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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 | Nuclear magnetic resonance--NMR | Dengue fever | Homeostasis | Glycoproteins | Hemorrhage | Cells | Index Medicus | 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
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 12/2007, Volume 104, Issue 52, pp. 20749 - 20752
Journal Article
Nature, ISSN 0028-0836, 01/2016, Volume 529, Issue 7587, pp. 541 - 545
Journal Article
Science, ISSN 0036-8075, 11/2012, Volume 338, Issue 6108, pp. 810 - 814
Fluorescent proteins (FPs) are widely used as optical sensors, whereas other light-absorbing domains have been used for optical control of protein localization... 
Proteins | Enzymes | Delta cells | NIH 3T3 cells | REPORTS | Fluorescence | Pseudopodia | Dimers | Cell membranes | Optical control | P branes | SPATIOTEMPORAL CONTROL | ACTIVATION | GTPASES | MULTIDISCIPLINARY SCIENCES | LIGHT | INDUCTION | EXCHANGE FACTORS | LOV DOMAIN | LIVING CELLS | MOTILITY | Darkness | NIH 3T3 Cells | Pseudopodia - ultrastructure | Native Polyacrylamide Gel Electrophoresis | Humans | Protein Multimerization | Adaptor Proteins, Vesicular Transport - genetics | Optogenetics | Adaptor Proteins, Vesicular Transport - metabolism | Recombinant Fusion Proteins - metabolism | Viral Nonstructural Proteins - chemistry | Light | Protein Engineering | Serine Endopeptidases - genetics | Luminescent Proteins - chemistry | Adaptor Proteins, Vesicular Transport - chemistry | Cell Membrane - metabolism | Protein Structure, Tertiary | Models, Molecular | Viral Nonstructural Proteins - genetics | Serine Endopeptidases - chemistry | Recombinant Fusion Proteins - chemistry | Animals | Pseudopodia - metabolism | Recombinant Fusion Proteins - genetics | Luminescent Proteins - genetics | Protein Conformation | Viral Nonstructural Proteins - metabolism | Mice | Serine Endopeptidases - metabolism | HeLa Cells | Luminescent Proteins - metabolism | Physiological aspects | Photoreception | Research | Fluorescent proteins | Sensors | Cellular biology | Index Medicus | Activated | Exposure | Optical sensors | Detection
Journal Article
Journal Article
PLoS ONE, ISSN 1932-6203, 10/2012, Volume 7, Issue 10, pp. e46039 - e46039
A highly crystallizable T4 lysozyme (T4L) was fused to the N-terminus of the beta(2) adrenergic receptor (beta(2)AR), a G-protein coupled receptor (GPCR) for... 
COMPLEX | ANTAGONIST | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | GPCR | BETA-ADRENERGIC RECEPTOR | MUSCARINIC ACETYLCHOLINE-RECEPTOR | Protein Engineering - methods | Receptors, G-Protein-Coupled - metabolism | Humans | Molecular Sequence Data | Crystallography, X-Ray | Tritium | Recombinant Fusion Proteins - metabolism | Viral Proteins - metabolism | Receptors, Adrenergic, beta-2 - chemistry | Sf9 Cells | Bacteriophage T4 - enzymology | Binding Sites | Binding, Competitive | Protein Structure, Tertiary | Amino Acid Sequence | Protein Structure, Secondary | Muramidase - chemistry | Receptors, Adrenergic, beta-2 - genetics | Viral Proteins - chemistry | Muramidase - genetics | Crystallization | Models, Molecular | Viral Proteins - genetics | Muramidase - metabolism | Recombinant Fusion Proteins - chemistry | Receptors, Adrenergic, beta-2 - metabolism | Animals | Dihydroalprenolol - metabolism | Protein Binding | Recombinant Fusion Proteins - genetics | Dihydroalprenolol - chemistry | Protein Conformation | Receptors, G-Protein-Coupled - genetics | Mutation | Receptors, G-Protein-Coupled - chemistry | Proteins | Lysozyme | G proteins | Protein engineering | G protein-coupled receptors | Crystal lattices | Science | Catecholamines | Crystallography | Medicine | Signaling | N-Terminus | Chemical bonds | Adrenergic receptors | Physiology | Crystal structure | Index Medicus
Journal Article
Science, ISSN 0036-8075, 12/2012, Volume 338, Issue 6114, pp. 1634 - 1637
The influenza viruses cause annual epidemics of respiratory disease and occasional pandemics, which constitute a major public-health issue. The segmented... 
Pandemics | RNA | Particle interactions | Virions | REPORTS | Ribonucleoproteins | Orthomyxoviridae | Viruses | Viral morphology | Atomic structure | Monomers | LOCALIZATION | NUCLEAR | REPLICATION | PARTICLES | RECONSTRUCTION | MULTIDISCIPLINARY SCIENCES | COMPLEXES | POLYMERASE | A VIRUS NUCLEOPROTEIN | OLIGOMERIZATION | Viral Core Proteins - ultrastructure | RNA Replicase - metabolism | Influenza A Virus, H1N1 Subtype - physiology | Virion - chemistry | Viral Proteins - metabolism | Influenza A Virus, H1N1 Subtype - ultrastructure | RNA Replicase - ultrastructure | Cell Nucleus - metabolism | Cell Nucleus - virology | Madin Darby Canine Kidney Cells | Viral Core Proteins - metabolism | Transcription, Genetic | RNA, Viral - metabolism | Ribonucleoproteins - chemistry | Viral Core Proteins - chemistry | Protein Structure, Secondary | Electron Microscope Tomography | Viral Proteins - chemistry | RNA-Binding Proteins - chemistry | Models, Molecular | Ribonucleoproteins - metabolism | Viral Proteins - ultrastructure | Microscopy, Electron | Cryoelectron Microscopy | RNA-Binding Proteins - ultrastructure | Animals | RNA, Viral - chemistry | Image Processing, Computer-Assisted | RNA Replicase - chemistry | Virion - ultrastructure | Protein Conformation | Influenza A Virus, H1N1 Subtype - chemistry | Ribonucleoproteins - ultrastructure | RNA-Binding Proteins - metabolism | Influenza viruses | Properties | RNA-protein interactions | Influenza | Genomics | Virology | Index Medicus | Ribonucleic acids | Mortality | Replication | Genomes | Online | Assembly
Journal Article
Journal of Molecular Biology, ISSN 0022-2836, 09/2015, Volume 427, Issue 19, pp. 3031 - 3041
Journal Article
Journal Article
Molecular Cell, ISSN 1097-2765, 2005, Volume 20, Issue 6, pp. 939 - 949
The death-inducing signaling complex (DISC) comprising Fas, Fas-associated death domain (FADD), and caspase-8/10 is assembled via homotypic associations... 
RECEPTOR SIGNALS | APOPTOSIS | INDUCED-PROXIMITY MODEL | BIOCHEMISTRY & MOLECULAR BIOLOGY | NMR STRUCTURE | DEATH-EFFECTOR DOMAIN | CASPASE ACTIVATION | CONTAINING PROTEIN | SIGNALING COMPLEX DISC | CELL-DEATH | PYRIN DOMAIN | CELL BIOLOGY | Caspase 8 | Humans | Multiprotein Complexes | Molecular Sequence Data | Crystallography, X-Ray | Intracellular Signaling Peptides and Proteins - metabolism | fas Receptor - metabolism | Viral Proteins - metabolism | Death Domain Receptor Signaling Adaptor Proteins | Caspases - metabolism | Molluscum contagiosum virus - genetics | Caspase 10 | fas Receptor - genetics | Intracellular Signaling Peptides and Proteins - genetics | Amino Acid Sequence | Caspases - genetics | Viral Proteins - chemistry | Intracellular Signaling Peptides and Proteins - antagonists & inhibitors | Models, Molecular | Viral Proteins - genetics | Fas-Associated Death Domain Protein | Tumor Necrosis Factor Receptor-Associated Peptides and Proteins - metabolism | Tumor Necrosis Factor Receptor-Associated Peptides and Proteins - chemistry | Sequence Alignment | Animals | Intracellular Signaling Peptides and Proteins - chemistry | Adaptor Proteins, Signal Transducing - genetics | Molluscum contagiosum virus - chemistry | Protein Conformation | CASP8 and FADD-Like Apoptosis Regulating Protein | Apoptosis - physiology | Mutation | Adaptor Proteins, Signal Transducing - metabolism | Proteins | Oligomers | Structure | Crystals | Index Medicus
Journal Article