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Chemistry, ISSN 0947-6539, 06/2016, Volume 22, Issue 26, p. 8768
The aggregation of the amyloid [beta]-peptide into fibrils is a complex process that involves mechanisms such as primary and secondary nucleation, fibril... 
Oligomers | Molecular dynamics | Peptides | Alzheimer's disease | Alzheimers disease | Nucleation | Oligomerization | Neurodegenerative diseases | Fibrils | Agglomeration | Hydrophobicity | Fragmentation | Neurotoxicity | Simulation | β-Amyloid | Catalysis | Elongation
Journal Article
PLOS Computational Biology, ISSN 1553-7358, 10/2019, Volume 15, Issue 10, p. e1007193
Journal Article
Journal of Chemical Theory and Computation, ISSN 1549-9618, 09/2017, Volume 13, Issue 9, pp. 4567 - 4583
Oligomers formed by amyloid β-protein (Aβ) are central to Alzheimer’s disease (AD) pathology, yet their structure remains elusive. Of the two predominant Aβ... 
Amino Acid Sequence | Thermodynamics | Peptide Fragments - chemistry | Protein Structure, Secondary | Humans | Protein Multimerization | Water - chemistry | Models, Molecular | Protein Conformation | Amyloid beta-Peptides - chemistry | Alzheimer Disease - pathology
Journal Article
Journal of Chemical Theory and Computation, ISSN 1549-9618, 09/2017, Volume 13, Issue 9, p. 4567
Oligomers formed by amyloid β-protein (Aβ) are central to Alzheimer’s disease (AD) pathology, yet their structure remains elusive. Of the two predominant Aβ... 
Proteins | Oligomers | Ion flux | Cell death | Ion channels | Trimers | Free energy | Elongation | Pore formation
Journal Article
Chemical Communications : Chem Comm, ISSN 1359-7345, 01/2018, Volume 54, Issue 56, pp. 7766 - 7769
In light of the high affinity of Cu2+ for Alzheimer's Aβ1–42 and its ability to subsequently catalyze the formation of radicals, we examine the effects of Cu2+... 
Binding | Oligomerization | Acidic oxides | Toxicity | Transportation networks | Molecular dynamics | Oxidation | Dimers | Copper | Acidosis | Molecular chains | Index Medicus
Journal Article
Chemical Communications, ISSN 1359-7345, 05/2014, Volume 50, Issue 40, pp. 5373 - 5375
The aggregation of amyloid-beta protein (1-42) is studied at experimental concentrations using all-atom molecular dynamics simulations. We observe a fast... 
A-BETA-42 | PEPTIDES | A-BETA(1-40) | ALZHEIMERS-DISEASE | SIMULATIONS | CHEMISTRY, MULTIDISCIPLINARY | OLIGOMERS | Humans | Protein Multimerization | Models, Molecular | Protein Binding | Protein Conformation | Amyloid beta-Peptides - chemistry | Molecular Dynamics Simulation
Journal Article
The Journal of Physical Chemistry B, ISSN 1520-6106, 04/2014, Volume 118, Issue 14, pp. 3761 - 3770
Journal Article
ISSN 1359-7345, 4/2014, Volume 5, Issue 4, pp. 5373 - 5375
The aggregation of amyloid-β protein (1-42) is studied at experimental concentrations using all-atom molecular dynamics simulations. We observe a fast... 
Journal Article
Journal of Physical Chemistry A, ISSN 1089-5639, 01/2014, Volume 118, Issue 4
Journal Article
The Journal of Physical Chemistry B, ISSN 1520-6106, 01/2014, Volume 118, Issue 4, pp. 1003 - 1011
Journal Article
Proteins: Structure, Function, and Bioinformatics, ISSN 0887-3585, 10/2015, Volume 83, Issue 10, pp. 1823 - 1835
Journal Article
ISSN 1359-7345, 7/2018, Volume 54, Issue 56, pp. 7766 - 7769
In light of the high affinity of Cu 2+ for Alzheimer's Aβ 1-42 and its ability to subsequently catalyze the formation of radicals, we examine the effects of Cu... 
Journal Article
Proteins: Structure, Function, and Bioinformatics, ISSN 0887-3585, 10/2015, Volume 83, Issue 10, pp. 1823 - 1835
Journal Article
Israel Journal of Chemistry, ISSN 0021-2148, 07/2017, Volume 57, Issue 7-8, p. 771
Amyloid-[beta] (A[beta]) is a natively unfolded peptide found in all Alzheimer's disease patients as the major component of fibrillar plaques, which are... 
Molecular dynamics | Copper compounds | Histidine | Peptides | Hydrogen-ion concentration | Alzheimer's disease | Binding | Dynamic structural analysis | Residues | Strands | Lag time | Distortion | Agglomeration | Patients | Carbonyl groups | pH | Copper | Ion exchange | Acidosis | Alzheimers disease | Carbonyls
Journal Article
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