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1. Full Text An Increased Percentage of Long Amyloid β Protein Secreted by Familial Amyloid β Protein Precursor (βAPP$_{717}$) Mutants
by Nobuhiro Suzuki and Tobun T. Cheung and Xiao-Dan Cai and Asano Odaka and Laszlo Otvos and Christopher Eckman and Todd E. Golde and Steven G. Younkin
Science (American Association for the Advancement of Science), ISSN 0036-8075, 5/1994, Volume 264, Issue 5163, pp. 1336 - 1340
Proteins | Pathology | Percentages | Enzyme linked immunosorbent assay | Cell lines | Reports | Data lines | Amyloids | Sandwiches | Alzheimers disease | Genetic mutation | Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | Neurology | Biological and medical sciences | Medical sciences | Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases | Enzyme-Linked Immunosorbent Assay | Amyloid beta-Protein Precursor - chemistry | Humans | Neuroblastoma | Culture Media, Conditioned | Amyloid beta-Protein Precursor - genetics | Transfection | Amyloid beta-Peptides - metabolism | Amyloid beta-Protein Precursor - metabolism | Amyloid beta-Peptides - chemistry | Mutation | Tumor Cells, Cultured | Alzheimer Disease - genetics | Alzheimer's disease | Genetic aspects | Index Medicus
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2. Full Text Changes of the enteric nervous system in amyloid-β protein precursor transgenic mice correlate with disease progression
by Semar, Sandra and Klotz, Markus and Letiembre, Maryse and Van Ginneken, Chris and Braun, Anne and Jost, Viktor and Bischof, Michael and Lammers, Wim J and Liu, Yang and Fassbender, Klaus and Wyss-Coray, Tony and Kirchhoff, Frank and Schafer, Karl-Herbert
Journal of Alzheimer's disease, ISSN 1387-2877, 2013, Volume 36, Issue 1, pp. 7 - 20
amyloid-β protein precursor | enteric nervous system | Alzheimer's disease | potential biomarker | Neurosciences | Neurosciences & Neurology | Life Sciences & Biomedicine | Science & Technology | Enteric Nervous System - chemistry | Enteric Nervous System - pathology | Gene Expression | Mice, Inbred C57BL | Biomarkers - analysis | Mice, Transgenic | Amyloid beta-Protein Precursor - analysis | Blotting, Western | Disease Progression | Alzheimer Disease - pathology | Alzheimer Disease - diagnosis | Gastrointestinal Motility | Animals | Alzheimer Disease - metabolism | Proteomics | Mice | Real-Time Polymerase Chain Reaction | Disease Models, Animal | Index Medicus
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3. Full Text Transmission of amyloid-β protein pathology from cadaveric pituitary growth hormone
by Purro, Silvia A and Farrow, Mark A and Linehan, Jacqueline and Nazari, Tamsin and Thomas, David X and Chen, Zhicheng and Chen, Zhicheng and Mengel, David and Mengel, David and Saito, Takashi and Saito, Takashi and Saido, Takaomi and Saido, Takaomi and Rudge, Peter and Brandner, Sebastian and Brandner, Sebastian and Walsh, Dominic M and Walsh, Dominic M and Collinge, John and Collinge, John
Nature (London), ISSN 0028-0836, 12/2018, Volume 564, Issue 7736, pp. 415 - 419
Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | Alzheimer Disease - etiology | Humans | tau Proteins - metabolism | Male | Drug Contamination - prevention & control | Case-Control Studies | Disease Transmission, Infectious - prevention & control | Disease Transmission, Infectious - statistics & numerical data | Amyloid beta-Peptides - metabolism | Female | Creutzfeldt-Jakob Syndrome - chemically induced | Iatrogenic Disease | Alzheimer Disease - chemically induced | Growth Hormone - administration & dosage | Disease Models, Animal | Prions - metabolism | Reproducibility of Results | Amyloid beta-Protein Precursor - adverse effects | Growth Hormone - pharmacology | Recombinant Proteins - pharmacology | Recombinant Proteins - administration & dosage | Creutzfeldt-Jakob Syndrome - etiology | Drug Contamination - statistics & numerical data | Animals | Models, Biological | Amyloid beta-Peptides - analysis | Amyloid beta-Protein Precursor - administration & dosage | Mice | tau Proteins - analysis | Cadaver | Brain | Seeds | Peptides | Creutzfeldt-Jakob disease | Proteins | Surgery | Vials | Children | Prion protein | Alzheimer's disease | Deposition | Public health | Plaques | Neurodegenerative diseases | Medical treatment | Patients | Disease control | Amyloid precursor protein | Laboratory tests | Pathology | Hypotheses | Tau protein | Prions | Pituitary | Cadavers | Growth hormones | Growth hormone | Laboratory animals | Alzheimers disease | Index Medicus
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4. Full Text MT5-MMP is a new pro-amyloidogenic proteinase that promotes amyloid pathology and cognitive decline in a transgenic mouse model of Alzheimer’s disease
by Baranger, Kévin and Baranger, Kévin and Marchalant, Yannick and Marchalant, Yannick and Bonnet, Amandine E and Bonnet, Amandine E and Crouzin, Nadine and Crouzin, Nadine and Carrete, Alex and Carrete, Alex and Paumier, Jean-Michel and Paumier, Jean-Michel and Py, Nathalie A and Py, Nathalie A and Bernard, Anne and Bernard, Anne and Bauer, Charlotte and Bauer, Charlotte and Charrat, Eliane and Charrat, Eliane and Moschke, Katrin and Moschke, Katrin and Seiki, Mothoharu and Seiki, Mothoharu and Vignes, Michel and Vignes, Michel and Lichtenthaler, Stefan F and Lichtenthaler, Stefan F and Checler, Frédéric and Checler, Frédéric and Khrestchatisky, Michel and Khrestchatisky, Michel and Rivera, Santiago and Rivera, Santiago
Cellular and molecular life sciences : CMLS, ISSN 1420-682X, 1/2016, Volume 73, Issue 1, pp. 217 - 236
Life Sciences | Biochemistry, general | Neuroprotection | Life Sciences, general | Synaptotoxicity | Knockout mouse | MMP-24 | Neurodegenerative disease | Biomedicine general | Cell Biology | Biochemistry & Molecular Biology | Life Sciences & Biomedicine | Science & Technology | Humans | Matrix Metalloproteinases, Membrane-Associated - analysis | Male | Amyloid beta-Protein Precursor - analysis | Cognition | Alzheimer Disease - pathology | Spatial Learning | Gene Deletion | Amyloid beta-Peptides - metabolism | Amyloid beta-Protein Precursor - metabolism | HEK293 Cells | Female | Hippocampus - enzymology | Alzheimer Disease - physiopathology | Mice, Inbred C57BL | Mice, Transgenic | Amyloid Precursor Protein Secretases - analysis | Hippocampus - pathology | Alzheimer Disease - enzymology | Matrix Metalloproteinases, Membrane-Associated - genetics | Hippocampus - metabolism | Amyloid Precursor Protein Secretases - metabolism | Animals | Long-Term Potentiation | Amyloid beta-Peptides - analysis | Alzheimer Disease - genetics | Matrix Metalloproteinases, Membrane-Associated - metabolism | Hippocampus - physiopathology | Analysis | Amyloid beta-protein | Genetically modified organisms | Resveratrol | Genetic engineering | Amyloidosis | Alzheimer's disease | Proteins | Nervous system | Membranes | Peptides | Alzheimers disease | Index Medicus | Neurons and Cognition | Alzheimer Disease | Matrix Metalloproteinases, Membrane-Associated | Amyloid Precursor Protein Secretases | Amyloid beta-Peptides | Amyloid beta-Protein Precursor | Hippocampus
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5. Full Text The Amyloid Precursor Protein Has a Flexible Transmembrane Domain and Binds Cholesterol
by Paul J. Barrett and Yuanli Song and Wade D. Van Horn and Eric J. Hustedt and Johanna M. Schafer and Arina Hadziselimovic and Andrew J. Beel and Charles R. Sanders
Science (American Association for the Advancement of Science), ISSN 0036-8075, 6/2012, Volume 336, Issue 6085, pp. 1168 - 1171
Micelles | REPORTS | Lipids | Protein precursors | Titration | Biochemistry | Nuclear magnetic resonance | Amyloids | Cholesterols | Curvature | Binding sites | Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | Fundamental and applied biological sciences. Psychology | Organic mental disorders. Neuropsychology | Intermolecular phenomena | Psychology. Psychoanalysis. Psychiatry | Interactions. Associations | Adult and adolescent clinical studies | Molecular biophysics | Psychopathology. Psychiatry | Biological and medical sciences | Medical sciences | Protein Structure, Tertiary | Amino Acid Sequence | Peptide Fragments - metabolism | Electron Spin Resonance Spectroscopy | Protein Structure, Secondary | Amyloid beta-Protein Precursor - chemistry | Humans | Molecular Sequence Data | Cholesterol - metabolism | Amino Acid Motifs | Peptide Fragments - chemistry | Amyloid beta-Protein Precursor - genetics | Amyloid beta-Protein Precursor - metabolism | Nuclear Magnetic Resonance, Biomolecular | Protein Binding | Mutation | Binding Sites | Peptide Fragments - genetics | Amyloid beta-protein | Physiological aspects | Development and progression | Health aspects | Alzheimer's disease | Cholesterol | Membrane proteins | Proteins | Membranes | Index Medicus | Precursors | Cleavage | Electron paramagnetic resonance
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6. Full Text Central and peripheral administration of antisense oligonucleotide targeting amyloid-β protein precursor improves learning and memory and reduces neuroinflammatory cytokines in Tg2576 (AβPPswe) mice
by Farr, Susan A and Erickson, Michelle A and Niehoff, Michael L and Banks, William A and Morley, John E
Journal of Alzheimer's disease, ISSN 1387-2877, 2014, Volume 40, Issue 4, pp. 1005 - 1016
blood brain barrier | object recognition | memory | cytokines | learning | Antisense oligonucleotide | T-maze | oxidative stress | Tg2576 | Neurosciences | Neurosciences & Neurology | Life Sciences & Biomedicine | Science & Technology | Drug Administration Routes | Cytokines - metabolism | Memory Disorders - genetics | Gene Expression Regulation - genetics | Amyloid beta-Protein Precursor - chemistry | Humans | Oligoribonucleotides, Antisense - administration & dosage | Learning Disorders - drug therapy | Male | Mice, Transgenic | Maze Learning - drug effects | Gene Expression Regulation - drug effects | Amyloid beta-Protein Precursor - genetics | Animals | Memory Disorders - drug therapy | Analysis of Variance | Amyloid beta-Peptides - metabolism | Amyloid beta-Protein Precursor - metabolism | Exploratory Behavior - drug effects | Learning Disorders - genetics | Mice | Oxidative Stress - drug effects | Disease Models, Animal | Index Medicus
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7. Full Text Familial Alzheimer's disease mutations within the amyloid precursor protein alter the aggregation and conformation of the amyloid-β peptide
by Hatami, Asa and Monjazeb, Sanaz and Milton, Saskia and Glabe, Charles G
The Journal of biological chemistry, ISSN 0021-9258, 02/2017, Volume 292, Issue 8, pp. 3172 - 3185
Life Sciences & Biomedicine | Biochemistry & Molecular Biology | Science & Technology | Protein Aggregates | Amyloid beta-Protein Precursor - ultrastructure | Amyloid beta-Protein Precursor - genetics | Amyloid beta-Peptides - genetics | Amyloid beta-Peptides - ultrastructure | Humans | Amyloid beta-Peptides - analysis | Protein Conformation | Amyloid beta-Protein Precursor - analysis | Mutation | Alzheimer Disease - genetics | Alzheimer Disease - pathology | Index Medicus | Protein Structure and Folding | aggregation | amyloid-β (Aβ) | monoclonal antibody | peptide conformation | Alzheimer disease
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8. Full Text Insights into the physiological function of the β‐amyloid precursor protein: beyond Alzheimer's disease
by Dawkins, Edgar and Small, David H
Journal of neurochemistry, ISSN 0022-3042, 06/2014, Volume 129, Issue 5, pp. 756 - 769
growth factor | heparin | neurotrophic | receptor | amyloid precursor protein | Alzheimer's disease | Biochemistry & Molecular Biology | Neurosciences | Neurosciences & Neurology | Life Sciences & Biomedicine | Science & Technology | Amyloid beta-Protein Precursor - genetics | Animals | Cell Proliferation | Humans | Alzheimer Disease - metabolism | Neural Stem Cells - physiology | Mice | Amyloid beta-Protein Precursor - physiology | Cell Differentiation - physiology | Promoter Regions, Genetic - genetics | Amyloid beta-Protein Precursor - pharmacology | Index Medicus | Review
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