Search results for "opsin"

showing 10 items of 95 documents

Optogenetic Control of Intracellular Signaling: Class II Opsins

2017

Class (computer programming)OpsinChemistryOptogeneticsNeuroscienceIntracellular
researchProduct

Bioaccessibility and decomposition of cylindrospermopsin in vegetables matrices after the application of an in vitro digestion model.

2018

Research on the human exposure to Cylindrospermopsin (CYN) via consumption of contaminated food is of great interest for risk assessment purposes. The aim of this work is to evaluate for the first time the CYN bioaccessibility in contaminated vegetables (uncooked lettuce and spinach, and boiled spinach) after an in vitro digestion model, including the salivar, gastric and duodenal phases and, colonic fermentation under lactic acid bacteria. The results obtained showed that the digestion processes are able to diminish CYN levels, mainly in the colonic phase, especially in combination with the boiling treatment, decreasing CYN levels in a significant way. Moreover, the potential decomposition…

ColonBacterial ToxinsBiological AvailabilityBioaccessibilityFood ContaminationDecomposition products010501 environmental sciencesIn Vitro TechniquesToxicology01 natural sciencesModels Biologicalchemistry.chemical_compound0404 agricultural biotechnologyAlkaloidsLactobacillalesTandem Mass SpectrometryVegetablesHumansFood scienceUracilChromatography High Pressure Liquid0105 earth and related environmental sciencesbiologyCyanobacteria ToxinsChemistryfood and beverages04 agricultural and veterinary sciencesGeneral MedicineSpinachContaminationLettucebiology.organism_classification040401 food scienceDecompositionLactic acidCylindrospermopsinFermentationSpinachFermentationDigestionCylindrospermopsinDigestionBacteriaFood ScienceFood and chemical toxicology : an international journal published for the British Industrial Biological Research Association
researchProduct

Rhodopsin's carboxy-terminal cytoplasmic tail acts as a membrane receptor for cytoplasmic dynein by binding to the dynein light chain Tctex-1.

1999

AbstractThe interaction of cytoplasmic dynein with its cargoes is thought to be indirectly mediated by dynactin, a complex that binds to the dynein intermediate chain. However, the roles of other dynein subunits in cargo binding have been unknown. Here we demonstrate that dynein translocates rhodopsin-bearing vesicles along microtubules. This interaction occurs directly between the C-terminal cytoplasmic tail of rhodopsin and Tctex-1, a dynein light chain. C-terminal rhodopsin mutations responsible for retinitis pigmentosa inhibit this interaction. Our results point to an alternative docking mechanism for cytoplasmic dynein, provide novel insights into the role of motor proteins in the pola…

CytoplasmRhodopsingenetic structuresMicrotubule-associated proteinRecombinant Fusion ProteinsDyneinMolecular Sequence DataReceptors Cell Surfacemacromolecular substancesBiologyT-Complex Genome RegionMicrotubulesGeneral Biochemistry Genetics and Molecular BiologyMotor protein03 medical and health sciencesMice0302 clinical medicineMicrotubuleAnimalsAmino Acid Sequence030304 developmental biologyt-Complex Genome Region0303 health sciencesBinding SitesBiochemistry Genetics and Molecular Biology(all)DyneinsNuclear ProteinsBiological Transport3. Good healthCell biologyCytoplasmRhodopsinMutagenesisDynactinbiology.proteinMicrotubule ProteinsCattlesense organsMicrotubule-Associated Proteins030217 neurology & neurosurgeryPhotoreceptor Cells VertebrateCell
researchProduct

Key roles for freshwater A ctinobacteria revealed by deep metagenomic sequencing

2014

Freshwater ecosystems are critical but fragile environments directly affecting society and its welfare. However, our understanding of genuinely freshwater microbial communities, constrained by our capacity to manipulate its prokaryotic participants in axenic cultures, remains very rudimentary. Even the most abundant components, freshwater Actinobacteria, remain largely unknown. Here, applying deep metagenomic sequencing to the microbial community of a freshwater reservoir, we were able to circumvent this traditional bottleneck and reconstruct de novo seven distinct streamlined actinobacterial genomes. These genomes represent three new groups of photoheterotrophic, planktonic Actinobacteria.…

DNA BacterialMolecular Sequence DatarhodopsinsFresh WaterCyanobacteria633 - Cultivos y producciones [CDU]GenomeFreshwater ecosystemActinobacteriaContig MappingPhylogeneticsRNA Ribosomal 16Slignin degradationGeneticsMicrococcineaePhylogenyEcology Evolution Behavior and SystematicsmetagenomicsbiologyEcologyHigh-Throughput Nucleotide SequencingSequence Analysis DNAbiology.organism_classificationfreshwater reservoirActinobacteriaSpainMetagenomicsMetagenomicsActinomycetalesWater MicrobiologyGenome BacterialGC-contentMolecular Ecology
researchProduct

Interfacial water structure controls protein conformation.

2007

A phenomenological theory of salt-induced Hofmeister phenomena is presented, based on a relation between protein solubility in salt solutions and protein-water interfacial tension. As a generalization of previous treatments, it implies that both kosmotropic salting out and chaotropic salting in are manifested via salt-induced changes of the hydrophobic/hydrophilic properties of protein-water interfaces. The theory is applied to describe the salt-dependent free energy profiles of proteins as a function of their water-exposed surface area. On this basis, three classes of protein conformations have been distinguished, and their existence experimentally demonstrated using the examples of bacter…

DYNAMICSMECHANISMKosmotropicProtein ConformationSURFACE-TENSIONSurface tensionchemistry.chemical_compoundProtein structureMaterials ChemistryPhysical and Theoretical ChemistryPURPLE MEMBRANESPECTROSCOPYbiologySTABILITYBACTERIORHODOPSINMyoglobinSALTTemperatureWaterBacteriorhodopsinSTABILITY MECHANISMSurfaces Coatings and FilmsION SPECIFICITYChaotropic agentCrystallographyMyoglobinchemistryTEMPERATURE-DEPENDENCEChemical physicsStructural stabilityBacteriorhodopsinsbiology.proteinSalting outThermodynamicsThe journal of physical chemistry. B
researchProduct

The effect of water on protein dynamics

2004

Neutron diffraction and spectroscopy were applied to describe the hydration and dynamics of a soluble protein and a natural membrane from extreme halophilic Archaea. The quantitative dependence of protein motions on water activity was clearly illustrated, and it was established that a minimum hydration shell is required for the systems to access their functional resilience, i.e. a dynamics state that allows biological activity.

Dynamical transitionWater activityNeutron diffractionHalophilic malate dehydrogenaseBacteriorhodopsinHydration shellNeutronEuryarchaeotaGeneral Biochemistry Genetics and Molecular BiologyMalate DehydrogenaseSpectroscopySpectrum AnalysibiologyChemistrySpectrum AnalysisProtein dynamicsWaterBacteriorhodopsinPurple membraneAgricultural and Biological Sciences (miscellaneous)Settore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Neutron DiffractionMembraneSolvation shellAgricultural and Biological Sciences (all)BiochemistryChemical physicsBacteriorhodopsinsbiology.proteinBacteriorhodopsinsGeneral Agricultural and Biological SciencesResearch ArticlePhilosophical Transactions of the Royal Society of London. Series B: Biological Sciences
researchProduct

Chapter 17 Muscarinic receptors and cell signalling

1996

Publisher Summary Cells have developed signal transduction mechanisms in order to communicate with the cell exterior. Acetylcholine as an external signal is recognized by nicotinic and muscarinic receptors. This chapter presents various muscarinic receptors belonging to the superfamily of G protein-coupled receptors consisting of seven transmembrane (TM) helices tightly packed in a ring-like structure and arranged in a counter-clockwise fashion. Agonist binding leads to a conformational change of the receptor, thereby activating associated G proteins. Muscarinic stimulation of G proteins leads to the activation or inhibition of ion channels, such as K + and Ca 2+ channels, the activation of…

G proteinHeterotrimeric G proteinMuscarinic acetylcholine receptor M5Muscarinic acetylcholine receptor M2Muscarinic acetylcholine receptor M1BiologyG protein-gated ion channelRhodopsin-like receptorsG protein-coupled receptorCell biology
researchProduct

Transgenic tools for proteomic analysis of ciliary transport

2015

Vision begins as photons are captured by photoreceptor cilia and light is converted into electrical signals that are then sent to the brain. As the photoreceptor cilium is not able to make its own proteins, all polypeptides needed for converting photons into electrical signals are synthetized in the cell body. How these molecules move from the cell body to cilia is still unclear. Opsin is one of the best-characterized transmembrane proteins. Our goal is to understand the mechanism of opsin transport into photoreceptor cilia. In this project, we use a combination of genetic and proteomic approaches in the zebrafish model. As the first step, we are constructing a transgenic line that expresse…

GeneticsOpsingenetic structuresbiologyCiliumTransgeneCre recombinaseCell Biologybiology.organism_classificationeye diseasesTransmembrane proteinOpsin transportGreen fluorescent proteinCell biologyPoster Presentationsense organsZebrafishCilia
researchProduct

Probing a Polar Cluster in the Retinal Binding Pocket of Bacteriorhodopsin by a Chemical Design Approach

2012

Bacteriorhodopsin has a polar cluster of amino acids surrounding the retinal molecule, which is responsible for light harvesting to fuel proton pumping. From our previous studies, we have shown that threonine 90 is the pivotal amino acid in this polar cluster, both functionally and structurally. In an attempt to perform a phenotype rescue, we have chemically designed a retinal analogue molecule to compensate the drastic effects of the T90A mutation in bacteriorhodopsin. This analogue substitutes the methyl group at position C(13) of the retinal hydrocarbon chain by and ethyl group (20-methyl retinal). We have analyzed the effect of reconstituting the wild-type and the T90A mutant apoprotein…

Halobacterium salinarumModels MolecularProtein FoldingProtein Denaturation01 natural sciencesBiotecnologiaBiochemistryBiophysics Simulationschemistry.chemical_compoundSensory RhodopsinsHalobacterium salinarum0303 health sciencesMultidisciplinarybiologyProtein StabilityQRTemperatureUltraviolet-visible spectroscopyThermal stabilityBacterial BiochemistryChemistryBiochemistryBacteriorhodopsinsRetinaldehydeMedicineProtonsResearch ArticleSteric effectsHydrogen bondingBioquímicaProtein StructureScienceRetinal bindingBiophysics010402 general chemistryMicrobiologyPhosphates03 medical and health sciencesBiology030304 developmental biologyAspartic AcidBinding SitesAdaptation OcularOrganic ChemistryOrganic SynthesisProteinsChromoproteinsRetinalBacteriorhodopsinBacteriologyBiological TransportChromophorebiology.organism_classification0104 chemical sciencesTransmembrane ProteinschemistryRetinaldehydeBiophysicsbiology.proteinMutant ProteinsPLoS ONE
researchProduct

Indoor artificial lighting: Prediction of the circadian effects of different spectral power distributions.

2014

The study presented in this paper aims to evaluate if and how the environment affects the circadian impact of a light source by predicting circadian stimulus (CS) resulting from the exposure to different light scenes, using equations reported in studies by Rea et al. The main findings are: (1) Above 600 lx at eye level the increase of CS is little; (2) Between 50 lx and 200 lx at the eye level an increase of only 50 lx determines a significant increase of CS; (3) Light sources with correlated colour temperatures between 2900 K and 4200 K have similar impacts on the circadian system according to the calculation method used; (4) Even an almost neutral environment affects the circadian impact…

Light sourceArtificial lightcircadian stimulus spectral power distribution circadian systemComputer scienceMELATONIN CLOCK PHOTOTRANSDUCTION PHOTORECEPTORS MELANOPSIN RHYTHMS HUMANS ROD circadian effects SPDs light sources non visual effectsAcousticsCircadian rhythmElectrical and Electronic EngineeringStimulus (physiology)RETINAL GANGLION-CELLS SYSTEMElectrical and Electronic Engineering circadian rhythmSimulation
researchProduct