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1. Full Text Mechanisms and Functions of Spatial Protein Quality Control
by Sontag, Emily Mitchell and Samant, Rahul S and Frydman, Judith
Annual review of biochemistry, ISSN 0066-4154, 6/2017, Volume 86, Issue 1, pp. 97 - 122
neurodegenerative diseases | aging | molecular chaperones | proteostasis | protein aggregation | misfolded protein clearance | Aging | Protein aggregation | Misfolded protein clearance | Proteostasis | Molecular chaperones | Neurodegenerative diseases | Proteostasis Deficiencies - metabolism | Protein Biosynthesis | Molecular Chaperones - metabolism | Humans | Amyloidogenic Proteins - chemistry | Prion Proteins - metabolism | Cell Compartmentation | Aging - genetics | Protein Aggregation, Pathological - pathology | Proteolysis | Prion Proteins - chemistry | Prion Proteins - genetics | Protein Aggregation, Pathological - genetics | Amyloidogenic Proteins - genetics | Neurodegenerative Diseases - pathology | Gene Expression Regulation | Molecular Chaperones - genetics | Protein Refolding | Proteostasis Deficiencies - pathology | Neurodegenerative Diseases - genetics | Neurodegenerative Diseases - metabolism | Protein Folding | Aging - pathology | Proteostasis Deficiencies - genetics | Amyloidogenic Proteins - metabolism | Protein Conformation | Protein Aggregation, Pathological - metabolism | Aging - metabolism | Proteins | Nervous system diseases | Quality control | Physiological aspects | Research | Protein folding | Proteomics | Cell survival | Pathogenesis | Homeostasis | Agglomeration | Chaperones | Disease control | Machinery | Diseases | Machinery and equipment | Neurological diseases | Compartments | Amyloid | Aberration | Proteomes | Protein interaction | Neurological disorders | Plaques | Cancer | Fitness | Index Medicus
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2. Full Text Amyloid fibril proteins and amyloidosis: chemical identification and clinical classification International Society of Amyloidosis 2016 Nomenclature Guidelines
by Sipe, Jean D and Benson, Merrill D and Buxbaum, Joel N and Ikeda, Shu-ichi and Merlini, Giampaolo and Saraiva, Maria J. M and Westermark, Per
Amyloid, ISSN 1350-6129, 10/2016, Volume 23, Issue 4, pp. 209 - 213
inclusion body | nomenclature | amyloidosis | Amyloid fibril | amyloid protein | Biochemistry & Molecular Biology | Life Sciences & Biomedicine | Medicine, General & Internal | General & Internal Medicine | Medicine, Research & Experimental | Science & Technology | Research & Experimental Medicine | Staining and Labeling - methods | Prealbumin - genetics | Guidelines as Topic | Apolipoprotein C-III - chemistry | Protein Precursors - chemistry | Humans | Apolipoprotein C-III - metabolism | tau Proteins - metabolism | Amyloidosis - diagnosis | Amyloidogenic Proteins - chemistry | Apolipoprotein C-III - genetics | Apolipoprotein C-II - genetics | tau Proteins - chemistry | Sequence Analysis, Protein | tau Proteins - genetics | Amyloidosis - genetics | Amyloidosis - classification | Prealbumin - chemistry | alpha-Synuclein - genetics | Apolipoprotein C-II - chemistry | Amyloidogenic Proteins - genetics | Biomarkers - metabolism | Gene Expression | Protein Precursors - genetics | Amyloidosis - pathology | Terminology as Topic | Protein Precursors - metabolism | alpha-Synuclein - chemistry | Amyloidogenic Proteins - metabolism | Prealbumin - metabolism | Apolipoprotein C-II - metabolism | Birefringence | Congo Red - chemistry | alpha-Synuclein - metabolism | Coloring Agents - chemistry | Index Medicus
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3. Full Text Structural Studies of Amyloid Proteins at the Molecular Level
by Eisenberg, David S and Sawaya, Michael R
Annual review of biochemistry, ISSN 0066-4154, 6/2017, Volume 86, Issue 1, pp. 69 - 95
solid-state nuclear magnetic resonance | amyloid symmetry | steric zipper | polymorphs | X-ray diffraction | ssNMR | cryo-EM | cryo-electron microscopy | SsNMR | Polymorphs | Solid-state nuclear magnetic resonance | Steric zipper | Cryo-EM | Amyloid symmetry | Cryo-electron microscopy | Gene Expression | Protein Structure, Secondary | Humans | Protein Multimerization | Amyloidogenic Proteins - chemistry | Prion Proteins - metabolism | Amino Acid Motifs | Cryoelectron Microscopy | Amyloidogenic Proteins - metabolism | Animals | Protein Aggregation, Pathological - pathology | X-Ray Diffraction | Protein Denaturation | Nuclear Magnetic Resonance, Biomolecular | Prion Proteins - chemistry | Protein Stability | Prion Proteins - genetics | Protein Aggregation, Pathological - genetics | Protein Aggregation, Pathological - metabolism | Amyloidogenic Proteins - genetics | Physiological aspects | Genetic aspects | Structure | Amyloid beta-protein | Neurodegenerative diseases | Structural stability | Fibrils | Amino acid sequence | Seeding | Membrane proteins | Proteins | Neurological diseases | Microorganisms | β-Amyloid | Prion protein | Neurological disorders | Cancer | Index Medicus
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4. Full Text Attempt to untangle the prion-like misfolding mechanism for neurodegenerative diseases
by Sarnataro, Daniela
International journal of molecular sciences, ISSN 1661-6596, 10/2018, Volume 19, Issue 10, p. 3081
Aggregation | APP | Prion-like | Seeds | Tau | Amyloid | Misfolding | Prion protein | PrP | Biochemistry & Molecular Biology | Physical Sciences | Chemistry | Life Sciences & Biomedicine | Chemistry, Multidisciplinary | Science & Technology | Alzheimer Disease - etiology | Proteostasis Deficiencies - metabolism | Neurodegenerative Diseases - etiology | Proteostasis Deficiencies - etiology | Humans | Endoplasmic Reticulum - metabolism | Amyloidogenic Proteins - chemistry | Prion Proteins - metabolism | Genetic Variation | Cell Membrane - metabolism | Prion Proteins - chemistry | Prion Proteins - genetics | Amyloidogenic Proteins - genetics | Disease Susceptibility | Signal Transduction | Proteostasis Deficiencies - pathology | Neurodegenerative Diseases - metabolism | Intrinsically Disordered Proteins - genetics | Protein Folding | Amyloidogenic Proteins - metabolism | Animals | Intrinsically Disordered Proteins - chemistry | Alzheimer Disease - metabolism | Protein Binding | Golgi Apparatus - metabolism | Protein Processing, Post-Translational | Intrinsically Disordered Proteins - metabolism | Index Medicus | Aβ | amyloid | prion-like | seeds | tau | aggregation | misfolding | prion protein
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