chemistry | PrPSc Proteins - genetics | alpha-Synuclein - chemistry | PrPSc Proteins - metabolism | Animals | tau Proteins - genetics | Amyloid beta-Peptides - genetics | Amyloid beta-Peptides - metabolism | Protein Domains | alpha-Synuclein - genetics | Amyloid beta-Peptides - chemistry | Protein Stability | alpha-Synuclein - metabolism | Electrons | Hydrogen-Ion Concentration | Protein folding | Physiological aspects | Nervous system | Development and progression | Degeneration | Genetic aspects | Research | Coils | Amyloidogenesis | Backbone | Rate constants | Agglomeration | Synuclein | pH effects | Neuromodulation | Modulators | Proteins | Oligomers | Fibrillogenesis | Pathways | Chirality | Chemical bonds | Catalysis | Prion protein | Dimerization | Folding | Linkages | Polypeptides | Incubation | Neurodegenerative diseases | Tertiary structure | Polymerization | Shielding | Secondary structure | Density distribution | Neurological diseases | Chemistry | Tensors | Propagation (polymerization) | Aggregates | Tau protein | Prions | Morphology | β-Amyloid | Dimers | Mutation | Protein structure
Journal Article
Biochemical journal, ISSN 1470-8728, 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... 
EUKARYOTIC STRESS GRANULES | MUTANT FUS PROTEINS | MULTISYSTEM PROTEINOPATHY | BIOCHEMISTRY & MOLECULAR BIOLOGY | PHASE-TRANSITION | TARDBP MUTATIONS | HNRNP A1 | AMYOTROPHIC-LATERAL-SCLEROSIS | FRONTOTEMPORAL LOBAR DEGENERATION | HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEINS | NEURODEGENERATIVE DISEASES | 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
Journal Article
PLoS ONE, ISSN 1932-6203, 05/2014, Volume 9, Issue 5, p. e95914
Protein conformational maladies such as Huntington Disease are characterized by accumulation of intracellular and extracellular protein inclusions containing amyloid-like proteins... 
NEURONAL INTRANUCLEAR INCLUSIONS | EXPANDED POLYGLUTAMINE | UBIQUITIN-PROTEASOME SYSTEM | EXPANSION PROTEINS | ALZHEIMERS-DISEASE | MULTIDISCIPLINARY SCIENCES | MUTANT HUNTINGTIN | CASPASE CLEAVAGE | BODY FORMATION | SACCHAROMYCES-CEREVISIAE | TRANSCRIPTION FACTOR | Protein Aggregates | RNA-Binding Proteins - genetics | Ribonucleases - genetics | Saccharomyces cerevisiae - genetics | Humans | Huntington Disease - pathology | Molecular Sequence Data | Amyloidogenic Proteins - chemistry | Intracellular Signaling Peptides and Proteins - metabolism | Ribonucleases - metabolism | Saccharomyces cerevisiae - metabolism | Heat-Shock Proteins - genetics | Nerve Tissue Proteins - chemistry | Peptides - metabolism | Nuclear Proteins - deficiency | Nuclear Proteins - genetics | Transgenes | Intracellular Signaling Peptides and Proteins - genetics | Protein-Serine-Threonine Kinases - metabolism | Amyloidogenic Proteins - genetics | Gene Expression Regulation, Fungal | Protein Structure, Tertiary | Amino Acid Sequence | Peptides - chemistry | Signal Transduction | Heat-Shock Proteins - metabolism | Protein-Serine-Threonine Kinases - genetics | HSP70 Heat-Shock Proteins - genetics | Saccharomyces cerevisiae Proteins - genetics | Nuclear Localization Signals | Huntington Disease - metabolism | Nerve Tissue Proteins - genetics | HSP70 Heat-Shock Proteins - metabolism | Protein Interaction Mapping | Nerve Tissue Proteins - metabolism | Huntingtin Protein | Amyloidogenic Proteins - metabolism | Models, Biological | Plasmids | Saccharomyces cerevisiae Proteins - metabolism | Huntington Disease - genetics | Protein Binding | Proteins | Proline | Heat shock proteins | Huntington's chorea | Quality control | Transcription factors | Disease | Huntingtin | Toxicity | Cytotoxicity | Biology | Agglomeration | Defense mechanisms | Nuclei | Cell cycle | Physiology | Localization | RNA processing | Trinucleotide repeat diseases | Polyglutamine | Benign | Hsp70 protein | Gene expression | Ribonucleic acid--RNA | Disease control | Suppressors | Intermediates | Prions | Intracellular | Protein interaction | Cytoplasm | RNA | Ribonucleic acid
Journal Article
PloS one, ISSN 1932-6203, 2011, Volume 6, Issue 10, p. e26319
... ATPase that collaborates with Hsp70 and Hsp40 to promote protein disaggregation and reactivation... 
YEAST | IN-VITRO | CAENORHABDITIS-ELEGANS | MOLECULAR CHAPERONES | MULTIDISCIPLINARY SCIENCES | AGGREGATED PROTEINS | ALPHA-SYNUCLEIN | SACCHAROMYCES-CEREVISIAE | HUNTINGTONS-DISEASE | HEAT-SHOCK-PROTEIN | NUCLEOTIDE EXCHANGE FACTORS | Mammals - metabolism | HSP40 Heat-Shock Proteins - metabolism | Biocatalysis | Humans | Adenosine Triphosphatases - metabolism | Rats | Substrate Specificity | HSP70 Heat-Shock Proteins - metabolism | HSP110 Heat-Shock Proteins - chemistry | Hydrolysis | Saccharomyces cerevisiae - metabolism | Cytosol - enzymology | Animals | Amyloid - metabolism | Cell-Free System | Adenosine Triphosphate - metabolism | Protein Structure, Quaternary | Saccharomyces cerevisiae Proteins - metabolism | Conserved Sequence | Protein Binding | HSP70 Heat-Shock Proteins - chemistry | HeLa Cells | HSP110 Heat-Shock Proteins - metabolism | HSP40 Heat-Shock Proteins - chemistry | Heat shock proteins | Prions | Cells | Adenosine triphosphatase | Baking yeast | Parkinson's disease | Cell-free system | Homology | Activation | Biochemistry | Kinases | Synuclein | Cytosol | Machinery | Machinery and equipment | Fungi | Protein folding | Bacteria | Amyloid | Trends | Prion protein | Movement disorders | Adenosine triphosphate | Protozoa | Neurodegenerative diseases | Disaggregation | Hsp70 protein | Hsp40 protein | Mammals | Substrates | Aggregates | Hsc70 protein | Mutation | Alzheimers disease | Endoplasmic reticulum | ATP
Journal Article
Journal of Proteome Research, ISSN 1535-3893, 04/2006, Volume 5, Issue 4, pp. 888 - 898
Regions of conserved disorder prediction (CDP) were found in protein domains from all available InterPro member databases, although with varying frequency... 
Intrinsic disorder | PONDR | Protein structure-function | Disorder prediction | UNSTRUCTURED PROTEINS | protein structure-function | CRYSTAL-STRUCTURE | SHIKIMATE KINASE | BIOCHEMICAL RESEARCH METHODS | disorder prediction | NATIVELY UNFOLDED PROTEINS | PRION PROTEIN | LARGE RIBOSOMAL-SUBUNIT | ENTEROPATHOGENIC ESCHERICHIA-COLI | ADHESION MOLECULE CD2 | intrinsic disorder | SEQUENCE COMPLEXITY | RATE HETEROGENEITY | Ribosomal Proteins - chemistry | RNA-Binding Proteins - genetics | Archaeal Proteins - chemistry | Bacterial Proteins - chemistry | Molecular Sequence Data | Structure-Activity Relationship | Viral Proteins - metabolism | Ribosomal Proteins - metabolism | DNA-Binding Proteins - metabolism | Databases, Protein | Conserved Sequence | Archaeal Proteins - genetics | Insect Proteins - metabolism | Archaeal Proteins - metabolism | Protein Structure, Tertiary | Amino Acid Sequence | Ribosomal Proteins - genetics | Viral Proteins - chemistry | RNA-Binding Proteins - chemistry | Bacterial Proteins - genetics | Insect Proteins - genetics | Viral Proteins - genetics | Plants | DNA-Binding Proteins - genetics | DNA-Binding Proteins - chemistry | Proteins - genetics | Sequence Homology, Amino Acid | Animals | Proteins - metabolism | Insect Proteins - chemistry | Bacterial Proteins - metabolism | Kinetics | Proteins - chemistry | RNA-Binding Proteins - metabolism | Evolution, Molecular
Journal Article
Protein science, ISSN 0961-8368, 2017, Volume 26, Issue 11, pp. 2126 - 2150
The role of microtubule‐associated protein Tau in neurodegeneration has been extensively investigated since the discovery of Tau amyloid aggregates in the brains of patients with Alzheimer's disease (AD... 
tauopathies | Tau protein | amyloidogenesis | Alzheimer's disease | protein aggregation | FULL-LENGTH TAU | UBIQUITIN-PROTEASOME SYSTEM | ALZHEIMERS-DISEASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | FIBRILLIZATION IN-VITRO | WILD-TYPE TAU | NEURODEGENERATIVE DISEASES | PAIRED HELICAL FILAMENTS | PROLYL ISOMERASE PIN1 | CREUTZFELDT-JAKOB-DISEASE | AMYLOID FIBRIL FORMATION | Neurons - pathology | Humans | tau Proteins - metabolism | Amyloid - ultrastructure | Prion Proteins - metabolism | tau Proteins - chemistry | Alzheimer Disease - pathology | tau Proteins - genetics | Amyloid - metabolism | Protein Aggregation, Pathological - pathology | Amyloidosis - genetics | Protein Domains | Neurons - metabolism | Prion Proteins - chemistry | Prion Proteins - genetics | Protein Aggregation, Pathological - genetics | Amyloidosis - pathology | Neurons - chemistry | Protein Structure, Secondary | Intrinsically Disordered Proteins - genetics | Amino Acid Motifs | Intrinsically Disordered Proteins - chemistry | Alzheimer Disease - metabolism | Protein Processing, Post-Translational | Alzheimer Disease - genetics | Amyloidosis - metabolism | Protein Aggregation, Pathological - metabolism | Intrinsically Disordered Proteins - metabolism | Nervous system diseases | Amyloidosis | Prions | Amyloidogenesis | Self assembly | Brain | Seeds | Peptides | Molecular structure | Agglomeration | Monomers | Proteins | Literature reviews | Fibrillogenesis | Neurodegeneration | Post-translation | Prion protein | Neurodegenerative diseases | Pathological effects | Neurological diseases | Self-assembly | Aggregates | β-Amyloid | Mutation | Alzheimers disease | Protein interaction | Reviews | Review
Journal Article