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1. Full Text Protein aggregation in amyotrophic lateral sclerosis
by Blokhuis, Anna M and Groen, Ewout J. N and Koppers, Max and van den Berg, Leonard H and Pasterkamp, R Jeroen
Acta Neuropathologica, ISSN 0001-6322, 6/2013, Volume 125, Issue 6, pp. 777 - 794
Amyotrophic lateral sclerosis (ALS) is a neurodegenerative disease characterized by the aggregation of ubiquitinated proteins in affected motor neurons. Recent... 
Aggregation | Pathology | Neurosciences | Protein degradation | Medicine & Public Health | Amyotrophic lateral sclerosis (ALS) | RNA granule | Motor neuron | RNA-PROCESSING PROTEIN | PRION-LIKE DOMAINS | PATHOLOGY | FRONTOTEMPORAL LOBAR DEGENERATION | DNA-BINDING PROTEIN | LENGTH POLYGLUTAMINE EXPANSIONS | NEUROSCIENCES | CLINICAL NEUROLOGY | NEURON DISEASES ALS | SPINAL MUSCULAR-ATROPHY | HEXANUCLEOTIDE REPEAT | C-TERMINAL FRAGMENTS | TRANSGENIC MICE | Transcription Factor TFIIIA - physiology | Proteins - physiology | DNA-Binding Proteins - physiology | Nerve Tissue Proteins - physiology | Humans | Inclusion Bodies - physiology | Ubiquitins - physiology | Amyotrophic Lateral Sclerosis - pathology | Ataxins | Proteolysis | Amyotrophic Lateral Sclerosis - metabolism | RNA-Binding Protein FUS - physiology | C9orf72 Protein | Amyotrophic Lateral Sclerosis - etiology | Cell Cycle Proteins - physiology | Review
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2. Full Text Trans-cellular propagation of Tau aggregation by fibrillar species
by Kfoury, Najla and Holmes, Brandon B and Jiang, Hong and Holtzman, David M and Diamond, Marc I
Journal of Biological Chemistry, ISSN 0021-9258, 06/2012, Volume 287, Issue 23, pp. 19440 - 19451
Aggregation of the microtubule associated protein Tau is associated with several neurodegenerative disorders, including Alzheimer disease and frontotemporal... 
NEUROFIBRILLARY TANGLES | CELLS | ALZHEIMERS-DISEASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ALPHA-SYNUCLEIN | PATHOLOGY | POLYGLUTAMINE AGGREGATION | NEURODEGENERATIVE DISEASES | PASSIVE-IMMUNIZATION | TANGLE MOUSE MODEL | PARKINSONS-DISEASE | Frontotemporal Dementia - genetics | Humans | tau Proteins - metabolism | Antibodies, Neutralizing - pharmacology | Multiprotein Complexes - genetics | Protein Folding | Alzheimer Disease - pathology | Multiprotein Complexes - antagonists & inhibitors | Frontotemporal Dementia - metabolism | Multiprotein Complexes - metabolism | tau Proteins - genetics | Models, Biological | Alzheimer Disease - metabolism | HEK293 Cells | Alzheimer Disease - genetics | Antibodies, Monoclonal, Murine-Derived - pharmacology | tau Proteins - antagonists & inhibitors | Frontotemporal Dementia - pathology | Aggregation | Aggregates | Propagation | Neurodegeneration | Fibrils | Neurobiology | Tau | Fluorescence Resonance Energy Transfer (FRET) | Alzheimer Disease
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3. Full Text From Macroscopic Measurements to Microscopic Mechanisms of Protein Aggregation
by Cohen, Samuel I.A and Vendruscolo, Michele and Dobson, Christopher M and Knowles, Tuomas P.J
Journal of Molecular Biology, ISSN 0022-2836, 08/2012, Volume 421, Issue 2-3, pp. 160 - 171
The ability to relate bulk experimental measurements of amyloid formation to the microscopic assembly processes that underlie protein aggregation is critical... 
nucleation | aggregation | amyloid | kinetics | mechanism | SPONTANEOUS FRAGMENTATION | NUCLEATED POLYMERIZATION | PRION DISEASES | ALZHEIMERS-DISEASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | AMYLOID-BETA-PROTEIN | ACTIN-FILAMENTS | POLYGLUTAMINE AGGREGATION | MISFOLDING DISEASES | ASSOCIATION | Models, Theoretical | Protein Binding | Proteins - metabolism | Kinetics | Amyloid - biosynthesis
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4. Full Text Excitation-induced ataxin-3 aggregation in neurons from patients with Machado-Joseph disease
by Koch, Philipp and Breuer, Peter and Peitz, Michael and Jungverdorben, Johannes and Kesavan, Jaideep and Poppe, Daniel and Doerr, Jonas and Ladewig, Julia and Mertens, Jerome and Tüting, Thomas and Hoffmann, Per and Klockgether, Thomas and Evert, Bernd O and Wüllner, Ullrich and Brüstle, Oliver
Nature, ISSN 0028-0836, 12/2011, Volume 480, Issue 7378, pp. 543 - 546
Machado-Joseph disease (MJD; also called spinocerebellar ataxia type 3) is a dominantly inherited late-onset neurodegenerative disorder caused by expansion of... 
POLYGLUTAMINE-EXPANDED ATAXIN-3 | IN-VITRO | INCLUSIONS | MULTIDISCIPLINARY SCIENCES | EXPANSION | NEURODEGENERATION | DISORDERS | MODEL | PROTEOLYSIS | CLEAVAGE | PROTEINS | Calpain - metabolism | Ataxin-3 | Glutamic Acid - pharmacology | Calcium - metabolism | Excitatory Amino Acids - pharmacology | Humans | Cells, Cultured | Nuclear Proteins - metabolism | Nerve Tissue Proteins - metabolism | Neurons - metabolism | Neurons - drug effects | Repressor Proteins - metabolism | Machado-Joseph Disease - pathology | Physiological aspects | Genetic engineering | Research | Cerebellar ataxia
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5. Full Text Protein degradation, aggregation, and misfolding
by Cuervo, Ana Maria and Wong, Esther S.P and Martinez‐Vicente, Marta
Movement Disorders, ISSN 0885-3185, 2010, Volume 25, Issue S1, pp. S49 - S54
The cellular surveillance systems guarantee proper removal of altered components from inside cells. Alterations of these systems in neurons have been proposed... 
neurodegeneration | lysosomes | protein aggregates | autophagy | proteases | Lysosomes | Neurodegeneration | Proteases | Autophagy | Protein aggregates | SYSTEM | CHAPERONE-MEDIATED AUTOPHAGY | SYNPHILIN-1 | ALPHA-SYNUCLEIN | CLINICAL NEUROLOGY | UBIQUITINATION | POLYGLUTAMINE DISEASES | PROTEASOME | BODY FORMATION | PARKINSONS-DISEASE | Neurons - pathology | Parkinson Disease - pathology | Humans | Ubiquitin - metabolism | Models, Molecular | Autophagy - physiology | Protein Folding | Animals | Proteins - metabolism | Protein Conformation | Neurons - metabolism | Parkinson Disease - metabolism | Proteasome Endopeptidase Complex - metabolism | alpha-Synuclein - metabolism
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6. Full Text Critical nucleus size for disease-related polyglutamine aggregation is repeat-length dependent
by Jayaraman, Murali and Kodali, Ravindra and Wetzel, Ronald and Sahoo, Bankanidhi and Kar, Karunakar
Nature Structural & Molecular Biology, ISSN 1545-9993, 03/2011, Volume 18, Issue 3, pp. 328 - 336
Because polyglutamine (polyQ) aggregate formation has been implicated as playing an important role in expanded CAG repeat diseases, it is important to... 
MECHANISM | PROTEIN AGGREGATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | MONOMERIC POLYGLUTAMINE | CELL BIOLOGY | PRION PROTEIN | IN-VITRO | THERMODYNAMICS | PEPTIDES | BIOPHYSICS | AMYLOID FIBRIL ELONGATION | NUCLEATION | MOLECULAR-DYNAMICS SIMULATIONS | Peptides - metabolism | Kinetics | Neurodegenerative Diseases - metabolism | Protein Structure, Secondary | Humans | Physiological aspects | Nervous system diseases | Genetic aspects | Polypeptides | Research | Polymerization | Biophysics | Peptides | Molecular biology | Pathogenesis
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7. Full Text Prefoldin prevents aggregation of α-synuclein
by Takano, Mariko and Tashiro, Erika and Kitamura, Akira and Maita, Hiroshi and Iguchi-Ariga, Sanae M.M and Kinjo, Masataka and Ariga, Hiroyoshi
Brain Research, ISSN 0006-8993, 2013, Volume 1542, pp. 186 - 194
Abstract Protein aggregation is observed in various neurodegeneration diseases, including Parkinson's disease (PD). Alpha-synuclein, a causative gene product... 
Neurology | α-Synuclein | Prefoldin | Protein aggregation | Cell death | Chaperone | UBIQUITIN-PROTEASOME SYSTEM | PROTEIN | HSP70 | MOLECULAR CHAPERONES | AUTOPHAGY | NEUROSCIENCES | POLYGLUTAMINE TOXICITY | OLIGOMERS | IN-VIVO | MUTATION | alpha-Synuclein | PARKINSONS-DISEASE | Green Fluorescent Proteins - metabolism | Molecular Chaperones - metabolism | Humans | RNA, Small Interfering - pharmacology | Molecular Chaperones - genetics | Ubiquitin - metabolism | Green Fluorescent Proteins - genetics | Mutation - genetics | Transfection | Cell Death - genetics | Cell Line, Tumor | Luminescent Proteins - genetics | alpha-Synuclein - genetics | Cell Death - drug effects | alpha-Synuclein - metabolism | Neuroblastoma - pathology | Luminescent Proteins - metabolism
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8. Full Text Poly(trehalose) Nanoparticles Prevent Amyloid Aggregation and Suppress Polyglutamine Aggregation in a Huntington's Disease Model Mouse
by Debnath, Koushik and Pradhan, Nibedita and Singh, Brijesh Kumar and Jana, Nihar R and Jana, Nikhil R
ACS Applied Materials and Interfaces, ISSN 1944-8244, 07/2017, Volume 9, Issue 28, pp. 24126 - 24139
Prevention and therapeutic strategies for various neurodegenerative diseases focus on inhibiting protein fibrillation, clearing aggregated protein plaques from... 
neurodegenerative disease | nanoparticle | trehalose | amyloid aggregation | polyglutamine aggregation | Huntington's disease | Alzheimer's disease | BETA-PROTEIN FIBRILLATION | ALZHEIMERS-DISEASE | STABILITY | MATERIALS SCIENCE, MULTIDISCIPLINARY | NANOSCIENCE & NANOTECHNOLOGY | NEUROTOXICITY | PEPTIDE | OLIGOMERS | INHIBITION | CHAPERONES | NUCLEATION | Huntington Disease | Nanoparticles | Animals | Peptides | Trehalose | Mice | Nerve Tissue Proteins | Index Medicus
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9. Full Text Does N‐terminal huntingtin function as a ‘holdase’ for inhibiting cellular protein aggregation?
by Sethi, Ratnika and Tripathi, Neha and Pallapati, Anusha R and Gaikar, Abhishek and Bharatam, Prasad V and Roy, Ipsita
The FEBS Journal, ISSN 1742-464X, 05/2018, Volume 285, Issue 10, pp. 1791 - 1811
Proteolytic cleavage of huntingtin gives rise to N‐terminal fragments. While the role of truncated mutant huntingtin is described in Huntington's disease (HD)... 
amphipathic helix | N17 domain | holdase | huntingtin | yeast model | Amino Acid Sequence | Exons | Humans | Solubility | Huntingtin Protein - physiology | Green Fluorescent Proteins - genetics | Protein Aggregation, Pathological | Huntingtin Protein - chemistry | Particle Size | Sequence Homology, Amino Acid | Peptides - metabolism | Mutagenesis | Models, Biological | Proteolysis | Hydrophobic and Hydrophilic Interactions | Protein Conformation | Huntingtin Protein - genetics | Protein Stability | Tumor proteins | Cellular proteins | Polyglutamine | Yeast | Huntingtin | Pathogenesis | p53 Protein | Heat shock proteins | Agglomeration | Small heat shock proteins | Gene deletion | Synuclein | Huntington's disease | Proteins | Clonal deletion | Deletion | Polyproline | Protein interaction | Trinucleotide repeat diseases | Protein structure | Elongation | Heat shock
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10. Full Text Huntingtin aggregation and toxicity in Huntington's disease
by Bates, Gillian
The Lancet, ISSN 0140-6736, 05/2003, Volume 361, Issue 9369, pp. 1642 - 1644
Context Huntington's disease is a late onset neurodegenerative disorder for which the mutation is a CAG/polyglutamine (polyQ) repeat expansion in the gene... 
NEURONAL INTRANUCLEAR INCLUSIONS | PATHOGENESIS | MEDICINE, GENERAL & INTERNAL | PEPTIDES | MECHANISM | CHANNELS | POLYGLUTAMINE AGGREGATION | BRAIN | Peptides - physiology | Humans | Peptides - genetics | Huntington Disease - genetics | Huntington Disease - metabolism | Cell Aggregation - genetics | Huntington Disease - etiology | Toxicity | Neurological disorders | Mutation | Huntingtons disease | Phenotypes | Huntingtin | Peptides | Pathogenesis | Huntington's disease | Proteins | Aggregates | Neurodegeneration | Toxic diseases | Localization | Apoptosis
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11. Full Text What is the role of protein aggregation in neurodegeneration?
by Poirier, Michelle A and Ross, Christopher A
Nature Reviews Molecular Cell Biology, ISSN 1471-0072, 11/2005, Volume 6, Issue 11, pp. 891 - 898
UBIQUITIN-PROTEASOME SYSTEM | CHAPERONE-MEDIATED AUTOPHAGY | ALZHEIMERS-DISEASE | NEURONAL DEATH | MUTANT ALPHA-SYNUCLEIN | POLYGLUTAMINE AGGREGATION | INCLUSION-BODY FORMATION | HUNTINGTONS-DISEASE | A-BETA OLIGOMERS | PARKINSONS-DISEASE | CELL BIOLOGY
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