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Annual Review of Biochemistry, ISSN 0066-4154, 6/2016, Volume 85, Issue 1, pp. 715 - 742
Molecular chaperones control the cellular folding, assembly, unfolding, disassembly, translocation, activation, inactivation, disaggregation, and degradation... 
Hsp70 | Hsp60 | unfoldases | Hsp104 | sHsps | protein homeostasis | heat-shock proteins | Hsp110 | small heat-shock proteins | Heat-shock proteins | Small heat-shock proteins | SHsps | Unfoldases | Protein homeostasis | BACTERIOPHAGE-LAMBDA | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | SUBUNIT BINDING-PROTEIN | ALPHA-B-CRYSTALLIN | QUALITY-CONTROL | RIBULOSEBISPHOSPHATE-CARBOXYLASE | HEAT-SHOCK-PROTEIN | ATP HYDROLYSIS | LAMBDA-DNA-REPLICATION | RIBULOSE-BISPHOSPHATE CARBOXYLASE | Protein Aggregates | Rhodospirillum rubrum - metabolism | Protein Unfolding | Humans | Mitochondrial Proteins - genetics | HSP110 Heat-Shock Proteins - chemistry | Mitochondrial Proteins - metabolism | Adenosine Triphosphate - metabolism | Escherichia coli - metabolism | Protein Structure, Quaternary | Chaperonin 60 - metabolism | HSP70 Heat-Shock Proteins - chemistry | Rhodospirillum rubrum - chemistry | Chaperonin 60 - chemistry | Chaperonin 60 - genetics | Gene Expression | Heat-Shock Proteins, Small - chemistry | Heat-Shock Proteins, Small - metabolism | Models, Molecular | HSP70 Heat-Shock Proteins - genetics | Escherichia coli - chemistry | Protein Folding | HSP70 Heat-Shock Proteins - metabolism | HSP110 Heat-Shock Proteins - genetics | Heat-Shock Proteins, Small - genetics | Mitochondrial Proteins - chemistry | Adenosine Triphosphate - chemistry | HSP110 Heat-Shock Proteins - metabolism | Molecular chaperones | Observations | Protein folding | Health aspects
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... 
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 | Spatial discrimination | 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, 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... 
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
PLoS ONE, ISSN 1932-6203, 2011, Volume 6, Issue 10, p. 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 | 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
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 9/2014, Volume 111, Issue 39, pp. 14141 - 14146
Journal Article