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Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 5/2011, Volume 108, Issue 19, pp. 8003 - 8008
Dengue virus (DENV) causes the major arboviral disease of the tropics, characterized in its severe forms by signs of hemorrhage and plasma leakage. DENV... 
Molecules | Lipoproteins | Secretion | Dengue | HDL lipoproteins | Lipids | Triglycerides | Dengue virus | Detergents | Fatty acids | Amphiphilic proteins | Dengue hemorrhagic fever | Arbovirus | amphiphilic proteins | CELLS | COMPLEMENT | INFECTIONS | RNA REPLICATION | FORM | GLYCOPROTEIN NS1 | MULTIDISCIPLINARY SCIENCES | arbovirus | dengue hemorrhagic fever | secretion | LIPID PROFILE | HEMORRHAGIC-FEVER | WEST-NILE | REVEALS | Cell Line | Protein Subunits | Recombinant Proteins - ultrastructure | Drosophila | Humans | Protein Multimerization | Dengue Virus - ultrastructure | Cercopithecus aethiops | Models, Molecular | Recombinant Proteins - chemistry | Dengue Virus - chemistry | Cryoelectron Microscopy | Lipoproteins, HDL - ultrastructure | Viral Nonstructural Proteins - chemistry | Animals | Computer Simulation | HEK293 Cells | Protein Structure, Quaternary | Lipoproteins, HDL - chemistry | Nuclear Magnetic Resonance, Biomolecular | Imaging, Three-Dimensional | Viral Nonstructural Proteins - ultrastructure | Vero Cells | Dengue viruses | Genetic aspects | Lipid metabolism | Viral Nonstructural Proteins/ultrastructure | Lipoproteins, HDL/ultrastructure | Life Sciences | Recombinant Proteins/chemistry | Lipoproteins, HDL/chemistry | Viral Nonstructural Proteins/chemistry | Dengue Virus/ultrastructure | Dengue Virus/chemistry | Recombinant Proteins/ultrastructure | Microbiology and Parasitology | Biological Sciences
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... 
MOTOR-NEURONS | PRIMARY VISUAL-CORTEX | OPTICAL SENSOR | PROTEIN | CELLULAR RESOLUTION | IN-VIVO | NETWORK ACTIVITY | GENE-EXPRESSION | BARREL CORTEX | NEUROSCIENCES | 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
Journal Article
Journal of the American Society for Mass Spectrometry, ISSN 1044-0305, 02/2010, Volume 21, Issue 2, pp. 220 - 231
The spatial distribution of neutral lipids and hydrocarbons has been imaged using MALDI-TOF mass spectrometry on intact plant and insect surfaces, namely wings... 
Biotechnology | Chemistry | Analytical Chemistry | Bioinformatics | Proteomics | Organic Chemistry | MATRIX | CHEMISTRY, ANALYTICAL | FINE-STRUCTURE | HYDROCARBONS | DROSOPHILA-MELANOGASTER | BIOCHEMICAL RESEARCH METHODS | CHEMISTRY, PHYSICAL | WAX ESTERS | SARCOPHAGA-BULLATA | TOF MS | RAT-BRAIN TISSUE | SPECTROSCOPY | DESORPTION/IONIZATION MASS-SPECTROMETRY | SCALE INSECT | Arecaceae - anatomy & histology | Plant Leaves - chemistry | Arabidopsis - chemistry | Lithium - chemistry | Sodium - chemistry | Male | Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization - methods | Diptera - chemistry | Image Processing, Computer-Assisted - methods | Potassium - chemistry | Photography | Lipids - chemistry | Animals | Hydrocarbons - chemistry | Plant Proteins - chemistry | Wings, Animal - anatomy & histology | Arabidopsis - anatomy & histology | Insect Proteins - chemistry | Wings, Animal - chemistry | Female | Gentisates - chemistry | Lipids - analysis | Drosophila melanogaster - anatomy & histology | Diptera - anatomy & histology | Arabidopsis thaliana | Somatotropin | Fruit-flies | Oases | Hydrocarbons | Lipids | Ecology | Mass spectrometry | Plants | Beer | Esters | Legs | Drosophila | Sublimation | Cuticle | Lithium | Dihydroxybenzoic acid | Spatial distribution | Insects | Dienes | Leaves | Sodium | Imaging | Palm
Journal Article
eLife, ISSN 2050-084X, 08/2014, Volume 3, Issue 2014, pp. 1 - 17
The Cdc45/Mcm2-7/GINS ( CMG) helicase separates DNA strands during replication in eukaryotes. How the CMG is assembled and engages DNA substrates remains... 
replication fork | DNA replication | helicase | motor proteins | AAA+ ATPase | Mcm2-7 | MCM2-7 HELICASE | HEXAMERIC HELICASE | MINICHROMOSOME MAINTENANCE PROTEIN | ARCHAEAL MCM | BUDDING YEAST | STRUCTURAL BASIS | BIOLOGY | REPLICATIVE HELICASE | ELECTRON-MICROSCOPY | 26S PROTEASOME | CRYO-EM STRUCTURE | Minichromosome Maintenance Proteins - metabolism | Protein Multimerization | Eukaryotic Cells - metabolism | Drosophila Proteins - metabolism | Minichromosome Maintenance Proteins - chemistry | Protein Subunits - metabolism | Cell Cycle Proteins - chemistry | DNA-Binding Proteins - metabolism | Drosophila melanogaster - metabolism | Multiprotein Complexes - metabolism | Adenosine Triphosphate - metabolism | Protein Structure, Quaternary | Repressor Proteins - metabolism | Protein Structure, Tertiary | Repressor Proteins - chemistry | Chromosomal Proteins, Non-Histone - metabolism | DNA, Single-Stranded - metabolism | RNA-Binding Proteins - chemistry | Cell Cycle Proteins - metabolism | RNA Splicing Factors | Adenosine Triphosphatases - metabolism | Models, Molecular | DNA Replication | DNA - metabolism | Drosophila Proteins - chemistry | Microscopy, Electron | DNA-Binding Proteins - chemistry | Adenosine Triphosphate - analogs & derivatives | DNA, Single-Stranded - chemistry | Multiprotein Complexes - ultrastructure | DNA - chemistry | Multiprotein Complexes - chemistry | Animals | Protein Binding | Adenosine Triphosphatases - chemistry | Protein Subunits - chemistry | Adenosine Triphosphate - chemistry | Chromosomal Proteins, Non-Histone - chemistry | RNA-Binding Proteins - metabolism | Medical research | Single-stranded DNA | Hexamers | Electron microscopy | DNA biosynthesis | DNA helicase | Handedness | Microscopy | Insects | Cdc45 protein | Cell cycle | Polarity | Dimerization | Deoxyribonucleic acid--DNA | Adenosine triphosphatase
Journal Article
Science, ISSN 0036-8075, 9/2007, Volume 317, Issue 5843, pp. 1390 - 1393
Tricyclic antidepressants exert their pharmacological effect--inhibiting the reuptake of serotonin, norepinephrine, and dopamine--by directly blocking... 
Molecules | Salts | Neurotransmitters | Antidepressants | Reuptake | Serotonin plasma membrane transport proteins | Neurotransmitter transport proteins | Reports | Pharmacology | Inhibitory concentration 50 | Crystal structure | SENSITIVE DOPAMINE TRANSPORTER | NOREPINEPHRINE TRANSPORTERS | MULTIDISCIPLINARY SCIENCES | ION-BINDING | MONOAMINE TRANSPORTERS | SEROTONIN | INHIBITORS | Dopamine - chemistry | Antidepressive Agents, Tricyclic - metabolism | Caenorhabditis elegans Proteins - chemistry | Humans | Bacterial Proteins - chemistry | Caenorhabditis elegans Proteins - metabolism | Molecular Sequence Data | Crystallography, X-Ray | Serotonin - chemistry | Dopamine Uptake Inhibitors - metabolism | Drosophila Proteins - metabolism | Antidepressive Agents, Tricyclic - chemistry | Neurotransmitter Uptake Inhibitors - metabolism | Desipramine - metabolism | Conserved Sequence | Binding Sites | Dopamine - metabolism | Serotonin Uptake Inhibitors - metabolism | Amino Acid Sequence | Cell Line | Leucine - metabolism | Norepinephrine Plasma Membrane Transport Proteins - antagonists & inhibitors | Models, Molecular | Serotonin Uptake Inhibitors - chemistry | Drosophila Proteins - chemistry | Plasma Membrane Neurotransmitter Transport Proteins - metabolism | Leucine - chemistry | Sequence Homology, Amino Acid | Animals | Norepinephrine - metabolism | Desipramine - chemistry | Neurotransmitter Uptake Inhibitors - chemistry | Norepinephrine - chemistry | Serotonin - metabolism | Dopamine Uptake Inhibitors - chemistry | Protein Binding | Bacterial Proteins - metabolism | Plasma Membrane Neurotransmitter Transport Proteins - chemistry | Protein Conformation | Norepinephrine Plasma Membrane Transport Proteins - metabolism | Norepinephrine Plasma Membrane Transport Proteins - chemistry | Leucine | Structure | Desipramine | Health aspects | Antidepressants, Tricyclic | Inhibitor drugs | Psychiatry | Binding sites
Journal Article
Molecular Cell, ISSN 1097-2765, 10/2009, Volume 36, Issue 1, pp. 39 - 50
In the largest E3 ligase subfamily, Cul3 binds a BTB domain, and an associated protein-interaction domain such as MATH recruits substrates for ubiquitination.... 
PROTEINS | ACTIVATION | PROTEIN | NRF2 | BIOCHEMISTRY & MOLECULAR BIOLOGY | SCF | ADAPTER | DEGRADATION | KEAP1 | DIMERIZATION | BTB DOMAIN | HEDGEHOG | CELL BIOLOGY | Transcription Factors - chemistry | Humans | Crystallography, X-Ray | Drosophila Proteins - metabolism | Mutation - physiology | Protein Multimerization - physiology | Protein Structure, Quaternary - physiology | Ubiquitination - physiology | Peptide Fragments - genetics | Repressor Proteins - metabolism | Amino Acid Sequence | Ubiquitin-Protein Ligases - metabolism | Models, Molecular | Repressor Proteins - genetics | Recombinant Fusion Proteins - chemistry | Nuclear Proteins - chemistry | Ubiquitin-Protein Ligases - chemistry | DNA-Binding Proteins - chemistry | Cullin Proteins - chemistry | Peptide Fragments - chemistry | Phosphoprotein Phosphatases - genetics | Consensus Sequence - physiology | Recombinant Fusion Proteins - genetics | Histones - metabolism | Ubiquitin-Protein Ligases - genetics | Drosophila melanogaster | Phosphoprotein Phosphatases - chemistry | Protein Binding - physiology | Adaptor Proteins, Signal Transducing - chemistry | Histones - chemistry | Protein Interaction Domains and Motifs - physiology | Phosphoprotein Phosphatases - metabolism | Recombinant Fusion Proteins - metabolism | DNA-Binding Proteins - metabolism | Cullin Proteins - metabolism | Nuclear Proteins - genetics | Peptide Fragments - metabolism | Repressor Proteins - chemistry | Nuclear Proteins - metabolism | Drosophila Proteins - chemistry | Transcription Factors - genetics | DNA-Binding Proteins - genetics | Cullin Proteins - genetics | Transcription Factors - metabolism | Animals | Histones - genetics | Adaptor Proteins, Signal Transducing - genetics | Drosophila Proteins - genetics | Adaptor Proteins, Signal Transducing - metabolism | Ubiquitin | Chromatin | Phosphatases | Ligases | CHROMATIN | BASIC BIOLOGICAL SCIENCES | SUBSTRATES | FLEXIBILITY | GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE | LIGASES | DIMERS | PHOSPHATASES
Journal Article
Cell, ISSN 0092-8674, 04/2018, Volume 173, Issue 3, pp. 677 - 692.e20
Journal Article
Molecular Cell, ISSN 1097-2765, 01/2008, Volume 29, Issue 1, pp. 92 - 101
Transcriptional activators, several different coactivators, and general transcription factors are necessary to access specific loci in the dense chromatin... 
DNA | UBIQUITINATION | COMPLEX | ACTIVATION | UBP8 | CHROMATIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | TRANSCRIPTION | UBIQUITYLATION | DEUBIQUITYLATION | MESSENGER-RNA EXPORT | SAGA | CELL BIOLOGY | Transcription Factors - chemistry | p300-CBP Transcription Factors - physiology | Histone Acetyltransferases - chemistry | Humans | Recombinant Fusion Proteins - physiology | Molecular Sequence Data | Trans-Activators - chemistry | Drosophila melanogaster - genetics | Promoter Regions, Genetic - genetics | Trans-Activators - physiology | Drosophila melanogaster - metabolism | Drosophila Proteins - physiology | Endopeptidases - chemistry | Conserved Sequence | Ubiquitination - physiology | p300-CBP Transcription Factors - chemistry | Amino Acid Sequence | Cell Line | Transcription Factors - physiology | Transcription Factors, General - chemistry | Animals, Genetically Modified | Gene Silencing | Thiolester Hydrolases - physiology | RNA Polymerase II - physiology | Drosophila Proteins - chemistry | Transcription Factors - genetics | Histone Acetyltransferases - physiology | Multiprotein Complexes - physiology | Protein Interaction Mapping | Sequence Homology, Amino Acid | Transcription Factors, General - physiology | Multiprotein Complexes - chemistry | Sequence Alignment | Animals | Endopeptidases - genetics | Heterochromatin - genetics | Receptors, Androgen - genetics | Drosophila Proteins - genetics | Thiolester Hydrolases - chemistry | Transcription, Genetic - genetics | Endopeptidases - physiology | Histones | p300-CBP Transcription Factors | Histone Acetyltransferases | Multiprotein Complexes | Receptors, Androgen | Recombinant Fusion Proteins | Life Sciences | Ubiquitination | Heterochromatin | Transcription, Genetic | Promoter Regions (Genetics) | Drosophila Proteins | Transcription Factors, General | Trans-Activators | Biochemistry, Molecular Biology | Thiolester Hydrolases | Transcription Factors | RNA Polymerase II | Drosophila melanogaster | Endopeptidases
Journal Article
The EMBO Journal, ISSN 0261-4189, 06/2011, Volume 30, Issue 12, pp. 2325 - 2335
The Hippo tumour suppressor pathway is a conserved signalling pathway that controls organ size. The core of the Hpo pathway is a kinase cascade, which in... 
hippo signalling | F‐actin | growth regulation | F-actin | TISSUE-GROWTH | BIOCHEMISTRY & MOLECULAR BIOLOGY | YORKIE PHOSPHORYLATION | TEAD/TEF FAMILY | CELL BIOLOGY | REGULATE CELL-PROLIFERATION | SIGNALING PATHWAY | GENE-EXPRESSION | CONTACT INHIBITION | SIZE-CONTROL | TUMOR-SUPPRESSOR PATHWAY | PROMOTES APOPTOSIS | Wings, Animal - cytology | Cell Proliferation | Humans | Drosophila melanogaster - genetics | Actins - genetics | Drosophila Proteins - biosynthesis | Organ Specificity - genetics | Wings, Animal - growth & development | Tumor Suppressor Proteins - chemistry | Tumor Suppressor Proteins - genetics | Actins - chemistry | RNA Caps - antagonists & inhibitors | RNA Caps - chemistry | Intracellular Signaling Peptides and Proteins - genetics | Cytoskeleton - chemistry | RNA Caps - genetics | Actins - biosynthesis | Carrier Proteins - biosynthesis | Cells, Cultured | Cytoskeleton - genetics | Drosophila melanogaster - cytology | Protein-Serine-Threonine Kinases - genetics | Signal Transduction - genetics | Drosophila Proteins - chemistry | Carrier Proteins - genetics | Phenotype | Animals | Drosophila melanogaster - chemistry | Intracellular Signaling Peptides and Proteins - chemistry | Wings, Animal - chemistry | Protein-Serine-Threonine Kinases - chemistry | Drosophila Proteins - genetics | HeLa Cells | Proteins | Signal transduction | Tumors
Journal Article
Journal Article