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Journal of the American Chemical Society, ISSN 0002-7863, 11/2017, Volume 139, Issue 43, pp. 15437 - 15445
Regulation of amyloid-beta (A beta) aggregation by metal ions and proteins is essential for understanding the pathology of Alzheimer's disease (AD). Human... 
PLASMA-EXCHANGE | IN-VITRO | PROTEIN AGGREGATION | A-BETA-PEPTIDE | MECHANISTIC INSIGHTS | PARTIALLY FOLDED STRUCTURE | MOBILITY-MASS SPECTROMETRY | MODERATE ALZHEIMERS-DISEASE | METAL-IONS | CHEMISTRY, MULTIDISCIPLINARY | SENILE PLAQUES | Chemical reactions | Usage | Serum albumin | Research | Protein-protein interactions | Metal ions | Index Medicus
Journal Article
Coordination Chemistry Reviews, ISSN 0010-8545, 11/2017, Volume 351, pp. 127 - 159
Journal Article
Physical Chemistry Chemical Physics, ISSN 1463-9076, 2017, Volume 19, Issue 40, pp. 27556 - 27569
Alzheimer's disease, a common neurodegenerative disease, is characterized by the aggregation of amyloid-beta (A beta) peptides. The interactions of A beta with... 
1-40 PEPTIDE | ALZHEIMERS-DISEASE BRAIN | AMYLOID ION CHANNELS | EXPERIMENTAL CONSTRAINTS | PROTEIN | FIBRILS | SOLID-STATE NMR | PARTIALLY FOLDED STRUCTURE | PHYSICS, ATOMIC, MOLECULAR & CHEMICAL | CHEMISTRY, PHYSICAL | FORCE-FIELD | MOLECULAR-DYNAMICS SIMULATIONS
Journal Article
PHYSICAL CHEMISTRY CHEMICAL PHYSICS, ISSN 1463-9076, 07/2016, Volume 18, Issue 25, pp. 16890 - 16901
The aggregation of amyloid-b (Ab) on neuronal membranes is implicated in both neuronal toxicity and the progression of Alzheimer's disease. Unfortunately, the... 
NMR | LIPID-BILAYERS | FIBRILS | PARTIALLY FOLDED STRUCTURE | CONFORMATIONAL TRANSITION | PHYSICS, ATOMIC, MOLECULAR & CHEMICAL | A-BETA | RANDOM COIL | CHEMISTRY, PHYSICAL | BETA-PEPTIDE | MOLECULAR-DYNAMICS SIMULATIONS | GANGLIOSIDE CLUSTERS
Journal Article
Journal of Molecular Biology, ISSN 0022-2836, 10/2018, Volume 430, Issue 21, pp. 4230 - 4244
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
Chemistry Letters, ISSN 0366-7022, 7/2017, Volume 46, Issue 7, pp. 979 - 982
Helical intermediates play important roles in the aggregation process of amyloid proteins. Herein, constrained helices were synthesized to mimic different... 
Aβ aggregation | Amyloid β (Aβ) | Helical intermediate | A beta aggregation | DESIGN | PROTEIN | AMYLOID FORMATION | MECHANISM | ALZHEIMERS-DISEASE | PARTIALLY FOLDED STRUCTURE | STATE | HYDROGEN-BOND SURROGATE | CHEMISTRY, MULTIDISCIPLINARY | PEPTIDE | INTERMEDIATE | Amyloid beta (A beta)
Journal Article