Redox Biology, ISSN 2213-2317, 04/2018, Volume 14, pp. 450 - 464
Oxidative stress is known to play an important role in the pathogenesis of a number of diseases. In particular, it is linked to the etiology of Alzheimer's...
Oxidative stress | Reactive oxygen species | Amyloid beta peptide | Metal-ions | Oxidative damages | CU(II) BINDING-SITES | LIPID-PEROXIDATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | MILD COGNITIVE IMPAIRMENT | METAL-CATALYZED OXIDATION | NEURODEGENERATIVE DISEASES | A-BETA | AMINO-ACID-RESIDUES | PRECURSOR PROTEIN | REDOX PROTEOMICS IDENTIFICATION | RECEPTOR-RELATED PROTEIN-1
Oxidative stress | Reactive oxygen species | Amyloid beta peptide | Metal-ions | Oxidative damages | CU(II) BINDING-SITES | LIPID-PEROXIDATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | MILD COGNITIVE IMPAIRMENT | METAL-CATALYZED OXIDATION | NEURODEGENERATIVE DISEASES | A-BETA | AMINO-ACID-RESIDUES | PRECURSOR PROTEIN | REDOX PROTEOMICS IDENTIFICATION | RECEPTOR-RELATED PROTEIN-1
Journal Article
JOURNAL OF ALZHEIMERS DISEASE, ISSN 1387-2877, 2010, Volume 19, Issue 1, pp. 311 - 323
Alzheimer's disease (AD) pathogenesis is widely believed to be driven by the production and deposition of the amyloid-beta peptide (A beta). For many years,...
INSULIN-DEGRADING ENZYME | oligomer | amyloid-beta protein precursor | BLOOD-BRAIN-BARRIER | NEUROSCIENCES | PITTSBURGH COMPOUND-B | PLAQUE CORE PROTEIN | SENILE PLAQUES | APP TRANSGENIC MICE | fibril | POSITRON-EMISSION-TOMOGRAPHY | A-BETA | GAMMA-SECRETASE ACTIVITY | PRECURSOR PROTEIN | Amyloid-beta
INSULIN-DEGRADING ENZYME | oligomer | amyloid-beta protein precursor | BLOOD-BRAIN-BARRIER | NEUROSCIENCES | PITTSBURGH COMPOUND-B | PLAQUE CORE PROTEIN | SENILE PLAQUES | APP TRANSGENIC MICE | fibril | POSITRON-EMISSION-TOMOGRAPHY | A-BETA | GAMMA-SECRETASE ACTIVITY | PRECURSOR PROTEIN | Amyloid-beta
Journal Article
SCIENTIFIC REPORTS, ISSN 2045-2322, 04/2019, Volume 9, Issue 1, pp. 5476 - 7
The aggregation of insoluble amyloid beta (A beta) peptides in the brain is known to trigger the onset of neurodegenerative diseases, such as Alzheimer's...
FIBRIL STRUCTURE | PROTEIN | ATOMIC-RESOLUTION STRUCTURE | ALZHEIMERS-DISEASE | MULTIDISCIPLINARY SCIENCES | DYNAMICS | SIMULATIONS | β-Amyloid | Oxidation | Peptides | Neurodegenerative diseases | Free energy
FIBRIL STRUCTURE | PROTEIN | ATOMIC-RESOLUTION STRUCTURE | ALZHEIMERS-DISEASE | MULTIDISCIPLINARY SCIENCES | DYNAMICS | SIMULATIONS | β-Amyloid | Oxidation | Peptides | Neurodegenerative diseases | Free energy
Journal Article
Journal of the American Chemical Society, ISSN 0002-7863, 07/2017, Volume 139, Issue 28, pp. 9566 - 9575
Previously published experimental studies have suggested that when the 40-residue amyloid beta peptide is encapsulated in a reverse micelle, it folds into a...
FIBRIL FORMATION | PROTEIN | AMIDE-I | ALZHEIMERS-DISEASE | SHEET STRUCTURE | AB-INITIO | MEMBRANES | INFRARED-SPECTROSCOPY | MOLECULAR-DYNAMICS SIMULATIONS | CHEMISTRY, MULTIDISCIPLINARY | AGGREGATION | Software | Amyloid beta-Peptides - chemistry | Micelles | Molecular Dynamics Simulation | Protein Folding | Chemical properties | Research | Structure | Protein folding | Amyloid beta-protein
FIBRIL FORMATION | PROTEIN | AMIDE-I | ALZHEIMERS-DISEASE | SHEET STRUCTURE | AB-INITIO | MEMBRANES | INFRARED-SPECTROSCOPY | MOLECULAR-DYNAMICS SIMULATIONS | CHEMISTRY, MULTIDISCIPLINARY | AGGREGATION | Software | Amyloid beta-Peptides - chemistry | Micelles | Molecular Dynamics Simulation | Protein Folding | Chemical properties | Research | Structure | Protein folding | Amyloid beta-protein
Journal Article
Journal of Alzheimer's Disease, ISSN 1387-2877, 2010, Volume 19, Issue 1, pp. 311 - 323
Alzheimer's disease (AD) pathogenesis is widely believed to be driven by the production and deposition of the amyloid-beta peptide (Abeta). For many years,...
Amyloid-β protein precursor | Amyloid-β | Oligomer | Fibril | Peptide Fragments - metabolism | Amyloid beta-Peptides - biosynthesis | Humans | Peptide Fragments - biosynthesis | Alzheimer Disease - pathology | Polymorphism, Genetic | Brain - metabolism | Animals | Amyloid beta-Peptides - genetics | Alzheimer Disease - metabolism | Amyloid beta-Peptides - metabolism | Brain - pathology | Protein Conformation | Alzheimer Disease - genetics | Peptide Fragments - genetics
Amyloid-β protein precursor | Amyloid-β | Oligomer | Fibril | Peptide Fragments - metabolism | Amyloid beta-Peptides - biosynthesis | Humans | Peptide Fragments - biosynthesis | Alzheimer Disease - pathology | Polymorphism, Genetic | Brain - metabolism | Animals | Amyloid beta-Peptides - genetics | Alzheimer Disease - metabolism | Amyloid beta-Peptides - metabolism | Brain - pathology | Protein Conformation | Alzheimer Disease - genetics | Peptide Fragments - genetics
Journal Article
Science Translational Medicine, ISSN 1946-6234, 06/2011, Volume 3, Issue 89, pp. 89ra57 - 89ra57
The apolipoprotein E (APOE) epsilon 4 allele is the strongest genetic risk factor for late-onset, sporadic Alzheimer's disease (AD). The APOE epsilon 4 allele...
FIBRIL FORMATION | MEDICINE, RESEARCH & EXPERIMENTAL | MOUSE MODEL | IN-VIVO | A-BETA | ONSET ALZHEIMER-DISEASE | CENTRAL-NERVOUS-SYSTEM | CEREBROSPINAL-FLUID A-BETA | PITTSBURGH COMPOUND-B | DENSITY-LIPOPROTEIN RECEPTOR | APOLIPOPROTEIN-E | CELL BIOLOGY | Apolipoprotein E4 - genetics | Apolipoprotein E4 - metabolism | Humans | Mice, Inbred C57BL | Middle Aged | Genotype | Male | Mice, Transgenic | Alzheimer Disease - pathology | Brain - metabolism | Animals | Microdialysis | Protein Isoforms - metabolism | Alleles | Alzheimer Disease - metabolism | Amyloid beta-Peptides - cerebrospinal fluid | Brain - pathology | Adult | Female | Aged | Mice | Biomarkers - cerebrospinal fluid | Alzheimer Disease - genetics | Protein Isoforms - genetics
FIBRIL FORMATION | MEDICINE, RESEARCH & EXPERIMENTAL | MOUSE MODEL | IN-VIVO | A-BETA | ONSET ALZHEIMER-DISEASE | CENTRAL-NERVOUS-SYSTEM | CEREBROSPINAL-FLUID A-BETA | PITTSBURGH COMPOUND-B | DENSITY-LIPOPROTEIN RECEPTOR | APOLIPOPROTEIN-E | CELL BIOLOGY | Apolipoprotein E4 - genetics | Apolipoprotein E4 - metabolism | Humans | Mice, Inbred C57BL | Middle Aged | Genotype | Male | Mice, Transgenic | Alzheimer Disease - pathology | Brain - metabolism | Animals | Microdialysis | Protein Isoforms - metabolism | Alleles | Alzheimer Disease - metabolism | Amyloid beta-Peptides - cerebrospinal fluid | Brain - pathology | Adult | Female | Aged | Mice | Biomarkers - cerebrospinal fluid | Alzheimer Disease - genetics | Protein Isoforms - genetics
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 12/2009, Volume 106, Issue 48, pp. 20324 - 20329
One of the neuropathological hallmarks of Alzheimer's disease (AD) is the amyloid plaque, primarily composed of aggregated amyloid-beta (Aβ) peptide. In vitro,...
Aggregation | Brain | Mental concentration | HEK293 cells | Neurons | Cell aggregates | Fluorescence | Amyloids | Alzheimers disease | Cell extracts | Lysosomes | Amyloid fibrils | Late endosomes | Plaques | FIBRIL FORMATION | HUMAN BRAIN | PROTEIN AGGREGATION | plaques | ALZHEIMERS-DISEASE | DEPOSITION | MULTIDISCIPLINARY SCIENCES | INTERSTITIAL FLUID | INTRANEURONAL A-BETA-42 ACCUMULATION | APOLIPOPROTEIN-E | late endosomes | amyloid fibrils | IN-VITRO MODEL | A-BETA | lysosomes | Alzheimer Disease - physiopathology | Humans | Immunoblotting | Microscopy, Confocal | Animals | Amyloid beta-Peptides - metabolism | Cytoplasmic Vesicles - metabolism | Thiazoles | Cell Line, Tumor | Plaque, Amyloid - metabolism | Mice | Neurons - metabolism | Amyloid beta-Peptides - pharmacokinetics | Properties | Amyloid beta-protein | Biological Sciences
Aggregation | Brain | Mental concentration | HEK293 cells | Neurons | Cell aggregates | Fluorescence | Amyloids | Alzheimers disease | Cell extracts | Lysosomes | Amyloid fibrils | Late endosomes | Plaques | FIBRIL FORMATION | HUMAN BRAIN | PROTEIN AGGREGATION | plaques | ALZHEIMERS-DISEASE | DEPOSITION | MULTIDISCIPLINARY SCIENCES | INTERSTITIAL FLUID | INTRANEURONAL A-BETA-42 ACCUMULATION | APOLIPOPROTEIN-E | late endosomes | amyloid fibrils | IN-VITRO MODEL | A-BETA | lysosomes | Alzheimer Disease - physiopathology | Humans | Immunoblotting | Microscopy, Confocal | Animals | Amyloid beta-Peptides - metabolism | Cytoplasmic Vesicles - metabolism | Thiazoles | Cell Line, Tumor | Plaque, Amyloid - metabolism | Mice | Neurons - metabolism | Amyloid beta-Peptides - pharmacokinetics | Properties | Amyloid beta-protein | Biological Sciences
Journal Article
8.
Full Text
The amyloid beta peptide: A chemist's perspective. role in Alzheimer's and fibrillization
Chemical Reviews, ISSN 0009-2665, 10/2012, Volume 112, Issue 10, pp. 5147 - 5192
GAMMA-SECRETASE INHIBITOR | SELF-ASSEMBLED MONOLAYERS | ATOMIC-FORCE MICROSCOPY | SOLID-STATE NMR | PROTEIN TRANSGENIC MICE | X-RAY-DIFFRACTION | LONG-TERM POTENTIATION | NICOTINIC ACETYLCHOLINE-RECEPTORS | MILD COGNITIVE IMPAIRMENT | BLOOD-BRAIN-BARRIER | CHEMISTRY, MULTIDISCIPLINARY | Amino Acid Sequence | Humans | Alzheimer Disease - drug therapy | Models, Molecular | Molecular Sequence Data | Animals | Amyloid beta-Peptides - genetics | Amyloid beta-Peptides - ultrastructure | Alzheimer Disease - metabolism | Amyloid beta-Peptides - metabolism | Protein Conformation | Amyloid beta-Peptides - chemistry | Mutation | Alzheimer Disease - genetics | Care and treatment | Usage | Magnetic resonance imaging | Peptides | Mitochondrial DNA | Genetic aspects | Diagnosis | Chemical properties | Structure | Alzheimer's disease
Journal Article
Autoimmunity Reviews, ISSN 1568-9972, 2008, Volume 7, Issue 6, pp. 415 - 420
Abstract Properties of human, natural anti-Aβ antibodies and commercially available intravenous immunoglobulin (IVIg) have been examined in light of the...
Allergy and Immunology | Avidity | Neurotoxicity | Aβ peptide | Antibody “masking” | Natural anti-Aβ antibodies | Antibody "masking" | PROTEIN | ALZHEIMERS-DISEASE | PATHOLOGY | IMMUNOLOGY | MEMORY LOSS | avidity | PATHOGENESIS | antibody "masking" | IMMUNIZATION | neurotoxicity | MOUSE MODEL | A-BETA | natural anti-A beta antibodies | A beta peptide | Antibody Specificity | Immunoglobulin G - blood | Autoantibodies - blood | Humans | Peptides - immunology | Alzheimer Disease - drug therapy | Amyloid beta-Peptides - antagonists & inhibitors | Autoantibodies - immunology | Immunoglobulin M - blood | Immunoglobulins, Intravenous - therapeutic use | Autoantibodies - therapeutic use | Amyloid beta-Peptides - immunology | Epitopes - chemistry | Immunoglobulins, Intravenous - immunology | Peptides | Immunoglobulins | Index Medicus
Allergy and Immunology | Avidity | Neurotoxicity | Aβ peptide | Antibody “masking” | Natural anti-Aβ antibodies | Antibody "masking" | PROTEIN | ALZHEIMERS-DISEASE | PATHOLOGY | IMMUNOLOGY | MEMORY LOSS | avidity | PATHOGENESIS | antibody "masking" | IMMUNIZATION | neurotoxicity | MOUSE MODEL | A-BETA | natural anti-A beta antibodies | A beta peptide | Antibody Specificity | Immunoglobulin G - blood | Autoantibodies - blood | Humans | Peptides - immunology | Alzheimer Disease - drug therapy | Amyloid beta-Peptides - antagonists & inhibitors | Autoantibodies - immunology | Immunoglobulin M - blood | Immunoglobulins, Intravenous - therapeutic use | Autoantibodies - therapeutic use | Amyloid beta-Peptides - immunology | Epitopes - chemistry | Immunoglobulins, Intravenous - immunology | Peptides | Immunoglobulins | Index Medicus
Journal Article
Science Translational Medicine, ISSN 1946-6234, 05/2016, Volume 8, Issue 340, p. 340ra72
The amyloid-beta peptide (A beta) is a key protein in Alzheimer's disease (AD) pathology. We previously reported in vitro evidence suggesting that A beta is an...
MEDICINE, RESEARCH & EXPERIMENTAL | CELLS | CAENORHABDITIS-ELEGANS | A-BETA(1-42) | ANTIMICROBIAL PEPTIDE | PRECURSOR PROTEIN | MUTATIONS | EXPRESSION | BINDING | BRAIN | BALB/C MICE | CELL BIOLOGY | Alzheimer Disease - microbiology | Amyloid beta-Peptides - physiology | Caenorhabditis elegans - microbiology | Caenorhabditis elegans - metabolism | Salmonella typhimurium - pathogenicity | Animals, Genetically Modified | Caenorhabditis elegans - genetics | Humans | Immunity, Innate - genetics | Mice, Transgenic | Animals | Amyloid beta-Peptides - genetics | Immunity, Innate - physiology | Alzheimer Disease - metabolism | Female | Mice | Alzheimer Disease - genetics | Disease Models, Animal
MEDICINE, RESEARCH & EXPERIMENTAL | CELLS | CAENORHABDITIS-ELEGANS | A-BETA(1-42) | ANTIMICROBIAL PEPTIDE | PRECURSOR PROTEIN | MUTATIONS | EXPRESSION | BINDING | BRAIN | BALB/C MICE | CELL BIOLOGY | Alzheimer Disease - microbiology | Amyloid beta-Peptides - physiology | Caenorhabditis elegans - microbiology | Caenorhabditis elegans - metabolism | Salmonella typhimurium - pathogenicity | Animals, Genetically Modified | Caenorhabditis elegans - genetics | Humans | Immunity, Innate - genetics | Mice, Transgenic | Animals | Amyloid beta-Peptides - genetics | Immunity, Innate - physiology | Alzheimer Disease - metabolism | Female | Mice | Alzheimer Disease - genetics | Disease Models, Animal
Journal Article
CHEMISTRY-A EUROPEAN JOURNAL, ISSN 0947-6539, 04/2018, Volume 24, Issue 24, pp. 6349 - 6353
Although fibrillar amyloid beta peptide (A) aggregates are one of the major hallmarks of Alzheimer's disease, increasing evidence suggests that soluble A...
CELLS | therapeutics | ALZHEIMERS-DISEASE | neurodegeneration | ALPHA-SYNUCLEIN | ANTIOXIDANT MODULATORS | CHEMISTRY, MULTIDISCIPLINARY | OLIGOMERS | aggregate | amyloid | LIGANDS | INHIBITORS | zinc | DERIVATIVES
CELLS | therapeutics | ALZHEIMERS-DISEASE | neurodegeneration | ALPHA-SYNUCLEIN | ANTIOXIDANT MODULATORS | CHEMISTRY, MULTIDISCIPLINARY | OLIGOMERS | aggregate | amyloid | LIGANDS | INHIBITORS | zinc | DERIVATIVES
Journal Article
BBA - Bioenergetics, ISSN 0005-2728, 07/2014, Volume 1837, Issue 7, pp. 1069 - 1074
Mitochondrial dysfunctions associated with amyloid-β peptide (Aβ) accumulation in mitochondria have been observed in Alzheimer's disease (AD) patients' brains...
Degradation | MAM | Presequence protease | Mitochondria | Amyloid-β peptide | PreP | INSULIN-DEGRADING ENZYME | BIOCHEMISTRY & MOLECULAR BIOLOGY | ALZHEIMERS-DISEASE NEURONS | BIOPHYSICS | MEMORY | Amyloid-beta peptide | MOUSE MODEL | A-BETA | ENDOPLASMIC-RETICULUM | PRECURSOR PROTEIN | DYSFUNCTION | ABNORMAL INTERACTION | TRANSGENIC MICE | Index Medicus | Biological Sciences | Biofysik | Biophysics | Naturvetenskap | Biokemi och molekylärbiologi | Biologiska vetenskaper | Biochemistry and Molecular Biology | Natural Sciences
Degradation | MAM | Presequence protease | Mitochondria | Amyloid-β peptide | PreP | INSULIN-DEGRADING ENZYME | BIOCHEMISTRY & MOLECULAR BIOLOGY | ALZHEIMERS-DISEASE NEURONS | BIOPHYSICS | MEMORY | Amyloid-beta peptide | MOUSE MODEL | A-BETA | ENDOPLASMIC-RETICULUM | PRECURSOR PROTEIN | DYSFUNCTION | ABNORMAL INTERACTION | TRANSGENIC MICE | Index Medicus | Biological Sciences | Biofysik | Biophysics | Naturvetenskap | Biokemi och molekylärbiologi | Biologiska vetenskaper | Biochemistry and Molecular Biology | Natural Sciences
Journal Article
Chemistry – A European Journal, ISSN 0947-6539, 04/2018, Volume 24, Issue 24, pp. 6349 - 6353
Although fibrillar amyloid beta peptide (Aβ) aggregates are one of the major hallmarks of Alzheimer's disease, increasing evidence suggests that soluble Aβ...
neurodegeneration | therapeutics | amyloid | zinc | aggregate | Oligomers | Peptides | Therapeutics | Cyclodextrins | Plants | Alzheimer's disease | Homeopathy | Materia medica and therapeutics | Porphyrins | Biological properties | Neurodegenerative diseases | Toxicity | Cytotoxicity | Agglomeration | Zinc | Zinc compounds | Cyclodextrin | β-Amyloid | Alzheimers disease | System effectiveness | Index Medicus
neurodegeneration | therapeutics | amyloid | zinc | aggregate | Oligomers | Peptides | Therapeutics | Cyclodextrins | Plants | Alzheimer's disease | Homeopathy | Materia medica and therapeutics | Porphyrins | Biological properties | Neurodegenerative diseases | Toxicity | Cytotoxicity | Agglomeration | Zinc | Zinc compounds | Cyclodextrin | β-Amyloid | Alzheimers disease | System effectiveness | Index Medicus
Journal Article
PLoS ONE, ISSN 1932-6203, 09/2013, Volume 8, Issue 9, p. e72169
Amyloid beta peptide (A beta) causes neurodegeneration by several mechanisms including oxidative stress, which is known to induce DNA damage with the...
ISCHEMIA-REPERFUSION INJURY | ADP-RIBOSE POLYMERASE-1 | SIGNAL-TRANSDUCTION | OXIDATIVE STRESS | DNA-BINDING | ALZHEIMERS-DISEASE | MULTIDISCIPLINARY SCIENCES | A-BETA | POLY(ADP-RIBOSE) POLYMERASE-1 | NF-KAPPA-B | NEUROBLASTOMA-CELLS | Cell Line | Cricetinae | Reactive Oxygen Species - metabolism | Cricetulus | Amyloid beta-Peptides - toxicity | Peptide Fragments - toxicity | Mice, Transgenic | DNA Primers | Poly(ADP-ribose) Polymerases - physiology | Comet Assay | Animals | Base Sequence | Electrophoretic Mobility Shift Assay | Mice | DNA Damage | Poly (ADP-Ribose) Polymerase-1 | Neurons - drug effects | CHO Cells | Genetic engineering | Peptides | Tumor proteins | Neurons | Sugars | Monosaccharides | Oxidative stress | Reactive oxygen species | Neurosciences | Bcl-2 protein | p53 Protein | DNA damage | Neuroblastoma | Kinases | ADP | Neuroblastoma cells | Proteins | Signal transduction | Neurotoxicity | Neurodegeneration | Ribose | Rodents | Pretreatment | Damage | Deoxyribonucleic acid--DNA | NF-κB protein | Medical research | Enzymes | Free radicals | Transgenic mice | Poly(ADP-ribose) polymerase | Gene expression | Polymerase | Poly(ADP-ribose) Polymerase 1 | Brain research | β-Amyloid | Alzheimers disease | Cancer | Apoptosis | Deoxyribonucleic acid | DNA
ISCHEMIA-REPERFUSION INJURY | ADP-RIBOSE POLYMERASE-1 | SIGNAL-TRANSDUCTION | OXIDATIVE STRESS | DNA-BINDING | ALZHEIMERS-DISEASE | MULTIDISCIPLINARY SCIENCES | A-BETA | POLY(ADP-RIBOSE) POLYMERASE-1 | NF-KAPPA-B | NEUROBLASTOMA-CELLS | Cell Line | Cricetinae | Reactive Oxygen Species - metabolism | Cricetulus | Amyloid beta-Peptides - toxicity | Peptide Fragments - toxicity | Mice, Transgenic | DNA Primers | Poly(ADP-ribose) Polymerases - physiology | Comet Assay | Animals | Base Sequence | Electrophoretic Mobility Shift Assay | Mice | DNA Damage | Poly (ADP-Ribose) Polymerase-1 | Neurons - drug effects | CHO Cells | Genetic engineering | Peptides | Tumor proteins | Neurons | Sugars | Monosaccharides | Oxidative stress | Reactive oxygen species | Neurosciences | Bcl-2 protein | p53 Protein | DNA damage | Neuroblastoma | Kinases | ADP | Neuroblastoma cells | Proteins | Signal transduction | Neurotoxicity | Neurodegeneration | Ribose | Rodents | Pretreatment | Damage | Deoxyribonucleic acid--DNA | NF-κB protein | Medical research | Enzymes | Free radicals | Transgenic mice | Poly(ADP-ribose) polymerase | Gene expression | Polymerase | Poly(ADP-ribose) Polymerase 1 | Brain research | β-Amyloid | Alzheimers disease | Cancer | Apoptosis | Deoxyribonucleic acid | DNA
Journal Article
Inorganic Chemistry, ISSN 0020-1669, 11/2013, Volume 52, Issue 21, pp. 12193 - 12206
Aggregation of amyloid-beta (A beta) by self-assembly into oligomers or amyloids is a central event in Alzheimer's disease. Coordination of transition-metal...
IN-VITRO | STRUCTURAL BASIS | INDUCED AGGREGATION | A-BETA | REDOX CHEMISTRY | PRECURSOR PROTEIN | COPPER COORDINATION | ZINC-BINDING | NEURODEGENERATIVE DISEASES | PHYSIOLOGICAL CONCENTRATIONS | CHEMISTRY, INORGANIC & NUCLEAR | Amyloid - metabolism | Zinc - metabolism | Humans | Alzheimer Disease - metabolism | Amyloid beta-Peptides - metabolism | Copper - metabolism | Amyloid - chemistry | Amyloid beta-Peptides - chemistry | Alzheimer Disease - pathology | Hydrogen-Ion Concentration
IN-VITRO | STRUCTURAL BASIS | INDUCED AGGREGATION | A-BETA | REDOX CHEMISTRY | PRECURSOR PROTEIN | COPPER COORDINATION | ZINC-BINDING | NEURODEGENERATIVE DISEASES | PHYSIOLOGICAL CONCENTRATIONS | CHEMISTRY, INORGANIC & NUCLEAR | Amyloid - metabolism | Zinc - metabolism | Humans | Alzheimer Disease - metabolism | Amyloid beta-Peptides - metabolism | Copper - metabolism | Amyloid - chemistry | Amyloid beta-Peptides - chemistry | Alzheimer Disease - pathology | Hydrogen-Ion Concentration
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 03/2010, Volume 285, Issue 12, pp. 9100 - 9113
Alzheimer disease is an age-related neurodegenerative disorder characterized by amyloid-beta (A beta) peptide deposition into cerebral amyloid plaques. The...
CANCER-CELLS | LIFE-SPAN | IN-VITRO | GALLIC ACID | ALZHEIMERS-DISEASE | FOOD-INTAKE | BIOCHEMISTRY & MOLECULAR BIOLOGY | MOUSE MODEL | DIETARY RESTRICTION | SIRT1 ACTIVATION | GAMMA-SECRETASE | AMP-Activated Protein Kinases - metabolism | Signal Transduction | Calcium - metabolism | Humans | Enzyme Inhibitors - pharmacology | Male | Mice, Transgenic | Stilbenes - pharmacology | Autophagy | Animals | Lysosomes - metabolism | Alzheimer Disease - metabolism | Cytosol - metabolism | Mice | Neurons - metabolism | Amyloid beta-Peptides - chemistry | Secretases | Calcium | Protein Kinases | Proteases | Neurobiology | Resveratrol | Amyloid | Alzheimer Disease | Diseases
CANCER-CELLS | LIFE-SPAN | IN-VITRO | GALLIC ACID | ALZHEIMERS-DISEASE | FOOD-INTAKE | BIOCHEMISTRY & MOLECULAR BIOLOGY | MOUSE MODEL | DIETARY RESTRICTION | SIRT1 ACTIVATION | GAMMA-SECRETASE | AMP-Activated Protein Kinases - metabolism | Signal Transduction | Calcium - metabolism | Humans | Enzyme Inhibitors - pharmacology | Male | Mice, Transgenic | Stilbenes - pharmacology | Autophagy | Animals | Lysosomes - metabolism | Alzheimer Disease - metabolism | Cytosol - metabolism | Mice | Neurons - metabolism | Amyloid beta-Peptides - chemistry | Secretases | Calcium | Protein Kinases | Proteases | Neurobiology | Resveratrol | Amyloid | Alzheimer Disease | Diseases
Journal Article