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Biochemical Journal, ISSN 0264-6021, 02/2013, Volume 449, Issue 3, pp. 613 - 621
The ASC (apoptosis speck-like protein) is a key component of multimeric protein complexes that mediate inflammation and host defence. Comprising a PYD (Pyrin)... 
Salmonella | Caspase activation and recruitment domain (CARD) | Inflammatory cytokine | Nucleotide-binding domain | Death domain | Signalling platform formation | Innate immunity | Caspase 1 | Inflammasome | Leucine-rich repeat-containing receptor (NLR) | NLR family CARD domain-containing protein 4 (NLRC4) | IMMUNITY | ACTIVATION | CASPASE-1 | INTERLEUKIN-1-BETA | BIOCHEMISTRY & MOLECULAR BIOLOGY | caspase 1 | PYROPTOSOME | IDENTIFICATION | IPAF | caspase activation and recruitment domain (CARD) | CELL-DEATH | inflammatory cytokine | innate immunity | leucine-rich repeat-containing receptor (NLR) | inflammasome | DISEASE | signalling platform formation | death domain | nucleotide-binding domain | Inflammasomes - metabolism | Cytoskeletal Proteins - genetics | NLR Family, Pyrin Domain-Containing 3 Protein | Humans | Caspase 1 - metabolism | Multiprotein Complexes - genetics | CARD Signaling Adaptor Proteins - genetics | Multiprotein Complexes - metabolism | CARD Signaling Adaptor Proteins - metabolism | Calcium-Binding Proteins - immunology | Interleukin-1beta - metabolism | HEK293 Cells | Cytoskeletal Proteins - metabolism | Mutant Proteins - immunology | DNA-Binding Proteins | Calcium-Binding Proteins - chemistry | Calcium-Binding Proteins - metabolism | CARD Signaling Adaptor Proteins - immunology | Cell Line | Salmonella typhimurium - immunology | Salmonella typhimurium - pathogenicity | Signal Transduction | Inflammasomes - chemistry | Mutant Proteins - genetics | Models, Molecular | Mutant Proteins - metabolism | Nuclear Proteins - metabolism | Cytoskeletal Proteins - chemistry | Immunity, Innate | Inflammasomes - genetics | Multiprotein Complexes - chemistry | Animals | Carrier Proteins - metabolism | Cytoskeletal Proteins - immunology | Inflammasomes - immunology | Mutant Proteins - chemistry | CARD Signaling Adaptor Proteins - chemistry | Mice | HeLa Cells | Calcium-Binding Proteins - genetics | Index Medicus | signaling platform formation | inflammatory cytokines | NLRC4 | death domains | CARD | Caspase-1 | Nod-like receptors (NLRs)
Journal Article
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 03/2016, Volume 291, Issue 13, pp. 6664 - 6678
Perilipins (PLINs) play a key role in energy storage by orchestrating the activity of lipases on the surface of lipid droplets. Failure of this activity... 
lipid droplet | ADIPOSE TRIGLYCERIDE LIPASE | membrane targeting | membrane | HORMONE-SENSITIVE LIPASE | PARTIAL LIPODYSTROPHY | BIOCHEMISTRY & MOLECULAR BIOLOGY | 11-mer repeat | amphipathic helix | ALPHA-SYNUCLEIN | CELLULAR FAT STORES | perilipin | monolayer | SECONDARY STRUCTURE ANALYSES | ENDOPLASMIC-RETICULUM | lipolysis | phospholipid | DIFFERENTIATION-RELATED PROTEIN | POSTTRANSLATIONAL REGULATION | lipodystrophy | Saccharomyces cerevisiae - genetics | Vesicular Transport Proteins - metabolism | Humans | Cercopithecus aethiops | Molecular Sequence Data | Saccharomyces cerevisiae - ultrastructure | Phosphoproteins - metabolism | Phosphoproteins - chemistry | Saccharomyces cerevisiae - metabolism | Biological Transport | Micelles | Carrier Proteins - chemistry | Membrane Proteins - metabolism | Protein Interaction Domains and Motifs | Lipid Droplets - metabolism | Transgenes | Binding Sites | Lipid Droplets - chemistry | Recombinant Proteins - metabolism | Amino Acid Sequence | Gene Expression | Protein Structure, Secondary | Membrane Proteins - genetics | Vesicular Transport Proteins - genetics | Models, Molecular | Recombinant Proteins - chemistry | Vesicular Transport Proteins - chemistry | Recombinant Proteins - genetics | Phosphoproteins - genetics | Protein Transport | Carrier Proteins - genetics | Sequence Alignment | Animals | Carrier Proteins - metabolism | Membrane Proteins - chemistry | Hydrophobic and Hydrophilic Interactions | Protein Binding | Mutation | COS Cells | Perilipin-3 | Perilipin-2 | Perilipin-1 | Index Medicus | Membrane Biology
Journal Article
Journal Article
Cell, ISSN 0092-8674, 12/2012, Volume 151, Issue 6, pp. 1200 - 1213
Journal Article
Molecular Biology of the Cell, ISSN 1059-1524, 09/2008, Volume 19, Issue 9, pp. 3871 - 3884
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 08/2017, Volume 292, Issue 34, pp. 14280 - 14289
The visual photo-transduction cascade is a prototypical G protein-coupled receptor (GPCR) signaling system, in which light-activated rhodopsin (Rho*) is the... 
SMALL-ANGLE SCATTERING | ALPHA-SUBUNIT | signal transduction | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | COUPLED RECEPTOR | 7-helix receptor | ADRENERGIC-RECEPTOR | SAXS | rhodopsin | MONOMERIC RHODOPSIN | photo-transduction | HIGH-RESOLUTION | G protein-coupled receptor (GPCR) | G-protein | structural biology | transducin | MEMBRANE-PROTEINS | ARRESTIN-1 BINDING | Rhodopsin - isolation & purification | Recombinant Fusion Proteins - isolation & purification | Retina - metabolism | Rod Cell Outer Segment - metabolism | Detergents - chemistry | Eye Proteins - chemistry | Eye Proteins - isolation & purification | Crystallography, X-Ray | Rhodopsin - metabolism | Recombinant Fusion Proteins - metabolism | Cattle | Retina - enzymology | X-Ray Diffraction | Light | GTP-Binding Protein beta Subunits - isolation & purification | Transducin - metabolism | Eye Proteins - genetics | GTP-Binding Protein beta Subunits - metabolism | Protein Stability - radiation effects | Peptide Fragments - genetics | Rod Cell Outer Segment - radiation effects | Protein Multimerization - radiation effects | Rhodopsin - chemistry | Retina - radiation effects | Transducin - isolation & purification | Transducin - genetics | GTP-Binding Protein gamma Subunits - metabolism | Peptide Fragments - metabolism | GTP-Binding Protein gamma Subunits - chemistry | Peptide Fragments - isolation & purification | Solubility | Models, Molecular | Scattering, Small Angle | Recombinant Fusion Proteins - chemistry | Microscopy, Electron | Transducin - chemistry | GTP-Binding Protein beta Subunits - chemistry | Peptide Fragments - chemistry | Animals | Protein Conformation - radiation effects | Eye Proteins - metabolism | GTP-Binding Protein gamma Subunits - isolation & purification | Rod Cell Outer Segment - enzymology | Index Medicus | Editors' Picks
Journal Article
GENES & DEVELOPMENT, ISSN 0890-9369, 03/2018, Volume 32, Issue 5-6, pp. 389 - 401
Cis-regulatory modules (CRMs) are defined by unique combinations of transcription factor-binding sites. Emerging evidence suggests that the number, affinity,... 
TRANSCRIPTION FACTORS | STRUCTURAL INSIGHTS | SITE | heart development | DNA-BINDING | DEVELOPMENTAL BIOLOGY | Drosophila embryogenesis | even-skipped | DROSOPHILA EMBRYONIC MESODERM | cis-regulatory syntax | CHROMATIN OCCUPANCY | CELL BIOLOGY | SWISS-MODEL | SELF-ASSOCIATION | ETS transcription factor | PATHWAY | GENETICS & HEREDITY | receptor tyrosine kinase | EYE DEVELOPMENT | Drosophila melanogaster - embryology | Transcription Factors - chemistry | Homeodomain Proteins - metabolism | Eye Proteins - chemistry | Gene Expression Regulation, Developmental - genetics | Proto-Oncogene Proteins - chemistry | Drosophila Proteins - metabolism | Drosophila melanogaster - genetics | DNA-Binding Proteins - metabolism | Cell Differentiation - genetics | Nerve Tissue Proteins - chemistry | Protein Structure, Quaternary | Eye Proteins - genetics | Repressor Proteins - metabolism | Proto-Oncogene Proteins - metabolism | Repressor Proteins - chemistry | Drosophila melanogaster - cytology | Models, Molecular | Repressor Proteins - genetics | Proto-Oncogene Proteins - genetics | Drosophila Proteins - chemistry | Transcription Factors - genetics | DNA-Binding Proteins - genetics | Homeodomain Proteins - chemistry | DNA-Binding Proteins - chemistry | Nerve Tissue Proteins - genetics | Homeodomain Proteins - genetics | Myocardium - cytology | Protein Transport | Nerve Tissue Proteins - metabolism | Transcription Factors - metabolism | Animals | Eye Proteins - metabolism | Organogenesis - genetics | Embryo, Nonmammalian | Protein Binding | Enhancer Elements, Genetic - genetics | Drosophila Proteins - genetics | Index Medicus | Research Paper
Journal Article
Protein Science, ISSN 0961-8368, 12/2016, Volume 25, Issue 12, pp. 2196 - 2208
Protein:protein interactions play key functional roles in the molecular machinery of the cell. A major challenge for structural biology is to gain... 
protein‐protein interaction | YFP | BiFC | aquaporin | calmodulin | Saccharomyces cerevisiae | membrane protein complex | protein-protein interaction | EUKARYOTIC MEMBRANE-PROTEINS | BIOCHEMISTRY & MOLECULAR BIOLOGY | SACCHAROMYCES-CEREVISIAE | YEAST | OVEREXPRESSION | PURIFICATION | PICHIA-PASTORIS | EXPRESSION | VECTORS | BINDING | Calmodulin - genetics | Saccharomyces cerevisiae - genetics | Humans | Aquaporins - chemistry | Bacterial Proteins - chemistry | Eye Proteins - chemistry | Eye Proteins - isolation & purification | Aquaporins - biosynthesis | Recombinant Proteins - biosynthesis | Calmodulin - isolation & purification | Genetic Complementation Test | Aquaporins - genetics | Luminescent Proteins - biosynthesis | Recombinant Proteins - isolation & purification | Saccharomyces cerevisiae - metabolism | Luminescent Proteins - chemistry | Eye Proteins - genetics | Calmodulin - chemistry | Calmodulin - biosynthesis | Bacterial Proteins - genetics | Aquaporin 1 - isolation & purification | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Aquaporin 1 - chemistry | Aquaporin 1 - genetics | Aquaporin 1 - biosynthesis | Aquaporins - isolation & purification | Luminescent Proteins - genetics | Bacterial Proteins - biosynthesis | Luminescent Proteins - isolation & purification | Bacterial Proteins - isolation & purification | Eye Proteins - biosynthesis | Fluorescence | Aquaporins | Calmodulin | Protein-protein interactions | Blood proteins | Proteins | Visualization | High resolution | Molecular machinery | Protein purification | Biology | Crystallography | Machinery | Fragmentation | X-ray crystallography | Functional anatomy | Calcium-binding protein | Aquaporin 1 | Construction | Yellow fluorescent protein | Purification | Fragments | C-Terminus | Electron microscopy | Membrane proteins | Screening | Protein interaction | Structural analysis | Index Medicus | Biochemistry and Molecular Biology | Biokemi och molekylärbiologi | Annan kemi | Other Chemistry Topics
Journal Article
FEBS Journal, ISSN 1742-464X, 08/2015, Volume 282, Issue 16, pp. 3175 - 3189
Drosophila melanogaster cryptochrome is one of the model proteins for animal blue‐light photoreceptors. Using time‐resolved and steady‐state optical... 
blue‐light photoreceptor | proton‐transfer reaction | time resolved optical spectroscopy | flavoprotein | cryptochrome | proton-transfer reaction | blue-light photoreceptor | ACTIVE-SITE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | DROSOPHILA CRYPTOCHROME | COLI DNA PHOTOLYASE | CYTOCHROME-C | REDOX STATES | TRANSFORM INFRARED-SPECTROSCOPY | ULTRAFAST DYNAMICS | INDUCED ELECTRON-TRANSFER | Flavin-Adenine Dinucleotide - chemistry | Protons | Free Radicals - radiation effects | Electron Transport | Cryptochromes - radiation effects | Cryptochromes - genetics | Eye Proteins - chemistry | Tryptophan - chemistry | Deoxyribodipyrimidine Photo-Lyase - metabolism | Drosophila melanogaster - genetics | Drosophila Proteins - radiation effects | Photochemical Processes | Light | Recombinant Proteins - radiation effects | Eye Proteins - genetics | Deoxyribodipyrimidine Photo-Lyase - chemistry | Deoxyribodipyrimidine Photo-Lyase - genetics | Mutagenesis, Site-Directed | Oxidation-Reduction | Free Radicals - chemistry | Models, Molecular | Recombinant Proteins - chemistry | Escherichia coli Proteins - metabolism | Recombinant Proteins - genetics | Drosophila Proteins - chemistry | Animals | Drosophila melanogaster - chemistry | Eye Proteins - radiation effects | Escherichia coli Proteins - genetics | Cryptochromes - chemistry | Drosophila Proteins - genetics | Escherichia coli Proteins - chemistry | Spectrophotometry | Amino Acid Substitution | Proteins | Tryptophan | Chemical properties | Fruit-flies | Analysis | Spectrum analysis | Amino acids | Kinetics | Biophysics | Index Medicus
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 9/2016, Volume 113, Issue 36, pp. 10073 - 10078
Cryptochrome (CRY) is the principal light sensor of the insect circadian clock. Photoreduction of the CRY (dCRY) flavin cofactor to the anionic semiquinone... 
Molecular dynamics | Redox | Flavoprotein | Light sensing | Photochemistry | MOLECULAR-DYNAMICS | MECHANISM | MULTIDISCIPLINARY SCIENCES | DROSOPHILA CRYPTOCHROME | PLANT CRYPTOCHROME | FLAVIN COFACTOR | molecular dynamics | light sensing | redox | BLUE-LIGHT PHOTORECEPTORS | photochemistry | ROLES | flavoprotein | PHOTOLYASE | ELECTROSTATICS | PROTEINS | Protons | Cryptochromes - genetics | Eye Proteins - chemistry | Crystallography, X-Ray | Benzoquinones - chemistry | Circadian Clocks - genetics | Histidine - metabolism | Drosophila Proteins - metabolism | Drosophila melanogaster - genetics | Drosophila melanogaster - metabolism | Light | Protein Interaction Domains and Motifs | Eye Proteins - genetics | Benzoquinones - metabolism | Cryptochromes - metabolism | Recombinant Proteins - metabolism | Protein Conformation, alpha-Helical | Catalytic Domain | Gene Expression | Oxidation-Reduction | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Drosophila Proteins - chemistry | Molecular Dynamics Simulation | Amino Acid Motifs | Animals | Eye Proteins - metabolism | Hydrogen Bonding | Protein Conformation, beta-Strand | Protein Binding | Flavins - chemistry | Cryptochromes - chemistry | Drosophila Proteins - genetics | Histidine - chemistry | Flavins - metabolism | Hydrogen-Ion Concentration | Histidine | Observations | Binding proteins | Health aspects | Hydrogen bonding | Proteins | Genetics | Circadian rhythm | Hydrogen bonds | Insects | Index Medicus | Biological Sciences | Physical Sciences
Journal Article
Journal Article