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2006, Advances in protein chemistry, ISBN 0120342731, Volume 73., vii, 320 p., [28] p of plates
Amyloids, Prions and Beta Proteins is the last volume of the three-part thematic series on Fibrous Proteins in the Advances in Protein Chemistry serial.... 
Proteins | Amyloid | Prions | Amyloid beta-protein
Book
1999, Methods in enzymology, ISBN 0121822109, Volume 309, xxxix, 820
This volume includes a core of methodologies to attack the unique experimental problems presented by protein misassembly. Emphasis is on human biology... 
Prions | Amyloid | Amyloid beta-protein | Proteins
Book
2007, ISBN 1852339616, xi, 298
Recent advances in genetics and brain biochemistry point to the Abeta peptide as the major culprit in causing neurodegeneration in Alzheimer’s Disease (AD).... 
Alzheimer's disease | Molecular aspects | Amyloid beta-protein
Book
2012, 2nd ed., Methods in molecular biology, ISBN 161779550X, Volume 849., xv, 548
Book
Journal of Biological Chemistry, ISSN 0021-9258, 09/2001, Volume 276, Issue 37, pp. 35176 - 35184
Assembly of the amyloid beta -protein (A beta) into neurotoxic oligomers and fibrils is a seminal event in Alzheimer's disease. Understanding the earliest... 
FIBRIL FORMATION | ENHANCED PRODUCTION | IN-VITRO | ATOMIC-FORCE MICROSCOPY | CONFORMATIONAL-CHANGES | TRANSTHYRETIN | ALZHEIMERS-DISEASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | CELL-CULTURE | FIBRILLOGENESIS | PEPTIDE | Prealbumin - chemistry | Molecular Weight | Amyloid beta-Peptides - chemistry | Light | Hydrogen-Ion Concentration | Index Medicus
Journal Article
The EMBO Journal, ISSN 0261-4189, 01/2018, Volume 37, Issue 2, pp. 282 - 299
Huntington's disease ( HD ) is a neurodegenerative disorder caused by an expanded CAG trinucleotide repeat in the huntingtin gene ( HTT ). Molecular chaperones... 
NPC | suppression | disaggregation | molecular chaperones | HttpolyQ | NPCs | EXPANDED HUNTINGTIN | HSP70 | PROTEIN AGGREGATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | DRUG DISCOVERY | CELLULAR-MODEL | CELL BIOLOGY | CAENORHABDITIS-ELEGANS | AMYLOID-LIKE FIBRILS | HEAT-SHOCK RESPONSE | POLYGLUTAMINE AGGREGATION | HUNTINGTONS-DISEASE | Neurons - pathology | HSC70 Heat-Shock Proteins - metabolism | Humans | Huntington Disease - pathology | Multiprotein Complexes - genetics | HSP110 Heat-Shock Proteins - chemistry | Multiprotein Complexes - metabolism | Protein Aggregation, Pathological - pathology | HEK293 Cells | Neurons - metabolism | HSP40 Heat-Shock Proteins - chemistry | Protein Aggregation, Pathological - genetics | HSC70 Heat-Shock Proteins - genetics | HSP40 Heat-Shock Proteins - metabolism | HSP40 Heat-Shock Proteins - genetics | Huntingtin Protein - metabolism | Huntington Disease - metabolism | Huntingtin Protein - chemistry | Caenorhabditis elegans | HSP110 Heat-Shock Proteins - genetics | Multiprotein Complexes - chemistry | Animals | HSC70 Heat-Shock Proteins - chemistry | Huntington Disease - genetics | Huntingtin Protein - genetics | HSP110 Heat-Shock Proteins - metabolism | Protein Aggregation, Pathological - metabolism | Huntingtons disease | Polyglutamine | Huntingtin | Neurodegenerative diseases | Fibrils | Trinucleotide repeats | Disaggregation | Agglomeration | Chaperones | Huntington's disease | Mammalian cells | Proteins | Fibrillogenesis | Hsc70 protein | Index Medicus | Neuroscience | Protein Biosynthesis & Quality Control | Molecular Biology of Disease
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 01/2013, Volume 288, Issue 3, pp. 1856 - 1870
Journal Article
Journal of Molecular Biology, ISSN 0022-2836, 06/2014, Volume 426, Issue 13, pp. 2500 - 2519
Misfolded protein aggregates, characterized by a canonical amyloid fold, play a central role in the pathobiology of neurodegenerative diseases. Agents that... 
amyloid | gene 3 protein | amyloid remodeling | Ig fusion | FIBRIL FORMATION | MEMBRANE-FILTER ASSAY | N-TERMINAL DOMAINS | ALZHEIMERS-DISEASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | ALPHA-SYNUCLEIN | FILAMENTOUS PHAGE FD | PROLYL ISOMERIZATION | CONFORMATIONAL CONVERSION | A-BETA | Neurodegenerative Diseases - etiology | Humans | Protein Multimerization | tau Proteins - metabolism | Bacteriophage M13 - metabolism | Recombinant Fusion Proteins - metabolism | tau Proteins - chemistry | Bacteriophage M13 - genetics | Amyloid beta-Peptides - metabolism | Capsid Proteins - chemistry | Membrane Transport Proteins - metabolism | Protein Interaction Domains and Motifs | Capsid Proteins - metabolism | Bacterial Outer Membrane Proteins - chemistry | Models, Molecular | Escherichia coli Proteins - metabolism | Neurodegenerative Diseases - metabolism | Recombinant Fusion Proteins - chemistry | Protein Folding | Membrane Transport Proteins - chemistry | alpha-Synuclein - chemistry | Bacterial Outer Membrane Proteins - metabolism | Protein Binding | Recombinant Fusion Proteins - genetics | Protein Conformation | Amyloid beta-Peptides - chemistry | Kinetics | Escherichia coli Proteins - chemistry | alpha-Synuclein - metabolism | Capsid Proteins - genetics | Viral proteins | Isomerization | Protein binding | Index Medicus
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 07/2015, Volume 290, Issue 28, pp. 17628 - 17641
Surfactant protein C (SP-C) is a novel amyloid protein found in the lung tissue of patients suffering from interstitial lung disease (ILD) due to mutations in... 
ENDOPLASMIC-RETICULUM MEMBRANE | INTERSTITIAL LUNG-DISEASE | REACTIVE PROTEIN | FIBRIL FORMATION | PHYSICAL-PROPERTIES | SURFACE-ACTIVITY | TRANSLOCATION | DOMAIN | AMYLOID BETA-PEPTIDE | BIOCHEMISTRY & MOLECULAR BIOLOGY | MUTATION | Recombinant Proteins - metabolism | Lung Diseases, Interstitial - metabolism | Mutagenesis, Site-Directed | Protein Precursors - genetics | Protein Precursors - chemistry | Humans | Endoplasmic Reticulum - metabolism | Pulmonary Surfactant-Associated Protein C - metabolism | Rats | Recombinant Proteins - chemistry | Amyloidogenic Proteins - chemistry | Recombinant Proteins - genetics | Pulmonary Surfactant-Associated Protein C - chemistry | Protein Folding | Protein Precursors - metabolism | Amyloidogenic Proteins - metabolism | Animals | Lung Diseases, Interstitial - genetics | Membrane Lipids - metabolism | Protein Binding | Pulmonary Surfactant-Associated Protein C - genetics | Protein Interaction Domains and Motifs | In Vitro Techniques | Amyloidogenic Proteins - genetics | Index Medicus | lung | amyloid diseases | chaperone activity | Membrane Biology | membrane structure | lipid-binding protein | amyloid-like fibril | lipid bilayer | protein folding | lipid-protein interactions | pulmonary surfactant | Biological Sciences | Naturvetenskap | Natural Sciences | Biologiska vetenskaper
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 02/2016, Volume 291, Issue 9, pp. 4374 - 4385
Although trace levels of phosphorylated alpha-synuclein (alpha-syn) are detectable in normal brains, nearly all alpha-syn accumulated within Lewy bodies in... 
MULTIPLE SYSTEM ATROPHY | INCLUSION FORMATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | DISEASE-LINKED MUTATIONS | LEWY BODY DISEASE | MEDIATED PHOSPHORYLATION | SER-129 PHOSPHORYLATION | PARKINSONS-DISEASE | TRANSGENIC MICE | CELL-DEATH | OLIGODENDROGLIAL CELLS | Phosphorylation | Mesencephalon - cytology | Dopaminergic Neurons - pathology | Mesencephalon - metabolism | Humans | Synaptosomes - metabolism | Recombinant Fusion Proteins - metabolism | Dopaminergic Neurons - cytology | Endocytosis | Synaptosomes - pathology | Protein Aggregation, Pathological - pathology | Dopaminergic Neurons - metabolism | Parkinson Disease - metabolism | alpha-Synuclein - genetics | Protein Aggregation, Pathological - genetics | Protein-Serine-Threonine Kinases - metabolism | Mesencephalon - pathology | Animals, Newborn | Recombinant Proteins - metabolism | Cell Line | Parkinson Disease - pathology | Cells, Cultured | Protein-Serine-Threonine Kinases - genetics | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Parkinson Disease - genetics | Serine - metabolism | Protein Folding | alpha-Synuclein - chemistry | Animals | Recombinant Fusion Proteins - genetics | Mice | Protein Processing, Post-Translational | Mutation | alpha-Synuclein - metabolism | Protein Aggregation, Pathological - metabolism | Amino Acid Substitution | Index Medicus | post-translational modification (PTM) | Molecular Bases of Disease | fibril | protein misfolding | Parkinson disease | endocytosis | protein self-assembly | protein kinase | vesicles
Journal Article