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The FEBS journal, ISSN 1742-464X, 10/2017, Volume 284, Issue 19, pp. 3218 - 3229
.... 1H, 15N spectra showed that the C‐terminal SH3 domain of BIN1 isoform 1 (BIN1Iso1) is not mobile in solution but locked with the core of the protein... 
SH3 domain | nuclear magnetic resonance spectroscopy | protein–protein interaction | Tau | BIN1 | Alzheimer's disease | 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 | 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
PloS one, ISSN 1932-6203, 09/2017, Volume 12, Issue 9, p. e0180905
Proteins associated with neurodegenerative diseases are highly pleiomorphic and may adopt an all-a-helical fold in one environment, assemble into all-beta-sheet or collapse into a coil in another... 
ALPHA-SYNUCLEIN OLIGOMERS | ATOMIC-FORCE MICROSCOPY | SOLID-STATE NMR | SODIUM DODECYL-SULFATE | MULTIDISCIPLINARY SCIENCES | PARTIALLY FOLDED STRUCTURE | PAIRED HELICAL FILAMENTS | AMYLOID-BETA-PROTEIN | C-TERMINAL THREONINE | INDUCED CONFORMATIONAL-CHANGES | HUMAN PRION PROTEIN | Protein Aggregates | Protein Structure, Secondary | Humans | Protein Multimerization | Models, Molecular | tau Proteins - metabolism | PrPSc Proteins - chemistry | Protein Folding | tau Proteins - chemistry | PrPSc Proteins - genetics | alpha-Synuclein - chemistry | PrPSc Proteins - metabolism | Animals | tau Proteins - genetics | Amyloid beta-Peptides - genetics | Amyloid beta-Peptides - metabolism | Protein Domains | alpha-Synuclein - genetics | Amyloid beta-Peptides - chemistry | Protein Stability | alpha-Synuclein - metabolism | Electrons | Hydrogen-Ion Concentration | Protein folding | Physiological aspects | Nervous system | Development and progression | Degeneration | Genetic aspects | Research | Coils | Amyloidogenesis | Backbone | Rate constants | Agglomeration | Synuclein | pH effects | Neuromodulation | Modulators | Proteins | Oligomers | Fibrillogenesis | Pathways | Chirality | Chemical bonds | Catalysis | Prion protein | Dimerization | Folding | Linkages | Polypeptides | Incubation | Neurodegenerative diseases | Tertiary structure | Polymerization | Shielding | Secondary structure | Density distribution | Neurological diseases | Chemistry | Tensors | Propagation (polymerization) | Aggregates | Tau protein | Prions | Morphology | β-Amyloid | Dimers | Mutation | Protein structure
Journal Article
Proceedings of the National Academy of Sciences - PNAS, ISSN 1091-6490, 2016, Volume 113, Issue 50, pp. E8187 - E8196
...) tau prions, were used to infect HEK293T cells expressing 3R tau fused to yellow fluorescent protein (YFP... 
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 | Biological Sciences | PNAS Plus | Pick’s disease
Journal Article
Journal Article
Biochemistry (Easton), ISSN 0006-2960, 01/2012, Volume 51, Issue 4, pp. 888 - 898
Journal Article
PloS one, ISSN 1932-6203, 2017, Volume 12, Issue 6, p. e0178933
Abundant regulatory 14-3-3 proteins have an extremely wide interactome and coordinate multiple cellular events via interaction with specifically phosphorylated partner proteins... 
Exoribonucleases - genetics | Phosphorylation | Humans | tau Proteins - metabolism | Protein Interaction Maps | Cyclic AMP-Dependent Protein Kinases - genetics | Protein Isoforms - metabolism | tau Proteins - genetics | Cloning, Molecular | Escherichia coli - metabolism | Biomarkers, Tumor - metabolism | Parkinson Disease - metabolism | Exoribonucleases - analysis | 14-3-3 Proteins - genetics | Cyclic AMP-Dependent Protein Kinases - metabolism | Gene Expression | Biomarkers, Tumor - analysis | Protein Isoforms - analysis | 14-3-3 Proteins - metabolism | Cyclic AMP-Dependent Protein Kinases - analysis | 14-3-3 Proteins - analysis | Escherichia coli - genetics | Alzheimer Disease - metabolism | Biomarkers, Tumor - genetics | tau Proteins - analysis | Exoribonucleases - metabolism | Protein Isoforms - genetics | Research | Protein kinases | Protein-protein interactions | Protein kinase A | Stoichiometry | Residues | Identification methods | Disorders | Displays | Biochemistry | Biology | Kinases | Proteins | Signal transduction | Functional anatomy | E coli | Rodents | Bacteria | Physiology | Binding | Neurodegenerative diseases | Fetuses | Cloning | Diseases | Studies | Neurological diseases | 14-3-3 protein | Tau protein | Protein kinase | Plasmids | Isoforms | Protein expression | Regulation | Alzheimers disease | In vitro methods and tests | Binding sites | Apoptosis
Journal Article
Nature communications, ISSN 2041-1723, 2018, Volume 9, Issue 1, pp. 4532 - 13
Journal Article