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Nature, ISSN 0028-0836, 08/2012, Volume 488, Issue 7409, pp. 96 - 99
Journal Article
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Journal of Clinical Investigation, ISSN 0021-9738, 01/2013, Volume 123, Issue 1, pp. 224 - 235
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Nature, ISSN 0028-0836, 02/2012, Volume 482, Issue 7384, pp. 216 - U107
Our understanding of Alzheimer's disease pathogenesis is currently limited by difficulties in obtaining live neurons from patients and the inability to model... 
AMYLOID BETA-PROTEIN | APP | MICROTUBULE-BINDING | PHOSPHORYLATION | MULTIDISCIPLINARY SCIENCES | DOWN-SYNDROME | MOUSE MODEL | TAU | DYSFUNCTION | FIBROBLASTS | SENILE PLAQUES | Neurons - pathology | Coculture Techniques | Humans | Middle Aged | Amyloid beta-Peptides - secretion | tau Proteins - metabolism | Male | Phosphoproteins - metabolism | Endosomes - metabolism | Synapsins - metabolism | Alzheimer Disease - pathology | Cellular Reprogramming | Protease Inhibitors - pharmacology | Amyloid beta-Protein Precursor - secretion | Proteolysis | Amyloid beta-Peptides - metabolism | Amyloid beta-Protein Precursor - metabolism | Aged, 80 and over | Female | Neurons - metabolism | Phosphorylation - drug effects | Neurons - drug effects | Fibroblasts - metabolism | Induced Pluripotent Stem Cells - metabolism | Astrocytes - cytology | Biomarkers - metabolism | Induced Pluripotent Stem Cells - pathology | Peptide Fragments - metabolism | Cells, Cultured | Peptide Fragments - secretion | Glycogen Synthase Kinase 3 - metabolism | Amyloid Precursor Protein Secretases - metabolism | Amyloid beta-Protein Precursor - genetics | Models, Biological | Alzheimer Disease - metabolism | Fibroblasts - cytology | Amyloid Precursor Protein Secretases - antagonists & inhibitors | Enzyme Activation | Messenger RNA | Synthesis | Glycogen | Stem cells | Physiological aspects | Research | Alzheimer's disease | Proteins | Phosphorylation | Neurons | Efficiency | Genomes | Mutation | Alzheimers disease | Index Medicus
Journal Article
Journal Article
Biochemical and Biophysical Research Communications, ISSN 0006-291X, 04/2017, Volume 486, Issue 2, pp. 321 - 328
Mitochondrial dysfunction is implicated in the pathological mechanism of Alzheimer's disease (AD). Amyloid β-protein (Aβ), which plays a central role in AD... 
BACE1 | Mitochondria | Subcellular fractionation | Amyloid β-protein | γ-secretase | Alzheimer's disease | PRESENILIN | OXIDATIVE STRESS | BIOCHEMISTRY & MOLECULAR BIOLOGY | Amyloid beta-protein | gamma-secretase | PEPTIDE | DAMAGE | ALZHEIMERS-DISEASE IMPLICATIONS | IMPORT | BIOPHYSICS | REGIONS | DYSFUNCTION | ACCUMULATION | BRAIN | Amyloid Precursor Protein Secretases - genetics | Cell Fractionation | Lysosomes - chemistry | Membrane Glycoproteins - metabolism | Peptide Hydrolases - genetics | ADAM10 Protein - genetics | Humans | ADAM10 Protein - metabolism | Aspartic Acid Endopeptidases - genetics | Lysosomes - metabolism | Membrane Transport Proteins - genetics | Amyloid beta-Protein Precursor - metabolism | Membrane Transport Proteins - metabolism | Membrane Proteins - metabolism | Neurons - metabolism | Mitochondria - chemistry | Peptide Hydrolases - metabolism | Centrifugation, Density Gradient | Neurons - chemistry | Signal Transduction | Membrane Proteins - genetics | Gene Expression Regulation | Presenilin-1 - genetics | Receptors, Cell Surface - metabolism | Mitochondria - metabolism | Cathepsin D - metabolism | Membrane Glycoproteins - genetics | Amyloid Precursor Protein Secretases - metabolism | Amyloid beta-Protein Precursor - genetics | Aspartic Acid Endopeptidases - metabolism | Presenilin-1 - metabolism | Cathepsin D - genetics | Cell Line, Tumor | Receptors, Cell Surface - genetics | Index Medicus
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