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2006, Advances in protein chemistry, ISBN 0120342731, Volume 73., vii, 320 p., [28] p of plates
Amyloids, Prions and Beta Proteins is the last volume of the three-part thematic series on Fibrous Proteins in the Advances in Protein Chemistry serial.... 
Proteins | Amyloid | Prions | Amyloid beta-protein
Book
PLoS ONE, ISSN 1932-6203, 2011, Volume 6, Issue 10, pp. e26319 - e26319
Bacteria, fungi, protozoa, chromista and plants all harbor homologues of Hsp104, a AAA+ ATPase that collaborates with Hsp70 and Hsp40 to promote protein... 
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 | Yeast | Parkinson's disease | Cell-free system | Homology | Activation | Biochemistry | Kinases | Synuclein | Cytosol | Machinery | 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 | Index Medicus
Journal Article
Journal of Cell Biology, ISSN 0021-9525, 2017, Volume 216, Issue 8, pp. 2295 - 2304
Disturbances in endoplasmic reticulum (ER) homeostasis create a condition termed ER stress. This activates the unfolded protein response (UPR), which alters... 
YEAST | OXIDATIVE STRESS | MOLECULAR CHAPERONES | GUANIDINE-HYDROCHLORIDE | MISFOLDED PROTEIN | MEMBRANE-PROTEIN | ENDOPLASMIC-RETICULUM | QUALITY-CONTROL | SACCHAROMYCES-CEREVISIAE | TRANSMEMBRANE PROTEIN | CELL BIOLOGY | Protein Aggregates | Basic-Leucine Zipper Transcription Factors - metabolism | Molecular Chaperones - metabolism | Membrane Glycoproteins - metabolism | Saccharomyces cerevisiae - genetics | Endoplasmic Reticulum - metabolism | Prion Proteins - metabolism | Saccharomyces cerevisiae - metabolism | Endoplasmic Reticulum - pathology | Time Factors | Proteomics - methods | Protein-Serine-Threonine Kinases - metabolism | Repressor Proteins - metabolism | Molecular Chaperones - genetics | Protein-Serine-Threonine Kinases - genetics | Ubiquitin-Protein Ligases - metabolism | Repressor Proteins - genetics | Genotype | Basic-Leucine Zipper Transcription Factors - genetics | Saccharomyces cerevisiae Proteins - genetics | Unfolded Protein Response | Protein Aggregation, Pathological | Membrane Glycoproteins - genetics | Phenotype | Endoplasmic Reticulum Stress | Saccharomyces cerevisiae Proteins - metabolism | Mutation | Ubiquitin-Protein Ligases - genetics | Cellular proteins | Stress (Physiology) | Analysis | Prions | Stresses | Homeostasis | Agglomeration | Chaperones | Gene expression | Stress | Proteins | Degradation | Correlation analysis | Protein folding | Quality control | Amyloid | Prion protein | Protein interaction | Endoplasmic reticulum | Index Medicus
Journal Article
1999, Methods in enzymology, ISBN 0121822109, Volume 309, 412, 413., 3 v.
This volume includes a core of methodologies to attack the unique experimental problems presented by protein misassembly. Emphasis is on human biology... 
Prions | Amyloid | Amyloid beta-protein | Proteins
Book
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
The EMBO Journal, ISSN 0261-4189, 10/2017, Volume 36, Issue 20, pp. 2951 - 2967
Neuronal inclusions of aggregated RNA ‐binding protein fused in sarcoma ( FUS ) are hallmarks of ALS and frontotemporal dementia subtypes. Intriguingly, FUS 's... 
frontotemporal dementia | prion | intrinsically disordered protein | ribonucleoprotein granule | amyotrophic lateral sclerosis | NEURODEGENERATIVE DISEASE | PRION-LIKE DOMAINS | BIOCHEMISTRY & MOLECULAR BIOLOGY | DISORDERED PROTEINS | AMYOTROPHIC-LATERAL-SCLEROSIS | WILD-TYPE FUS | CELL BIOLOGY | RNA-BINDING PROTEINS | CELL-FREE FORMATION | MOTOR-NEURON DEGENERATION | C-TERMINAL DOMAIN | STRESS GRANULES | RNA-Binding Protein FUS - chemistry | Cell Line | Amyotrophic Lateral Sclerosis - pathology | Phosphorylation | Magnetic Resonance Spectroscopy | Humans | Protein Conformation | Protein Processing, Post-Translational | RNA-Binding Protein FUS - metabolism | Protein Aggregation, Pathological | Frontotemporal Dementia - pathology | Cell culture | Salts | Yeast | Nuclear magnetic resonance--NMR | Self-association | Toxicity | DNA damage | Cytotoxicity | Agglomeration | Kinases | Complexity | Magnetic resonance spectroscopy | Proteins | FUS protein | Neurotoxicity | Post-translation | Dementia disorders | Deoxyribonucleic acid--DNA | Spectroscopy | Sarcoma | Therapeutic applications | Amyotrophic lateral sclerosis | Pharmacology | Ribonucleic acid--RNA | RNA-binding protein | DNA-dependent protein kinase | Phase separation | Frontotemporal dementia | Protein interaction | Index Medicus | 60 APPLIED LIFE SCIENCES | Neuroscience | Protein Biosynthesis & Quality Control
Journal Article
PLoS ONE, ISSN 1932-6203, 11/2017, Volume 12, Issue 11, pp. e0188308 - e0188308
Humic substances (HS) are the largest constituent of soil organic matter and are considered as a key component of the terrestrial ecosystem. HS may facilitate... 
SOIL PARTICLES | INFRARED-SPECTRA | ATOMIC-FORCE MICROSCOPY | ACID | NMR-SPECTROSCOPY | MULTIDISCIPLINARY SCIENCES | ORGANIC-MATTER | SECONDARY STRUCTURE | CONFORMATION | FATE | BINDING | Prion Diseases - genetics | Magnetic Resonance Spectroscopy | Protein Structure, Secondary | Chemical Precipitation | Scrapie - genetics | Recombinant Proteins - chemistry | Prion Diseases - pathology | Wasting Disease, Chronic - pathology | Zinc - chemistry | Prion Proteins - metabolism | Deer | Protein Folding | Protein Interaction Maps | Animals | Protein Aggregates - genetics | Scrapie - pathology | Soil | Sheep | Prion Proteins - chemistry | Wasting Disease, Chronic - genetics | Prion Proteins - genetics | Prion Diseases - metabolism | Humic Substances | Physiological aspects | Genetic aspects | Research | Prions | Humic acid | Self assembly | Shedding | Neurosciences | Organic matter | Scrapie | Chronic wasting disease | Terrestrial environments | Animal diseases | Environmental changes | Proteins | Case studies | Ecological effects | Soils (organic) | Protein folding | Infectivity | Spectrum analysis | Physiology | Prion protein | Adducts | Recombinant | Biodegradation | Preservation | Transmissible spongiform encephalopathy | Secondary structure | Self-assembly | Adsorption | Microscopy | Environmental degradation | Soil organic matter | Protein structure | Salting | Index Medicus
Journal Article
2010, ISBN 9780954333522, vii, 77 p. : ill. ; 28 cm.
Book
PLoS ONE, ISSN 1932-6203, 09/2017, Volume 12, Issue 9, pp. e0180905 - e0180905
Proteins associated with neurodegenerative diseases are highly pleiomorphic and may adopt an all-a-helical fold in one environment, assemble into... 
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 | Index Medicus
Journal Article