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PLoS ONE, ISSN 1932-6203, 12/2006, Volume 1, Issue 1, pp. e119 - e119
Biomedical researchers have become increasingly aware of the limitations of conventional 2-dimensional tissue cell culture systems, including coated Petri... 
BIOLOGY | Protein Multimerization | Molecular Sequence Data | Neurons - cytology | Gene Expression Profiling | Cell Culture Techniques - methods | Tissue Scaffolds - chemistry | Laminin | Peptides - chemical synthesis | Drug Design | Cell Differentiation | Neurons - metabolism | Nanofibers - chemistry | Amino Acid Sequence | Nanofibers - ultrastructure | Adult Stem Cells - cytology | Microscopy, Electron, Scanning | Proteoglycans | Peptides - chemistry | Cell Survival | Models, Molecular | Amino Acid Motifs | Adult Stem Cells - metabolism | Animals | Collagen | Mice | Drug Combinations | Stem cell research | Peptides | Cell differentiation | Gene expression | Stem cells | Neurophysiology | Cell culture | Self assembly | Nestin | Populations | Motility | Media (culture) | Leukocyte migration | Leukemia | Differentiation (biology) | Tissue culture | Stem cell transplantation | Nervous system | Biology | Cell adhesion & migration | Proteins | Three dimensional bodies | Homing | Biomedical materials | Tubulin | Allografts | Assembling | Cell adhesion | Bone marrow | Extracellular matrix | Synthetic peptides | Growth factors | Biomedical engineering | Medical research | Cell survival | Tissue engineering | Glial fibrillary acidic protein | Cultures | Metabolism | Neurotrophic factors | Self-assembly | Culture media | Neural stem cells | Bone | Nanofibers | Scaffolds | Cell migration | Cancer | Index Medicus
Journal Article
Journal of Neuroscience, ISSN 0270-6474, 10/2012, Volume 32, Issue 40, pp. 13819 - 13840
Genetically encoded calcium indicators (GECIs) are powerful tools for systems neuroscience. Recent efforts in protein engineering have significantly increased... 
2-PHOTON EXCITATION | GREEN FLUORESCENT PROTEIN | DROSOPHILA-MELANOGASTER | CELLULAR RESOLUTION | IN-VIVO | NETWORK ACTIVITY | MOTOR CORTEX | BARREL CORTEX | NEUROSCIENCES | MOUSE VISUAL-CORTEX | CA2+ INDICATORS | Olfactory Receptor Neurons - physiology | Hippocampus - chemistry | Humans | Peptides - genetics | Recombinant Fusion Proteins - analysis | Crystallography, X-Ray | Green Fluorescent Proteins - genetics | Neuromuscular Junction - chemistry | Neuropil - ultrastructure | Neurons - ultrastructure | Lasers | Astrocytes - chemistry | Green Fluorescent Proteins - isolation & purification | Neuroimaging - methods | Neuropil - physiology | Neurons - chemistry | Genes, Synthetic | Models, Molecular | Rats | Recombinant Fusion Proteins - chemistry | Astrocytes - ultrastructure | Olfactory Receptor Neurons - chemistry | Caenorhabditis elegans | Larva | Retinal Bipolar Cells - ultrastructure | Recombinant Fusion Proteins - genetics | Drosophila melanogaster - growth & development | Protein Conformation | Mice | Peptides - analysis | Fluorescent Dyes - analysis | Fluorometry - methods | Olfactory Receptor Neurons - ultrastructure | Synaptic Transmission | Retinal Bipolar Cells - physiology | Neurons - physiology | Female | Green Fluorescent Proteins - chemistry | Calcium Signaling | Fluorescent Dyes - chemistry | Green Fluorescent Proteins - analysis | Mutagenesis, Site-Directed | Peptides - chemistry | Neuropil - chemistry | Retinal Bipolar Cells - chemistry | HEK293 Cells - chemistry | Hippocampus - cytology | HEK293 Cells - ultrastructure | Neuromuscular Junction - ultrastructure | Zebrafish - growth & development | Animals | Genetic Vectors | Photic Stimulation | Index Medicus | GCaMP5 | functional imaging | genetically encoded calcium indicator | GECI | GCaMP3
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
Science, ISSN 0036-8075, 7/2009, Volume 325, Issue 5938, pp. 328 - 332
Amyloids are highly organized cross--β-sheet--rich protein or peptide aggregates that are associated with pathological conditions including Alzheimer's disease... 
Aggregation | Secretory vesicles | Neurons | Cell aggregates | Antibodies | Fluorescence | Reports | Amyloids | Hormones | Solar fibrils | Monomers | CELLS | PROTEIN | FIBRILS | GLYCOSAMINOGLYCANS | MOLECULAR-ORGANIZATION | PROLACTIN GRANULES | BIOGENESIS | ALZHEIMERS-DISEASE | MULTIDISCIPLINARY SCIENCES | ALPHA-SYNUCLEIN | AMYLOIDOGENESIS | Humans | Secretory Vesicles - metabolism | Neurons - cytology | Pituitary Gland - chemistry | Amyloid - chemistry | Pituitary Gland, Anterior - metabolism | Pituitary Hormones - chemistry | Peptide Hormones - metabolism | Urocortins - metabolism | beta-Endorphin - metabolism | Amyloid - metabolism | Neurons - physiology | Pituitary Hormones - metabolism | Peptide Hormones - chemistry | Adrenocorticotropic Hormone - metabolism | beta-Endorphin - chemistry | Secretory Vesicles - chemistry | Adrenocorticotropic Hormone - chemistry | Cell Survival | Pituitary Gland, Posterior - chemistry | Heparin, Low-Molecular-Weight - chemistry | Rats | Corticotropin-Releasing Hormone - chemistry | Urocortins - chemistry | Corticotropin-Releasing Hormone - metabolism | Animals | Pituitary Gland, Posterior - metabolism | Protein Conformation | Sheep | Mice | Pituitary Gland, Anterior - chemistry | Hydrogen-Ion Concentration | Glycoproteins | Research | Properties | Peptide hormones | Proteins | Pituitary gland | Physiology | Peptides | Cellular biology | Index Medicus | Medical and Health Sciences | MEDICINE | Medicin och hälsovetenskap | MEDICIN
Journal Article
Science, ISSN 0036-8075, 1/2013, Volume 339, Issue 6118, pp. 452 - 456
Journal Article
Analytical and Bioanalytical Chemistry, ISSN 1618-2642, 1/2013, Volume 405, Issue 1, pp. 203 - 213
Liquid chromatography coupled to tandem mass spectrometry has been compared to shotgun analysis with the objective of finding the best compromise for a single... 
Biochemistry, general | Chemistry | Analytical Chemistry | Food Science | Characterization and Evaluation of Materials | Shotgun | Liquid chromatography | Phospholipids | Laboratory Medicine | Mass spectrometry | Environmental Monitoring/Analysis | CHEMISTRY, ANALYTICAL | MULTIPLE PRECURSOR | BIOLOGICAL SAMPLES | BIOCHEMICAL RESEARCH METHODS | SHOTGUN LIPIDOMICS | TANDEM MASS-SPECTROMETRY | QUANTITATIVE-ANALYSIS | ENERGY COLLISIONAL ACTIVATION | DRIVEN FRAGMENTATION PROCESSES | MECHANISTIC PROPOSAL | DATA-DEPENDENT ACQUISITION | ELECTROSPRAY-IONIZATION | Reproducibility of Results | Chromatography, High Pressure Liquid - methods | Phosphatidylinositols - chemistry | Phosphatidylserines - chemistry | Phospholipids - chemistry | Phosphatidylcholines - chemistry | Fungi - metabolism | Carbon - chemistry | Lipids - chemistry | Phosphatidylglycerols - chemistry | Chemistry Techniques, Analytical | Phosphatidic Acids - chemistry | Acyltransferases - chemistry | Chromatography, Liquid - methods | Phosphatidylethanolamines - chemistry | Tandem Mass Spectrometry - methods | Yeast fungi | Physiological aspects | Microbiological chemistry | Chemical properties | Research | Identification and classification | Methods | Index Medicus | Polyethylenes | Atomic properties | Shotguns | Carbon | Fatty acids | Strain | Analytical chemistry | Life Sciences | Quantitative Methods | Biochemistry, Molecular Biology | Genomics | Neurons and Cognition | Neurobiology | Biomolecules | Chemical Sciences
Journal Article
2004, 2nd ed., Molecular and cellular neurobiology series, ISBN 0198509987, xvii, 480
Neurons are arguably the most complex of all cells. From the action of these cells comes movement, thought, and consciousness. It is a challenging task to... 
Molecular biology | Molecular neurobiology | Neurons
Book
Journal Article
Science, ISSN 0036-8075, 5/2013, Volume 340, Issue 6132, pp. 610 - 614
Serotonin or 5-hydroxytryptamine (5-HT) regulates a wide spectrum of human physiology through the 5-HT receptor family. We report the crystal structures of the... 
Receptors | Sand sheets | Hydrogen bonds | Serotonin receptors | REPORTS | Ligands | Agonists | Indoles | Grants | LSD | Binding sites | LIGANDS | PROTEIN-COUPLED RECEPTOR | PHARMACOLOGY | MULTIDISCIPLINARY SCIENCES | MUTATION | CARDIAC VALVULOPATHY | VALVULAR HEART-DISEASE | SCHIZOPHRENIA | DISORDERS | FENFLURAMINE | AGONIST | Pindolol - chemistry | Humans | Lysergic Acid Diethylamide - metabolism | Molecular Sequence Data | Crystallography, X-Ray | Propranolol - metabolism | Serotonin 5-HT1 Receptor Agonists - chemistry | Ergotamine - chemistry | Ergotamine - metabolism | Receptor, Serotonin, 5-HT1B - genetics | Receptor, Serotonin, 5-HT1B - metabolism | Binding Sites | Amino Acid Sequence | Tryptamines - chemistry | Norfenfluramine - metabolism | Dihydroergotamine - chemistry | Protein Structure, Secondary | Models, Molecular | Dihydroergotamine - metabolism | Lysergic Acid Diethylamide - chemistry | Propranolol - chemistry | Serotonin 5-HT1 Receptor Agonists - metabolism | Pindolol - analogs & derivatives | Protein Folding | Norfenfluramine - chemistry | Hydrogen Bonding | Mutagenesis | Tryptamines - metabolism | Receptor, Serotonin, 5-HT1B - chemistry | Hydrophobic and Hydrophilic Interactions | Protein Conformation | Molecular Docking Simulation | Pindolol - metabolism | Physiological aspects | Research | G proteins | Serotonin | Molecular biology | Ligands (Biochemistry) | Neurons | Index Medicus
Journal Article
Science, ISSN 0036-8075, 2/2010, Volume 327, Issue 5969, pp. 1132 - 1135
The prion hypothesis posits that a misfolded form of prion protein (PrP) is responsible for the infectivity of prion disease. Using recombinant murine PrP... 
Nervous system diseases | RNA | Neurons | Prions | Cell lines | Antibodies | Prion diseases | Lipids | Reports | Mice | Inoculum | STRAINS | SCRAPIE | RESISTANT | IN-VITRO | MULTIDISCIPLINARY SCIENCES | MICE | CONFORMATION | PROPAGATION | PRP | MOLECULES | Cell Line | Neurons - chemistry | Prions - pathogenicity | PrPSc Proteins - analysis |