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1. Full Text Green Tea Seed Isolated Theasaponin E1 Ameliorates AD Promoting Neurotoxic Pathogenesis by Attenuating A beta Peptide Levels in SweAPP N2a Cells
by Khan, Muhammad Imran and Shin, Jin Hyuk and Kim, Min Yong and Shin, Tai Sun and Kim, Jong Deog
Molecules (Basel, Switzerland), ISSN 1420-3049, 05/2020, Volume 25, Issue 10, p. 2334
Biochemistry & Molecular Biology | Physical Sciences | Chemistry | Life Sciences & Biomedicine | Chemistry, Multidisciplinary | Science & Technology | Camellia sinensis - chemistry | Amyloid Precursor Protein Secretases - genetics | Neurons - pathology | Plant Extracts - chemistry | Membrane Glycoproteins - metabolism | ADAM10 Protein - genetics | Oleanolic Acid - analogs & derivatives | ADAM10 Protein - metabolism | Oleanolic Acid - pharmacology | Aspartic Acid Endopeptidases - genetics | Presenilins - antagonists & inhibitors | Acetylcholinesterase - genetics | Dose-Response Relationship, Drug | Insulysin - antagonists & inhibitors | Membrane Glycoproteins - antagonists & inhibitors | Neuroprotective Agents - pharmacology | Amyloid beta-Peptides - genetics | Presenilins - metabolism | Amyloid beta-Peptides - metabolism | Presenilins - genetics | Neprilysin - genetics | Membrane Proteins - metabolism | Neurons - metabolism | Seeds - chemistry | Neurons - drug effects | Oleanolic Acid - isolation & purification | Insulysin - metabolism | Aspartic Acid Endopeptidases - antagonists & inhibitors | Membrane Proteins - genetics | Neprilysin - metabolism | Membrane Proteins - agonists | Membrane Glycoproteins - genetics | Gene Expression Regulation - drug effects | Amyloid Precursor Protein Secretases - metabolism | Amyloid beta-Peptides - antagonists & inhibitors | Animals | Saponins - isolation & purification | Neuroprotective Agents - isolation & purification | Aspartic Acid Endopeptidases - metabolism | Neprilysin - antagonists & inhibitors | Cell Line, Tumor | Insulysin - genetics | Mice | Amyloid Precursor Protein Secretases - antagonists & inhibitors | Acetylcholinesterase - metabolism | Tea - chemistry | Saponins - pharmacology | Amyloidogenesis | Neuroprotection | Brain | Saponins | Peptides | Pathogenesis | Memory | Genes | Presenilin | Activation | Neuroblastoma | Acetylcholinesterase | Neuroblastoma cells | Western blotting | Proteins | Neurotoxicity | Neurodegeneration | Dementia disorders | Green tea | Alzheimer's disease | Enzyme-linked immunosorbent assay | Enzymes | b-Site APP cleaving enzyme 1 | Neurodegenerative diseases | Medical treatment | Liquid chromatography | Gene expression | High-performance liquid chromatography | Insulin | Polymerase chain reaction | Tea | Nicastrin | Hypotheses | Natural products | Presenilin 1 | Neprilysin | Secretase | Index Medicus | SweAPP N2a cells | α-secretase | Alzheimer’s disease | theasaponin E1 | amyloid precursor proteins | amyloidogenic pathway
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2. Full Text Effective suppression of the modified PHF6 peptide/1N4R Tau amyloid aggregation by intact curcumin, not its degradation products: Another evidence for the pigment as preventive/therapeutic “functional food”
by Bijari, Nooshin and Balalaie, Saeed and Akbari, Vali and Golmohammadi, Farhad and Moradi, Sajad and Adibi, Hadi and Khodarahmi, Reza
International journal of biological macromolecules, ISSN 0141-8130, 12/2018, Volume 120, Issue Pt A, pp. 1009 - 1022
Curcumin | Degradation products | 1N4R Tau isoform | Amyloid aggregation | Biochemistry & Molecular Biology | Physical Sciences | Chemistry | Life Sciences & Biomedicine | Chemistry, Applied | Polymer Science | Science & Technology | tau Proteins - ultrastructure | Amyloid - antagonists & inhibitors | Carrier Proteins - ultrastructure | Amyloidosis - pathology | Curcumin - chemistry | Humans | Carrier Proteins - antagonists & inhibitors | Curcumin - pharmacology | Amyloidogenic Proteins - chemistry | Amyloidosis - drug therapy | Amyloid - chemistry | Functional Food | Protein Aggregation, Pathological - drug therapy | tau Proteins - chemistry | Amyloid beta-Peptides - antagonists & inhibitors | X-Ray Diffraction | Microscopy, Atomic Force | Carrier Proteins - chemistry | Amyloid beta-Peptides - chemistry | Binding Sites | tau Proteins - antagonists & inhibitors | Amyloidogenic Proteins - ultrastructure | Functional foods | Alzheimer's disease | Methylene blue | Index Medicus
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3. Full Text The amyloid cascade hypothesis: are we poised for success or failure?
by Karran, Eric and De Strooper, Bart
Journal of neurochemistry, ISSN 0022-3042, 10/2016, Volume 139, Issue S2, pp. 237 - 252
Alzheimer's disease | Amyloid cascade clinical development | Biochemistry & Molecular Biology | Neurosciences | Neurosciences & Neurology | Life Sciences & Biomedicine | Science & Technology | Amino Acid Sequence | Amyloid - genetics | Antibodies, Monoclonal - pharmacology | Humans | Alzheimer Disease - therapy | Antibodies, Monoclonal - therapeutic use | Amyloidogenic Proteins - antagonists & inhibitors | Brain - drug effects | Brain - metabolism | Amyloid beta-Peptides - antagonists & inhibitors | Amyloidogenic Proteins - metabolism | Animals | Amyloid - metabolism | Signal Transduction - drug effects | Amyloid beta-Peptides - genetics | Amyloidosis - genetics | Alzheimer Disease - metabolism | Amyloid beta-Peptides - metabolism | Signal Transduction - physiology | Alzheimer Disease - genetics | Amyloidosis - metabolism | Amyloidogenic Proteins - genetics | Development and progression | Neurochemistry | Alzheimers disease | Pathogenesis | Index Medicus
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4. Full Text A Two-Site Mechanism for the Inhibition of IAPP Amyloidogenesis by Zinc
by Salamekh, Samer and Brender, Jeffrey R and Hyung, Suk-Joon and Nanga, Ravi Prakash Reddy and Vivekanandan, Subramanian and Ruotolo, Brandon T and Ramamoorthy, Ayyalusamy
Journal of molecular biology, ISSN 0022-2836, 2011, Volume 410, Issue 2, pp. 294 - 306
metal binding | amylin | amyloid | structure | Life Sciences & Biomedicine | Biochemistry & Molecular Biology | Science & Technology | Amino Acid Sequence | Amyloid - antagonists & inhibitors | Stereoisomerism | Zinc - metabolism | Humans | Protein Multimerization | Islet Amyloid Polypeptide - metabolism | Molecular Sequence Data | Amyloidogenic Proteins - chemistry | Amyloid - chemistry | Islet Amyloid Polypeptide - antagonists & inhibitors | Zinc - chemistry | Amyloidogenic Proteins - antagonists & inhibitors | Amyloidogenic Proteins - metabolism | Islet Amyloid Polypeptide - chemistry | Amyloid - biosynthesis | Protein Binding | Protein Conformation | Oligomers | Ionization | Dimethyl sulfoxide | Development and progression | Amyloidosis | Diabetes | Glucose | Mass spectrometry | Dextrose | Index Medicus | metal-binding
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5. Full Text Utilizing Structures of CYP2D6 and BACE1 Complexes To Reduce Risk of Drug–Drug Interactions with a Novel Series of Centrally Efficacious BACE1 Inhibitors
by Brodney, Michael A and Beck, Elizabeth M and Butler, Christopher R and Barreiro, Gabriela and Johnson, Eric F and Riddell, David and Parris, Kevin and Nolan, Charles E and Fan, Ying and Atchison, Kevin and Gonzales, Cathleen and Robshaw, Ashley E and Doran, Shawn D and Bundesmann, Mark W and Buzon, Leanne and Dutra, Jason and Henegar, Kevin and LaChapelle, Erik and Hou, Xinjun and Rogers, Bruce N and Pandit, Jayvardhan and Lira, Ricardo and Martinez-Alsina, Luis and Mikochik, Peter and Murray, John C and Ogilvie, Kevin and Price, Loren and Sakya, Subas M and Yu, Aijia and Zhang, Yong and O’Neill, Brian T and Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Journal of medicinal chemistry, ISSN 0022-2623, 04/2015, Volume 58, Issue 7, pp. 3223 - 3252
Protease Inhibitors - pharmacokinetics | Humans | Cytochrome P-450 CYP2D6 - chemistry | Ether-A-Go-Go Potassium Channels - metabolism | Molecular Sequence Data | Crystallography, X-Ray | Male | Structure-Activity Relationship | ERG1 Potassium Channel | Protease Inhibitors - pharmacology | Pyrazoles - chemistry | Drug Interactions | Drug Design | Inhibitory Concentration 50 | Protease Inhibitors - administration & dosage | Amino Acid Sequence | Aspartic Acid Endopeptidases - chemistry | Cytochrome P-450 CYP2D6 - genetics | Aspartic Acid Endopeptidases - antagonists & inhibitors | Models, Molecular | Protease Inhibitors - chemistry | Mice, Inbred Strains | Amyloid Precursor Protein Secretases - chemistry | Ether-A-Go-Go Potassium Channels - antagonists & inhibitors | Amyloidogenic Proteins - metabolism | Animals | Cytochrome P-450 CYP2D6 - metabolism | Amyloid Precursor Protein Secretases - antagonists & inhibitors | Index Medicus | 60 APPLIED LIFE SCIENCES | INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY
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6. Full Text Underlying mechanisms and chemical/biochemical therapeutic approaches to ameliorate protein misfolding neurodegenerative diseases
by Hekmatimoghaddam, Seyedhossein and Zare‐Khormizi, Mohamad Reza and Pourrajab, Fatemeh
BioFactors (Oxford), ISSN 0951-6433, 11/2017, Volume 43, Issue 6, pp. 737 - 759
cell proteostasis network | protein misfolding | chemical and/or biochemical therapeutic approches | Biochemistry & Molecular Biology | Endocrinology & Metabolism | Life Sciences & Biomedicine | Science & Technology | Heat-Shock Response - drug effects | Proteostasis Deficiencies - metabolism | Chalcones - chemistry | Molecular Chaperones - metabolism | Humans | Endoplasmic Reticulum - metabolism | Amyloidogenic Proteins - chemistry | Molecular Chaperones - chemistry | Neurodegenerative Diseases - drug therapy | Pyrimidinones - chemistry | Amyloidogenic Proteins - antagonists & inhibitors | Neuroprotective Agents - pharmacology | Protein Aggregation, Pathological - pathology | Protein Aggregation, Pathological - prevention & control | Protein Folding - drug effects | Endoplasmic Reticulum - drug effects | Chalcones - pharmacology | Pyrimidinones - pharmacology | Proteostasis - drug effects | Protein Aggregation, Pathological - genetics | Amyloidogenic Proteins - genetics | Unfolded Protein Response - drug effects | Neurodegenerative Diseases - pathology | Neuroprotective Agents - chemistry | Gene Expression Regulation | Molecular Chaperones - genetics | Proteostasis Deficiencies - pathology | Thiophenes - pharmacology | Neurodegenerative Diseases - genetics | Neurodegenerative Diseases - metabolism | Hydrazones - chemistry | Hydrazones - pharmacology | Proteostasis Deficiencies - genetics | Amyloidogenic Proteins - metabolism | Animals | Proteostasis Deficiencies - drug therapy | Thiophenes - chemistry | Protein Aggregation, Pathological - metabolism | Proteins | Nervous system | Degeneration | Health aspects | Protein binding | Index Medicus
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7. Full Text Generic inhibition of amyloidogenic proteins by two naphthoquinone–tryptophan hybrid molecules
by Scherzer‐Attali, Roni and Shaltiel‐Karyo, Ronit and Adalist, Yonatan H and Segal, Daniel and Gazit, Ehud
Proteins, structure, function, and bioinformatics, ISSN 0887-3585, 08/2012, Volume 80, Issue 8, pp. 1962 - 1973
lysozyme | calcitonin | insulin | amyloid fibrils | thioflavin‐T | IAPP | α‐synuclein | Calcitonin | Amyloid fibrils | Thioflavin-T | Insulin | α-synuclein | Lysozyme | Biochemistry & Molecular Biology | Biophysics | Life Sciences & Biomedicine | Science & Technology | Amyloidogenic Proteins - antagonists & inhibitors | Islet Amyloid Polypeptide - chemistry | Insulin - chemistry | Muramidase - chemistry | Calcitonin - chemistry | Humans | Alzheimer Disease - metabolism | Tryptophan - chemistry | Naphthoquinones - chemistry | Amyloidogenic Proteins - chemistry | Alzheimer Disease - pathology | alpha-Synuclein - chemistry | Index Medicus
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