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Journal of the American Chemical Society, ISSN 0002-7863, 01/2016, Volume 138, Issue 2, pp. 527 - 539
Filamentous β-amyloid aggregates are crucial for the pathology of Alzheimer's disease. Despite the tremendous biomedical importance, the molecular pathway of... 
Thermodynamics | Peptide Fragments - chemistry | Amyloid beta-Peptides - chemistry | Molecular Dynamics Simulation | Water - chemistry | Index Medicus
Journal Article
Journal Article
Journal Article
Journal of the American Chemical Society, ISSN 0002-7863, 05/2011, Volume 133, Issue 17, pp. 6505 - 6508
A critical aspect to understanding the molecular basis of Alzheimer's disease (AD) is the characterization of the kinetics of interconversion between the... 
Peptide Fragments - chemistry | Spectrometry, Mass, Electrospray Ionization | Amyloid - chemistry | Amyloid beta-Peptides - chemistry | Humans | Alzheimer Disease - metabolism | Index Medicus
Journal Article
Journal of the American Chemical Society, ISSN 0002-7863, 01/2014, Volume 136, Issue 1, pp. 219 - 225
The aggregation of the amyloid beta peptide, Aβ42, implicated in Alzheimer's disease, is characterized by a lag phase followed by a rapid growth phase.... 
Peptide Fragments - analysis | Microscopy, Electron, Transmission | Peptide Fragments - chemistry | Models, Biological | Humans | Amyloid beta-Peptides - analysis | Biological Assay | Amyloid beta-Peptides - chemistry | Kinetics | Index Medicus
Journal Article