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Nature, ISSN 0028-0836, 06/2015, Volume 522, Issue 7557, pp. 478 - 481
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 6/2010, Volume 107, Issue 26, pp. 12005 - 12010
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 7/2008, Volume 105, Issue 29, pp. 10238 - 10243
Journal Article
PLOS PATHOGENS, ISSN 1553-7366, 09/2016, Volume 12, Issue 9, pp. e1005835 - e1005835
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
Journal of Clinical Investigation, ISSN 0021-9738, 12/2006, Volume 116, Issue 12, pp. 3204 - 3210
Journal Article
Journal Article