Search results for "Lins"

showing 10 items of 460 documents

Three-Dimensional Printing of Nonlinear Optical Lenses.

2018

In the current paper, a series of nonlinear optical (NLO) active devices was prepared by utilizing stereolithographic three-dimensional printing technique. Microcrystalline NLO active component, urea, or potassium dihydrogen phosphate was dispersed in a simple photopolymerizable polyacrylate-based resin and used as the printing material to fabricate highly efficient transparent NLO lenses. The nonlinear activity of the printed lenses was confirmed by second-harmonic generation measurements using a femtosecond laser-pumped optical parametric amplifier operating at a wavelength of 1195 nm. The three-dimensional printing provides a simple method to utilize a range of NLO active compounds witho…

Materials scienceGeneral Chemical Engineeringlinssit (optiikka)Crystal growth010402 general chemistry01 natural sciencesnonlinear optical lensesArticlelcsh:ChemistryNonlinear optical3D-tulostusthree-dimensional printingta216ta116ta114010405 organic chemistrybusiness.industryGeneral ChemistryOptical parametric amplifier0104 chemical sciencesWavelengthNonlinear systemMicrocrystallinelcsh:QD1-999Three dimensional printingFemtosecondOptoelectronicsbusinessACS omega
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A genome-wide association study of marginal zone lymphoma shows association to the HLA region

2015

Marginal zone lymphoma (MZL) is the third most common subtype of B-cell non-Hodgkin lymphoma. Here we perform a two-stage GWAS of 1,281 MZL cases and 7,127 controls of European ancestry and identify two independent loci near BTNL2 (rs9461741, P=3.95 × 10−15) and HLA-B (rs2922994, P=2.43 × 10−9) in the HLA region significantly associated with MZL risk. This is the first evidence that genetic variation in the major histocompatibility complex influences MZL susceptibility.

Medicin och hälsovetenskapLymphomaResearch Support U.S. Gov't P.H.S.Follicular lymphomaGeneral Physics and AstronomyGenome-wide association studyMarginal ZoneP.H.S.Medical and Health SciencesMajor Histocompatibility ComplexPolymorphism (computer science)Non-U.S. Gov'tGENE-EXPRESSIONCELL DEVELOPMENTGeneticsMultidisciplinaryMembrane GlycoproteinsResearch Support Non-U.S. Gov'tSingle NucleotideMarginal zone3. Good healthMultidisciplinary SciencesScience & Technology - Other TopicsNON-HODGKIN-LYMPHOMASUSCEPTIBILITY LOCIGenotypeCèl·lules BEuropean Continental Ancestry GroupEPIDEMIOLOGIC RESEARCHHuman leukocyte antigenBiologyResearch SupportPolymorphism Single NucleotideCLASSIFICATIONGeneral Biochemistry Genetics and Molecular BiologyWhite PeopleArticleN.I.H.Research Support N.I.H. ExtramuralMarginal zone lymphomaMD MultidisciplinaryGenetic variationmedicineJournal ArticleHumansPolymorphismGASTRIC LYMPHOMAIntramuralB cellsScience & TechnologyButyrophilinsGastric lymphomaB-CellExtramuralComputational BiologyGeneral ChemistryLymphoma B-Cell Marginal ZoneResearch Support N.I.H. Intramuralmedicine.diseaseRISK LOCIRHEUMATOID-ARTHRITISLymphomaMalaltia de HodgkinImmunologyU.S. Gov'tHodgkin's diseaseFOLLICULAR LYMPHOMAGenome-Wide Association Study
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Thermal induced conformational changes involved in the aggregation pathways of beta-lactoglobulin.

2004

Aggregation of proteins appears to be associated most often with conformational and structural changes that lead to exposure of some apolar residues. Depending on the native structure of the protein in exam, aggregation is a process that involves different mechanisms, whose time of occurrence and interplay can depend upon temperature. To single out information about the multistages of the aggregation pathway, here we investigate the thermally induced conformational and structural changes of the beta-lactoglobulin (BLG). The experimental approach consists in studying steady-state fluorescence spectra of intrinsic chromophores, two tryptophans, and Anylino-Naphthalene-Sulfonate dye (ANS) mole…

Models MolecularCircular dichroismProtein DenaturationChemistryProtein ConformationSpectrum AnalysisOrganic ChemistryKineticsIntermolecular forceBiophysicsTemperatureLactoglobulinsProtein aggregationChromophoreCrystallography X-RayBiochemistryFluorescenceHydrophobic effectCrystallographyKineticsProtein structureBiophysicsDimerizationBiophysical chemistry
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Nuclear magnetic resonance spectroscopic study of beta-lactoglobulin interactions with two flavor compounds, gamma-decalactone and beta-ionone.

2002

Interactions between a well-characterized protein, beta-lactoglobulin, and two flavor compounds, beta-ionone and gamma-decalactone, were studied by 2D NMR spectroscopy. NMR spectra were recorded in aqueous solution (pH 2.0, 12 mM NaCl, 10% D(2)O) under conditions such that beta-lactoglobulin is present in a monomeric state. TOCSY and NOESY spectra were recorded on the protein and the complexes between protein and ligands. The spectra of the NH-CH(alpha) region showed the cross-signals due to the coupling between N- and C-bonded protons in the polypeptide backbone. The observed chemical shift variations in the presence of ligands can be assigned to changes in the protein conformation. It app…

Models MolecularKetoneMagnetic Resonance SpectroscopyStereochemistryProtein ConformationLactoglobulinsIononechemistry.chemical_compoundLactonesSpectroscopyBeta-lactoglobulinFlavorchemistry.chemical_classificationBinding SitesbiologyMolecular StructureTerpenesGeneral ChemistryNuclear magnetic resonance spectroscopyNMR spectra databasechemistryOdorantsbiology.proteinPhysical chemistryGeneral Agricultural and Biological SciencesNorisoprenoidsTwo-dimensional nuclear magnetic resonance spectroscopyJournal of agricultural and food chemistry
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Oxytocin receptors and cholesterol: interaction and regulation.

2000

Cholesterol affects the ligand binding function of the oxytocin receptor in a highly specific manner. While the structurally-related cholecystokinin receptor shows a strong correlation between the membrane fluidity and its binding function, the oxytocin receptor behaves differently. A stringent and unique requirement of the affinity state of the oxytocin receptor for structural features of the sterol molecule has been found. The molecular requirements differ both from those postulated for sterol-phospholipid interactions and from those known to be necessary for the activity of other proteins. Employing a new detergent-free subcellular fractionation protocol, a two-fold enrichment of the oxy…

Models MolecularMembrane FluidityCaveolin 1Green Fluorescent ProteinsBiologyKidneyTransfectionCholecystokinin receptorCaveolinsGenes ReportermedicineMembrane fluidityExtracellularHumansReceptorCells CulturedBinding SitesCholesterol bindingCell MembraneMembrane ProteinsGeneral MedicineOxytocin receptorRecombinant ProteinsLuminescent ProteinsMembraneCholesterolOxytocinBiochemistryReceptors OxytocinBiophysicsIndicators and ReagentsReceptors CholecystokininSteroidshormones hormone substitutes and hormone antagonistsmedicine.drugExperimental physiology
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Structure of rat odorant-binding protein OBP1 at 1.6 angstrom resolution

2009

The nasal mucosa is a specialist interfacial region sandwiched between the olfactory system and the gaseous chemical milieu. In mammals and insects, this region is rich in odorant-binding proteins that are thought to aid olfaction by assisting mass transfer of the many different organoleptic compounds that make up the olfactory landscape. However, in mammals at least, our grasp on the exact function of odorant-binding proteins is tentative and better insight into the role of these proteins is warranted, not least because of their apparent significance in the olfactory systems of insects. Here, the crystal structure of rat odorant-binding protein 1 is reported at 1.6 Å resolution. This prote…

Models MolecularOlfactory systemCristallographyProtein ConformationRecombinant Fusion ProteinsMolecular Sequence DataOlfactionOBP1Crystallography X-RayReceptors Odorant010402 general chemistry01 natural sciencesPheromonesPichia pastoris03 medical and health sciences[ CHIM.CRIS ] Chemical Sciences/CristallographyProtein structureSpecies SpecificityStructural BiologyODORANT-BINDING PROTEINS[CHIM.CRIS]Chemical Sciences/CristallographyAnimalsAmino Acid SequencePeptide sequence030304 developmental biology0303 health sciencesBinding SitesSequence Homology Amino AcidbiologyProteinsGeneral MedicineLigand (biochemistry)biology.organism_classificationLipocalinsRatsCristallographie0104 chemical sciencesTransport proteinDNA-Binding ProteinsBiochemistryOdorant-binding proteinbiology.proteinODORANT-BINDING PROTEINS;OBP1Sequence Alignment
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2NH and 3OH are crucial structural requirements in sphingomyelin for sticholysin II binding and pore formation in bilayer membranes.

2013

AbstractSticholysin II (StnII) is a pore-forming toxin from the sea anemone Stichodactyla heliantus which belongs to the large actinoporin family. The toxin binds to sphingomyelin (SM) containing membranes, and shows high binding specificity for this lipid. In this study, we have examined the role of the hydrogen bonding groups of the SM long-chain base (i.e., the 2NH and the 3OH) for StnII recognition. We prepared methylated SM-analogs which had reduced hydrogen bonding capability from 2NH and 3OH. Both surface plasmon resonance experiments, and isothermal titration calorimetry measurements indicated that StnII failed to bind to bilayers containing methylated SM-analogs, whereas clear bind…

Models MolecularPore Forming Cytotoxic ProteinsMembrane permeabilizationLipid BilayersBiophysicsCalorimetryta3111Biochemistrychemistry.chemical_compoundCnidarian VenomsAnimalsComputer SimulationLipid bilayerta116Binding selectivityUnilamellar LiposomesPhosphocholineBinding SitesMolecular StructureChemistryHydrogen bondVesicleta1182Isothermal titration calorimetryHydrogen BondingCell BiologySurface Plasmon ResonanceProtein Structure TertiarySphingomyelinsKineticsMembraneSea AnemonesBiochemistryMolecular dockingIsothermal titration calorimetryBiophysicsPhosphatidylcholinesSphingomyelinProtein BindingBiochimica et biophysica acta
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Effect of beta-lactoglobulin polymorphism on milk-related traits of dairy ewes analysed by a repeated measures design.

2000

Among specific genes that may affect economically important traits in sheep, the β-lactoglobulin (LGB) locus has been extensively studied. Polymorphism has been detected in several breeds, but studies of the effect of LGB alleles on milk production traits have given conflicting results. Some found that LGB polymorphism significantly affects milk yield (Bolla et al. 1989; Herget et al. 1995; Fraghì et al. 1996), fat and protein content (Garzon & Martínez 1992; Giaccone et al. 1997; Kukovics et al. 1998), only fat content (Pirisi et al. 1998) and cheese yield and composition (Di Stasio et al. 1997; Rampilli et al. 1997). However, other studies failed to detect any effect of the gene on mi…

Models StatisticalPolymorphism GeneticSheepGenotypeLinear modelRepeated measures designGeneral MedicineLactoglobulinsCovarianceBiologyBreedCorrelationmedicine.anatomical_structureMilkLactationStatisticsmedicineAnimalsRegression AnalysisAnimal Science and ZoologyFemaleFood scienceAlleleDairy cattleFood ScienceThe Journal of dairy research
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Receptor protein-tyrosine phosphatases: origin of domains (catalytic domain, Ig-related domain, fibronectin type III module) based on the sequence of…

2001

Abstract Reversible tyrosine phosphorylation of proteins is one of the major regulatory physiological events in response to cell-cell- and cell-matrix contact in Metazoa. Previously it was documented that the tyrosine phosphorylating enzymes, the tyrosine kinases (TKs), are autapomorphic characters of Metazoa, including sponges. In this paper the tyrosine dephosphorylating enzymes, the protein-tyrosine phosphatases (PTPs), are studied which can be grouped into two subfamilies, the soluble PTPs and the receptor PTPs (RPTPs). PTPs are characterized by one PTPase domain which interestingly comprises sequence similarity to yeast PTPs. In contrast to the PTPs, the RPTPs – which have been found o…

Molecular Sequence DataImmunoglobulinsBiologyPolymerase Chain ReactionEvolution Molecularchemistry.chemical_compoundCatalytic DomainGene duplicationGeneticsAnimalsAmino Acid SequenceTyrosineCloning MolecularPhylogenychemistry.chemical_classificationPhylogenetic treeSequence Homology Amino AcidTyrosine phosphorylationGeneral MedicineProtein-Tyrosine KinasesAmino acidFibronectinsPoriferaProtein Structure TertiaryOpen reading framechemistryBiochemistryPhosphorylationProtein Tyrosine PhosphatasesTyrosine kinaseSequence AnalysisGene
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Multiple Ig-like featuring genes divergent within and among individuals of the marine sponge Geodia cydonium.

1998

Abstract The receptor tyrosine kinase of the marine sponge Geodia cydonium features two extracellular Ig-like domains in which we recently documented RT-PCR polymorphism among individuals. Genomic-PCR analysis presented here revealed 14 unique sequences from four sponges, differing predominantly in the sequence of an intron which splits the Ig-like domains. Nevertheless, analysis of putative coding regions in 19 distinct clones (156–159 aa) from seven sponges revealed 69 positions of nucleotide substitutions, 67.6% of them non-synonymous, translating into 43 positions of divergent residues. Excluding aa deletions, these 19 sequences share pairwise aa identities of 89–99%. In three sponges, …

Molecular Sequence DataImmunoglobulinsGenomePolymerase Chain ReactionReceptor tyrosine kinaselaw.inventionlawMHC class IGeneticsCoding regionAnimalsHumansAmino Acid SequenceGenePolymerase chain reactionGeneticsPolymorphism GeneticbiologyBase SequenceSequence Homology Amino AcidIntronReceptor Protein-Tyrosine KinasesGeneral MedicineDNAbiology.organism_classificationIntronsPoriferaSpongeMultigene Familybiology.proteinSequence AlignmentGene
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