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Nature, ISSN 0028-0836, 05/2012, Volume 485, Issue 7399, pp. 507 - 511
The mechanisms leading to neuronal death in neurodegenerative disease are poorly understood. Many of these disorders, including Alzheimer's, Parkinson's and... 
UNFOLDED PROTEIN RESPONSE | TOXICITY IN-VIVO | ALZHEIMERS-DISEASE | ER STRESS | MULTIDISCIPLINARY SCIENCES | GENE-EXPRESSION | MICE | ENDOPLASMIC-RETICULUM STRESS | DYSFUNCTION | PRP | PROTEOSTASIS | Neurons - pathology | Neuroprotective Agents | Phosphorylation | Prions - genetics | Eukaryotic Initiation Factor-2 - chemistry | Neurodegenerative Diseases - etiology | PrPSc Proteins - analysis | Synapses - pathology | Thiourea - pharmacology | Phosphoproteins - metabolism | Repressor Proteins - analysis | PrPSc Proteins - metabolism | Synapses - metabolism | Phosphoproteins - analysis | Protein Folding - drug effects | Protein Phosphatase 1 - genetics | Eukaryotic Initiation Factor-2 - metabolism | Synaptic Transmission - drug effects | Cell Death - drug effects | PrPSc Proteins - toxicity | Neurons - drug effects | Repressor Proteins - metabolism | Prions - metabolism | Synapses - drug effects | Repressor Proteins - chemistry | Neurodegenerative Diseases - pathology | Mice, Inbred C57BL | Kaplan-Meier Estimate | Hippocampus - pathology | Prion Diseases - pathology | Neurodegenerative Diseases - metabolism | Hippocampus - cytology | Cinnamates - pharmacology | Eukaryotic Initiation Factor-2 - analysis | Hippocampus - metabolism | Protein Phosphatase 1 - metabolism | Animals | Prions - biosynthesis | Protein Biosynthesis - drug effects | Mice | Unfolded Protein Response - physiology | Thiourea - analogs & derivatives | Index Medicus
Journal Article
Journal Article
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
PLoS ONE, ISSN 1932-6203, 07/2013, Volume 8, Issue 7, pp. e71081 - e71081
Journal Article
Molecular Cell, ISSN 1097-2765, 2007, Volume 26, Issue 2, pp. 175 - 188
Journal Article
Journal Article