Search results for "Opsin"

showing 10 items of 95 documents

Induced Night-Vision by Singlet-Oxygen-Mediated Activation of Rhodopsin

2019

In humans, vision is limited to a small fraction of the whole electromagnetic spectrum. One possible strategy for enhancing vision in deep-red or poor-light conditions consists of recruiting chlorophyll derivatives in the rod photoreceptor cells of the eye, as suggested in the case of some deep-sea fish. Here, we employ all-atom molecular simulations and high-level quantum chemistry calculations to rationalize how chlorin e6 (Ce6), widely used in photodynamic therapy although accompanied by enhanced visual sensitivity, mediates vision in the dark, shining light on a fascinating but largely unknown molecular mechanism. First, we identify persistent interaction sites between Ce6 and the extra…

genetic structuresbiology010405 organic chemistrySinglet oxygenPhotoreceptor proteinRetinal010402 general chemistry01 natural sciencesVisual sensitivityeye diseasesTransmembrane protein0104 chemical scienceschemistry.chemical_compoundchemistryRhodopsinNight visionbiology.proteinBiophysics[CHIM]Chemical SciencesGeneral Materials SciencePhysical and Theoretical ChemistryComputingMilieux_MISCELLANEOUSVisual phototransduction
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Rhodopsin transport in the membrane of the connecting cilium of mammalian photoreceptor cells

2000

The transport of the photopigment rhodopsin from the inner segment to the photosensitive outer segment of vertebrate photoreceptor cells has been one of the main remaining mysteries in photoreceptor cell biology. Because of the lack of any direct evidence for the pathway through the photoreceptor cilium, alternative extracellular pathways have been proposed. Our primary aim in the present study was to resolve rhodopsin trafficking from the inner to the outer segment. We demonstrate, predominantly by high-sensitive immunoelectron microscopy, that rhodopsin is also densely packed in the membrane of the photoreceptor connecting cilium. Present prominent labeling of rhodopsin in the ciliary mem…

RhodopsinOpsingenetic structuresPhotoreceptor Connecting CiliumImmunoblottingMolecular Sequence Datamacromolecular substancesMyosinsBiologyPhotoreceptor cellRats Sprague-DawleyMiceRetinal Rod Photoreceptor CellsStructural BiologymedicineAnimalsHumansPhotopigmentAmino Acid SequenceCiliaMicroscopy ImmunoelectronCiliary membraneCiliumRod OpsinsAntibodies MonoclonalDyneinsBiological TransportCell BiologyMiddle AgedRod Cell Outer SegmentActin cytoskeletonImmunohistochemistryActinseye diseasesRatsCell biologyMice Inbred C57BLmedicine.anatomical_structureRhodopsinMyosin VIIabiology.proteinCattleFemalesense organsRetinitis PigmentosaCell Motility and the Cytoskeleton
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Effect of opsin on the shape of the potential energy surfaces at the conical intersection of the Rhodopsin chromophore

2008

Abstract In order to disentangle the role of the protein in the control of the photoisomerization of the chromophore of the visual pigment Rhodopsin, we compare the structure of the ground and excited potential energy surfaces of gas-phase and opsin-embedded 11- cis retinal chromophore at the corresponding (lowest energy) conical intersections. It is shown that, along the branching plane, the asymmetric opsin environment destabilizes one of the ground state relaxation channels emerging from the conical intersection. This suggests that opsin promotes the formation of the product (bathorhodopsin) via enhanced decay probability along the all- trans exit channel. In contrast, in the gas-phase n…

Quantitative Biology::BiomoleculesOpsinbiologyPhotoisomerizationChemistryGeneral Physics and AstronomyConical intersectionChromophorePhotochemistryPotential energyMolecular physicsRhodopsinExcited statebiology.proteinPhysical and Theoretical ChemistryGround stateChemical Physics
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Disruption of the retinitis pigmentosa 28 gene Fam161a in mice affects photoreceptor ciliary structure and leads to progressive retinal degeneration.

2014

Mutations in the FAM161A gene were previously identified as the cause for autosomal-recessive retinitis pigmentosa 28. To study the effects of Fam161a dysfunction in vivo, we generated gene-trapped Fam161a(GT/GT) mice with a disruption of its C-terminal domain essential for protein-protein interactions. We confirmed the absence of the full-length Fam161a protein in the retina of Fam161a(GT/GT) mice using western blots and showed weak expression of a truncated Fam161a protein by immunohistochemistry. Histological analyses demonstrated that photoreceptor segments were disorganized in young Fam161a(GT/GT) mice and that the outer retina was completely lost at 6 months of age. Reactive microglia…

Retinal degenerationMaleOpsinGenotypeVision DisordersAction PotentialsGene ExpressionMice TransgenicRetinal Pigment EpitheliumBiologyRetinaMiceRetinitis pigmentosaGeneticsmedicineAnimalsHumansPhotoreceptor CellsPeripherin 2Eye ProteinsMolecular BiologyGenetics (clinical)Retinal regenerationRetinaGene therapy of the human retinaCiliumRetinal DegenerationGeneral Medicinemedicine.diseaseeye diseasesCell biologyProtein Transportmedicine.anatomical_structureGenetic LociGene TargetingMutationFemalesense organsMicrogliaCarrier ProteinsProtein BindingHuman molecular genetics
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Peripherin-2 differentially interacts with cone opsins in outer segments of cone photoreceptors

2016

Peripherin-2 is a glycomembrane protein exclusively expressed in the light-sensing compartments of rod and cone photoreceptors designated as outer segments (OS). Mutations in peripherin-2 are associated with degenerative retinal diseases either affecting rod or cone photoreceptors. While peripherin-2 has been extensively studied in rods, there is only little information on its supramolecular organization and function in cones. Recently, we have demonstrated that peripherin-2 interacts with the light detector rhodopsin in OS of rods. It remains unclear, however, if peripherin-2 also binds to cone opsins. Here, using a combination of co-immunoprecipitation analyses, transmission electron micr…

0301 basic medicineRhodopsinOpsingenetic structuresmacromolecular substances030105 genetics & heredityBiologymedicine.disease_causeRetinaMice03 medical and health scienceschemistry.chemical_compoundImmunolabelingMicroscopy Electron TransmissionAntigens NeoplasmFluorescence Resonance Energy TransferGeneticsmedicineAnimalsHumansPeripherin 2Molecular BiologyGenetics (clinical)MutationRetinal DegenerationRetinalGeneral MedicineCone Opsinseye diseases030104 developmental biologyFörster resonance energy transfernervous systemchemistryRhodopsinMutationRetinal Cone Photoreceptor CellsBiophysicsbiology.proteinsense organsProtein BindingVisual phototransductionHuman Molecular Genetics
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Molecular genetics of autosomal dominant retinitis pigmentosa (ADRP): a comprehensive study of 43 Italian families

2005

Retinitis pigmentosa is the most common form of retinal degeneration and is heterogeneous both clinically and genetically. The autosomal dominant forms ( ADRP) can be caused by mutations in 12 different genes. This report describes the first simultaneous mutation analysis of all the known ADRP genes in the same population, represented by 43 Italian families. This analysis allowed the identification of causative mutations in 12 of the families (28% of the total). Seven different mutations were identified, two of which are novel (458delC and 6901C --> T (P2301S), in the CRX and PRPF8 genes, respectively). Several novel polymorphisms leading to amino acid changes in the FSCN2, NRL, IMPDH1, and…

Retinal degenerationDNA Mutational Analysismedicine.disease_causeGene FrequencyPrevalenceAge of OnsetSPLICING-FACTOR GENESChildGenetics (clinical)Genes DominantGeneticsMutationeducation.field_of_studyRNA-Binding ProteinsMiddle AgedDNA-Binding ProteinsBasic-Leucine Zipper Transcription FactorsItalyChild PreschoolMESSENGER-RNAMicrotubule-Associated ProteinsRetinitis PigmentosaFORMAdultRhodopsinmedicine.medical_specialtycongenital hereditary and neonatal diseases and abnormalitiesAdolescentPopulationRHODOPSIN GENEBiologyMolecular geneticsRetinitis pigmentosaGeneticsmedicineHumansFamilyEye ProteinseducationGeneAllele frequencyHomeodomain ProteinsMUTATIONSmedicine.diseaseeye diseasesMutationTrans-ActivatorsMutation testingOnline Mutation ReportCarrier Proteins
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Rev-Erb modulates retinal visual processing and behavioral responses to light

2016

International audience; The circadian clock is thought to adjust retinal sensitivity to ambient light levels, yet the involvement of specific clock genes is poorly understood. We explored the potential role of the nuclear receptor subfamily 1, group D, member 1 (REV-ERB; or NR1D1) in this respect. In light-evoked behavioral tests, compared with wild-type littermates, Rev-Erb(-/-) mice showed enhanced negative masking at low light levels (0.1 lx). Rev-Erb(-/-) mouse retinas displayed significantly higher numbers of intrinsically photosensitive retinal ganglion cells (ipRGCs; 62% more compared with wild-type) and more intense melanopsin immunostaining of individual ipRGCs. In agreement with a…

0301 basic medicineRetinal Ganglion CellsLight[SDV]Life Sciences [q-bio]Circadian clockelectroretinogramBiochemistrychemistry.chemical_compound0302 clinical medicinecircadian clockskin and connective tissue diseasesComputingMilieux_MISCELLANEOUSMice KnockoutipRGCsBehavior AnimalphotoreceptorsorganizationCircadian Rhythmmedicine.anatomical_structurerodtranscriptionBiotechnologyPhotopic visionMelanopsinnegative maskingrat retinaBiologyRetina03 medical and health sciences[ SDV.MHEP ] Life Sciences [q-bio]/Human health and pathologyCircadian ClocksGeneticsmedicineAnimalsCircadian rhythmScotopic visionmelanopsin-knockout miceMolecular BiologymouseRetinaIntrinsically photosensitive retinal ganglion cellsRod OpsinsRetinalganglion-cellsbody regionsmammalian retina030104 developmental biologychemistryNuclear Receptor Subfamily 1 Group D Member 1sense organsNeuroscience030217 neurology & neurosurgeryPhotic Stimulation[SDV.MHEP]Life Sciences [q-bio]/Human health and pathology
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Synthesis of the new oligopeptide pyrrole derivative isonetropsin and its one pyrrole unit analogue

2013

We have designed and synthesized isonetropsin and its one pyrrole unit analogue in which the amine and carbonyl groups have been switched in positions 2 and 4, respectively instead of 4 and 2 positions of the natural antibiotic netropsin.

OligopeptideStereochemistryOrganic ChemistryNetropsinBiochemistryPyrrole derivativesDNA minor groove binderchemistry.chemical_compoundDNA minor groove binderschemistryNetropsinmental disordersDrug DiscoveryNetropsin; DNA minor groove binders; Isonetropsin; Oligopeptide pyrroleAmine gas treatingOligopeptide pyrrolepsychological phenomena and processesIsonetropsinPyrroleTetrahedron
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Circadian gene expression patterns of melanopsin and pinopsin in the chick pineal gland

2004

The directly light-sensitive chick pineal gland contains at least two photopigments. Pinopsin seems to mediate the acute inhibitory effect of light on melatonin synthesis, whereas melanopsin may act by phase-shifting the intrapineal circadian clock. In the present study we have investigated, by means of quantitative RT-PCR, the daily rhythm of photopigment gene expression as monitored by mRNA levels. Under a 12-h light/12-h dark cycle, the mRNA levels of both pigments were 5-fold higher in the transitional phase from light to dark than at night, both in vivo and in vitro. Under constant darkness in vivo and in vitro, the peak of pinopsin mRNA levels was attenuated, whereas that of melanopsi…

Melanopsinmedicine.medical_specialtyLightPhotoperiodCircadian clockBiophysicsNerve Tissue ProteinsBiologyPineal GlandBiochemistryAvian ProteinsPineal glandInternal medicineGene expressionmedicineAnimalsPhotopigmentCircadian rhythmMolecular BiologyCells CulturedRegulation of gene expressionAdaptation OcularRod OpsinsCell BiologyCircadian Rhythmmedicine.anatomical_structureEndocrinologyAnimals NewbornGene Expression RegulationLight effects on circadian rhythmsense organsChickensBiochemical and Biophysical Research Communications
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Homology models of melatonin receptors: challenges and recent advances

2013

Melatonin exerts many of its actions through the activation of two G protein-coupled receptors (GPCRs), named MT1 and MT2. So far, a number of different MT1 and MT2 receptor homology models, built either from the prototypic structure of rhodopsin or from recently solved X-ray structures of druggable GPCRs, have been proposed. These receptor models differ in the binding modes hypothesized for melatonin and melatonergic ligands, with distinct patterns of ligand-receptor interactions and putative bioactive conformations of ligands. The receptor models will be described, and they will be discussed in light of the available information from mutagenesis experiments and ligand-based pharmacophore …

Models MolecularProtein Conformationhomology modelingMolecular Sequence DataDruggabilityReviewComputational biologyLigandsBioinformaticsCatalysisInorganic Chemistrylcsh:ChemistryStructure-Activity Relationshipmelatonin receptorsAnimalsHumansAmino Acid SequenceHomology modelingmelatonin receptors; MT1; MT2; homology modeling; structure-activity relationships; docking; molecular dynamics simulationsPhysical and Theoretical ChemistryReceptorMolecular Biologylcsh:QH301-705.5SpectroscopyMelatoninG protein-coupled receptorBinding SitesSequence Homology Amino AcidbiologyReceptor Melatonin MT2Receptor Melatonin MT1MT1Organic ChemistryMT2structure-activity relationshipsGeneral Medicinemolecular dynamics simulationsComputer Science ApplicationsMelatonergiclcsh:Biology (General)lcsh:QD1-999Structural Homology ProteinDocking (molecular)RhodopsindockingMutagenesis Site-Directedbiology.proteinPharmacophore
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