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Amyloid, ISSN 1350-6129, 10/2016, Volume 23, Issue 4, pp. 209 - 213
The Nomenclature Committee of the International Society of Amyloidosis (ISA) met during the XVth Symposium of the Society, 3 July-7 July 2016, Uppsala, Sweden,... 
inclusion body | nomenclature | amyloidosis | Amyloid fibril | amyloid protein | MEDICINE, RESEARCH & EXPERIMENTAL | BIOCHEMISTRY & MOLECULAR BIOLOGY | TRANSTHYRETIN AMYLOIDOSIS | MEDICINE, GENERAL & INTERNAL | TRANSMISSION | SEMEN | DISEASE | SENILE SYSTEMIC AMYLOIDOSIS | 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 | Basic Medicine | Medical and Health Sciences | Medicin och hälsovetenskap | Medicinska och farmaceutiska grundvetenskaper | Cell and Molecular Biology | Cell- och molekylärbiologi
Journal Article
The FEBS Journal, ISSN 1742-464X, 10/2017, Volume 284, Issue 19, pp. 3218 - 3229
Bridging integrator 1 ( bin1 ) gene is a genetic determinant of Alzheimer's disease (AD) and has been reported to modulate Alzheimer's pathogenesis through... 
nuclear magnetic resonance spectroscopy | protein–protein interaction | Tau | Alzheimer's disease | BIN | 3 domain | SH3 domain | BIN1 | ALZHEIMERS-DISEASE | NMR-SPECTROSCOPY | BIOCHEMISTRY & MOLECULAR BIOLOGY | PATHOLOGY | MODEL | IDENTIFIES VARIANTS | AMPHIPHYSIN | MEMBRANE CURVATURE | protein-protein interaction | BINDING | EXPRESSION | GENOME-WIDE ASSOCIATION | Adaptor Proteins, Signal Transducing - chemistry | Humans | Peptides - genetics | tau Proteins - metabolism | tau Proteins - chemistry | Peptides - metabolism | Protein Isoforms - metabolism | tau Proteins - genetics | Protein Isoforms - chemistry | Tumor Suppressor Proteins - chemistry | Tumor Suppressor Proteins - genetics | Cloning, Molecular | Escherichia coli - metabolism | Nuclear Magnetic Resonance, Biomolecular | Neurons - metabolism | Protein Interaction Domains and Motifs | Nuclear Proteins - genetics | Binding Sites | Recombinant Proteins - metabolism | Protein Conformation, alpha-Helical | Gene Expression | Tumor Suppressor Proteins - metabolism | Neurons - chemistry | Peptides - chemistry | Models, Molecular | Recombinant Proteins - chemistry | Nuclear Proteins - metabolism | Recombinant Proteins - genetics | Nuclear Proteins - chemistry | Amino Acid Motifs | Sequence Homology, Amino Acid | Sequence Alignment | Protein Conformation, beta-Strand | Escherichia coli - genetics | Adaptor Proteins, Signal Transducing - genetics | Protein Binding | Kinetics | Adaptor Proteins, Signal Transducing - metabolism | Protein Isoforms - genetics | Nuclear magnetic resonance spectroscopy | Neurons | Protein-protein interactions | Spectroscopy | Clathrin | Nuclear magnetic resonance--NMR | Peptides | Neurodegenerative diseases | Pathogenesis | Complexity | Proteins | Magnetic resonance spectroscopy | Tau protein | Spectrum analysis | Isoforms | Alzheimers disease | Binding sites | Index Medicus | tau Proteins/metabolism | Nuclear Proteins/chemistry | Protein Isoforms/chemistry | Protein Isoforms/genetics | Adaptor Proteins, Signal Transducing/genetics | Recombinant Proteins/metabolism | Peptides/metabolism | Life Sciences | Recombinant Proteins/chemistry | Adaptor Proteins, Signal Transducing/chemistry | Nuclear Proteins/metabolism | Tumor Suppressor Proteins/chemistry | Nuclear Proteins/genetics | Tumor Suppressor Proteins/metabolism | Protein Isoforms/metabolism | Peptides/chemistry | Recombinant Proteins/genetics | Biochemistry, Molecular Biology | Escherichia coli/genetics | Escherichia coli/metabolism | Adaptor Proteins, Signal Transducing/metabolism | Neurons/chemistry | Tumor Suppressor Proteins/genetics | tau Proteins/genetics | Neurons/metabolism | Peptides/genetics | tau Proteins/chemistry
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 01/2013, Volume 288, Issue 3, pp. 1856 - 1870
Journal Article
Human Molecular Genetics, ISSN 0964-6906, 2/2008, Volume 17, Issue 3, pp. 431 - 439
Journal Article
Nature, ISSN 0028-0836, 2012, Volume 485, Issue 7400, pp. 651 - 655
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 2018, Volume 293, Issue 8, pp. 2687 - 2700
The microtubule-associated protein tau forms insoluble, amyloid-type aggregates in various dementias, most notably Alzheimer's disease. Cellular chaperone... 
HEAT-SHOCK PROTEINS | NEUROFIBRILLARY TANGLES | OXIDATIVE STRESS | ALZHEIMERS-DISEASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | FRONTOTEMPORAL DEMENTIA | PAIRED HELICAL FILAMENTS | ALPHA-B-CRYSTALLIN | PLASTICITY DEFICITS | BETA-STRUCTURE | AGGREGATION | HSP27 Heat-Shock Proteins - chemistry | HSC70 Heat-Shock Proteins - metabolism | Humans | tau Proteins - metabolism | Amyloid - chemistry | Amyloid - ultrastructure | HSC70 Heat-Shock Proteins - ultrastructure | Recombinant Fusion Proteins - metabolism | tau Proteins - chemistry | HSP27 Heat-Shock Proteins - genetics | HSP27 Heat-Shock Proteins - ultrastructure | Protein Isoforms - metabolism | tau Proteins - genetics | Amyloid - metabolism | Protein Aggregation, Pathological - pathology | Protein Aggregation, Pathological - prevention & control | Protein Isoforms - chemistry | Amyloid - drug effects | Protein Interaction Domains and Motifs | Dimerization | Heparin - pharmacology | tau Proteins - ultrastructure | HSC70 Heat-Shock Proteins - genetics | Solubility | Models, Molecular | Recombinant Fusion Proteins - chemistry | Down-Regulation - drug effects | Amino Acid Motifs | Cryoelectron Microscopy | HSC70 Heat-Shock Proteins - chemistry | Anticoagulants - pharmacology | HSP27 Heat-Shock Proteins - metabolism | Kinetics | Mutation | Protein Aggregation, Pathological - metabolism | Amino Acid Substitution | Index Medicus | Protein Structure and Folding | amyloid | chaperone | 70 kilodalton heat shock protein (Hsp70) | tau | aggregation | small heat shock protein (sHsp)
Journal Article
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
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 12/2016, Volume 113, Issue 50, pp. E8187 - E8196
Tau prions are thought to aggregate in the central nervous system, resulting in neurodegeneration. Among the tauopathies, Alzheimer's disease (AD) is the most... 
Pick's disease | Tauopathies | Argyrophilic grain disease | Progressive supranuclear palsy | Corticobasal degeneration | MOUSE-BRAIN | NEUROFIBRILLARY TANGLES | corticobasal degeneration | BRAIN-INJURY | MULTIDISCIPLINARY SCIENCES | FRONTOTEMPORAL DEMENTIA | SHARE ANTIGENIC DETERMINANTS | PICKS-DISEASE | ABNORMAL PHOSPHORYLATION | argyrophilic grain disease | MICROTUBULE-ASSOCIATED PROTEIN | PAIRED HELICAL FILAMENTS | tauopathies | progressive supranuclear palsy | TRANSGENIC MICE | Up-Regulation | Chronic Traumatic Encephalopathy - metabolism | Humans | Bacterial Proteins - chemistry | tau Proteins - metabolism | Pick Disease of the Brain - genetics | Recombinant Fusion Proteins - metabolism | tau Proteins - chemistry | Protein Isoforms - metabolism | tau Proteins - genetics | Chronic Traumatic Encephalopathy - genetics | HEK293 Cells | Luminescent Proteins - chemistry | Pick Disease of the Brain - metabolism | Supranuclear Palsy, Progressive - genetics | Cell Line | Bacterial Proteins - genetics | Recombinant Fusion Proteins - chemistry | Alzheimer Disease - metabolism | Recombinant Fusion Proteins - genetics | Supranuclear Palsy, Progressive - metabolism | Bacterial Proteins - metabolism | Luminescent Proteins - genetics | Mutation | Alzheimer Disease - genetics | Luminescent Proteins - metabolism | Protein Isoforms - genetics | Physiological aspects | Alzheimer's disease | Health aspects | Prions | Encephalopathy | Proteins | Brain | Alzheimers disease | Cells | Index Medicus
Journal Article
Journal of the American Chemical Society, ISSN 0002-7863, 10/2011, Volume 133, Issue 42, pp. 16958 - 16969
Journal Article
Science, ISSN 0036-8075, 10/2006, Volume 314, Issue 5796, pp. 130 - 133
Ubiquitin-positive, tau- and α-synuclein--negative inclusions are hallmarks of frontotemporal lobar degeneration with ubiquitin-positive inclusions and... 
Proteins | Pathology | Nervous system diseases | Spinal cord | Neurodegenerative diseases | Neurons |