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1. Full Text Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade
by Chiti, Fabrizio and Dobson, Christopher M
Annual review of biochemistry, ISSN 0066-4154, 6/2017, Volume 86, Issue 1, pp. 27 - 68
amyloidosis | quality control | protein aggregation | protein homeostasis | conformational diseases | chaperones | functional amyloid | Protein aggregation | Quality control | Functional amyloid | Amyloidosis | Chaperones | Protein homeostasis | Conformational diseases | Proteostasis Deficiencies - metabolism | Molecular Chaperones - metabolism | History, 21st Century | Parkinson Disease - history | Humans | Proteostasis Deficiencies - history | Protein Aggregation, Pathological - history | Drugs, Investigational | Parkinson Disease - drug therapy | Amyloid - chemistry | Diabetes Mellitus, Type 2 - metabolism | Diabetes Mellitus, Type 2 - history | Molecular Targeted Therapy | Alzheimer Disease - pathology | Amyloid - metabolism | Protein Aggregation, Pathological - pathology | Protein Aggregation, Pathological - prevention & control | Parkinson Disease - metabolism | Immunoglobulin Light-chain Amyloidosis | Amyloid - genetics | Alzheimer Disease - history | Parkinson Disease - pathology | Amyloidosis - pathology | Amyloidosis - history | Gene Expression Regulation | Molecular Chaperones - genetics | Proteostasis Deficiencies - pathology | Alzheimer Disease - drug therapy | Amyloidosis - drug therapy | Protein Folding | Proteostasis Deficiencies - prevention & control | Alzheimer Disease - metabolism | Protein Conformation | Diabetes Mellitus, Type 2 - pathology | Proteostasis Deficiencies - drug therapy | Diabetes Mellitus, Type 2 - drug therapy | Amyloidosis - metabolism | Protein Aggregation, Pathological - metabolism | Physiological aspects | Development and progression | Genetic aspects | Protein folding | Amyloid beta-protein | Peptides | Diabetes mellitus | Fibrils | Parkinsons disease | Disorders | Agglomeration | Tissues | Human tissues | Proteins | Aggregates | β-Amyloid | Genetic factors | Alzheimers disease | Protein interaction | Index Medicus
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2. Full Text The green tea polyphenol (−)-epigallocatechin gallate prevents the aggregation of tau protein into toxic oligomers at substoichiometric ratios
by Wobst, Heike J and Sharma, Apurwa and Diamond, Marc I and Wanker, Erich E and Bieschke, Jan
FEBS letters, ISSN 0014-5793, 01/2015, Volume 589, Issue 1, pp. 77 - 83
Tau oligomers | Aggregation inhibitors | Polyphenol | (−)-Epigallocatechin gallate | Alzheimer‘s disease | Tau protein | ThT | NBT | Thioflavin T | 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide | EGCG | AFM | MTT | atomic force microscopy | (−)-epigallocatechin gallate | nitroblue tetrazolium | Alzheimer's disease | PCR | polymerase chain reaction | Alzheimers disease | (-)-Epigallocatechin gallate | Biochemistry & Molecular Biology | Biophysics | Life Sciences & Biomedicine | Science & Technology | Cell Biology | Humans | Rats | tau Proteins - metabolism | PC12 Cells | tau Proteins - chemistry | Animals | tau Proteins - genetics | Protein Aggregation, Pathological - pathology | Catechin - analogs & derivatives | Catechin - pharmacology | Protein Aggregation, Pathological - genetics | Catechin - chemistry | Protein Aggregation, Pathological - metabolism | Tea - chemistry | Prevention | Oligomers | Catechin | Green tea | Index Medicus | aggregation inhibitors | tau oligomers | polyphenol
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3. Full Text Amyloid-β receptors: The good, the bad, and the prion protein
by Jarosz-Griffiths, Heledd H and Noble, Elizabeth and Rushworth, Jo V and Hooper, Nigel M
The Journal of biological chemistry, ISSN 0021-9258, 02/2016, Volume 291, Issue 7, pp. 3174 - 3183
Neurons - pathology | Receptors, N-Methyl-D-Aspartate - antagonists & inhibitors | PrPC Proteins - agonists | Apoptosis - drug effects | Humans | Receptors, N-Methyl-D-Aspartate - metabolism | Molecular Targeted Therapy | Receptors, Cell Surface - antagonists & inhibitors | Alzheimer Disease - pathology | Nerve Tissue Proteins - chemistry | Receptor Aggregation - drug effects | Protein Isoforms - metabolism | Protein Aggregation, Pathological - pathology | Alzheimer Disease - prevention & control | Protein Aggregation, Pathological - prevention & control | Protein Isoforms - chemistry | Amyloid beta-Peptides - metabolism | Neurons - metabolism | PrPC Proteins - metabolism | Neurons - drug effects | PrPC Proteins - antagonists & inhibitors | Protein Aggregates - drug effects | Nerve Tissue Proteins - antagonists & inhibitors | Receptor for Advanced Glycation End Products - metabolism | Receptors, Cell Surface - agonists | Alzheimer Disease - drug therapy | Low Density Lipoprotein Receptor-Related Protein-1 - metabolism | Nootropic Agents - therapeutic use | Receptors, Cell Surface - metabolism | Receptor for Advanced Glycation End Products - agonists | Protein Aggregation, Pathological - drug therapy | Nerve Tissue Proteins - metabolism | Amyloid beta-Peptides - antagonists & inhibitors | Animals | Low Density Lipoprotein Receptor-Related Protein-1 - agonists | Signal Transduction - drug effects | Models, Biological | Receptors, N-Methyl-D-Aspartate - agonists | Alzheimer Disease - metabolism | Ligands | Transcytosis - drug effects | Amyloid beta-Peptides - chemistry | Nootropic Agents - pharmacology | Protein Aggregation, Pathological - metabolism | Protein Isoforms - antagonists & inhibitors | Index Medicus | Minireviews | oligomer | prion | amyloid | receptor | Alzheimer disease
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4. Full Text Multistep Inhibition of α‑Synuclein Aggregation and Toxicity in Vitro and in Vivo by Trodusquemine
by Perni, Michele and Flagmeier, Patrick and Limbocker, Ryan and Cascella, Roberta and Aprile, Francesco A and Galvagnion, Céline and Heller, Gabriella T and Meisl, Georg and Chen, Serene W and Kumita, Janet R and Challa, Pavan K and Kirkegaard, Julius B and Cohen, Samuel I. A and Mannini, Benedetta and Barbut, Denise and Nollen, Ellen A. A and Cecchi, Cristina and Cremades, Nunilo and Knowles, Tuomas P. J and Chiti, Fabrizio and Zasloff, Michael and Vendruscolo, Michele and Dobson, Christopher M
ACS chemical biology, ISSN 1554-8929, 08/2018, Volume 13, Issue 8, pp. 2308 - 2319
FIBRIL FORMATION | AMPLIFICATION STEPS | LIFE-SPAN | CAENORHABDITIS-ELEGANS | SOLID-STATE NMR | SPECTROSCOPY | INITIATION | BETA-SYNUCLEIN | C-ELEGANS | PARKINSONS-DISEASE | Life Sciences & Biomedicine | Biochemistry & Molecular Biology | Science & Technology | Cell Line | Humans | Spermine - therapeutic use | Cholestanes - therapeutic use | Parkinson Disease - drug therapy | Caenorhabditis elegans - physiology | Animals | Spermine - pharmacology | Protein Aggregation, Pathological - prevention & control | Cholestanes - pharmacology | Neurons - metabolism | Parkinson Disease - metabolism | Neurons - drug effects | alpha-Synuclein - metabolism | Protein Aggregation, Pathological - metabolism | Spermine - analogs & derivatives | Disease Models, Animal | Protein Aggregates - drug effects | Index Medicus
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