Search results for "interaction [dark matter]"

showing 10 items of 363 documents

Resonance energy transfer between two atoms in a conducting cylindrical waveguide

2018

We consider the energy transfer process between two identical atoms placed inside a perfectly conducting cylindrical waveguide. We first introduce a general analytical expression of the energy transfer amplitude in terms of the electromagnetic Green's tensor; we then evaluate it in the case of a cylindrical waveguide made of a perfect conductor, for which analytical forms of the Green's tensor exist. We numerically analyse the energy transfer amplitude when the radius of the waveguide is such that the transition frequency of both atoms is below the lower cutoff frequency of the waveguide, so that the resonant photon exchange is strongly suppressed. We consider both cases of atomic dipoles p…

PhysicsQuantum PhysicsPhotonResonancePhysics::OpticsFOS: Physical sciencesResonant energy transfer. Resonance dipole-dipole interactions. Cavity quantum electrodynamics.Interaction energy01 natural sciencesCutoff frequency010305 fluids & plasmasExcited state0103 physical sciencesWaveguide (acoustics)Perfect conductorAtomic physics010306 general physicsGround stateQuantum Physics (quant-ph)
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Towards an Experimental Determination of the Transition Strength Between the Ground States of $^{20}$F and $^{20}$Ne

2017

Electron capture on $^{20}$Ne is thought to play a crucial role in the final evolution of electron-degenerate ONe stellar cores. Recent calculations suggest that the capture process is dominated by the second-forbidden transition between the ground states of $^{20}$Ne and $^{20}$F, making an experimental determination of this transition strength highly desirable. To accomplish this task we are refurbishing an intermediate-image magnetic spectrometer capable of focusing 7 MeV electrons, and designing a scintillator detector surrounded by an active cosmic-ray veto shield, which will serve as an energy-dispersive device at the focal plane.

Physicsstellar evolutionPhysics - Instrumentation and Detectorsta114Condensed matter physicsPhysics::Instrumentation and Detectorsweak-interaction ratesnuclear experimentFOS: Physical sciencesInstrumentation and Detectors (physics.ins-det)Transition strengthAstrophysics - Solar and Stellar Astrophysicsbeta-decaySolar and Stellar Astrophysics (astro-ph.SR)
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Phospholipid monolayers at water∣oil interfaces: theoretical modelling of surface pressure–molecular area isotherms

1998

Abstract The phospholipid adsorption and surface pressure–molecular area isotherms at interfaces are interpreted theoretically from two-dimensional (2D) lattice and real gas models that incorporate a minimum number of adjustable parameters. The first model is based on the lattice statistics of binary solutions and the molecular parameters introduced are the energy changes involved in the mixing process of the phospholipid and organic solvent molecules and the effective phospholipid head area. The surface pressure is interpreted in terms of the difference between the two liquid surface tensions. The second model makes use of (i) a non-localised adsorption model with a square-well potential e…

Physics::Biological PhysicsReal gasChromatographyChemistryGeneral Chemical EngineeringPhospholipidThermodynamicsInteraction energySurface pressurePotential energyAnalytical ChemistryCondensed Matter::Soft Condensed Matterchemistry.chemical_compoundAdsorptionMonolayerElectrochemistrylipids (amino acids peptides and proteins)Physics::Chemical PhysicsOrder of magnitudeJournal of Electroanalytical Chemistry
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Functional characterization of two melanocortin (MC) receptors in lamprey showing orthology to the MC1 and MC4 receptor subtypes

2007

Abstract Background The melanocortin (MC) receptors have a key role in regulating body weight and pigmentation. They belong to the rhodopsin family of G protein-coupled receptors (GPCRs). The purpose of this study was to identify ancestral MC receptors in agnathan, river lamprey. Results We report cloning of two MC receptors from river lamprey. The lamprey receptors, designated MCa and MCb, showed orthology to the MC1 and MC4 receptor subtypes, respectively. The molecular clock analysis suggested that lamprey MC receptor genes were not duplicated recently and diverged from each other more than 400 MYR ago. Expression and pharmacological characterization showed that the lamprey MCa receptor …

Pro-OpiomelanocortinSecond Messenger SystemsGene DuplicationProtein Interaction MappingCyclic AMPPetromyzonReceptorPhylogenyCell Line TransformedSkinGeneticsbiologyReceptors MelanocortinMelanocortin 3 receptorCell biologyOrgan SpecificityRhodopsinReceptor Melanocortin Type 4HagfishesMelanocortinReceptor Melanocortin Type 1Protein BindingResearch ArticleEvolutionRecombinant Fusion ProteinsMolecular Sequence DataBinding CompetitivePeptides CyclicEvolution Moleculargamma-MSHAdrenocorticotropic HormoneSpecies SpecificityMelanocortin receptorbeta-MSHQH359-425AnimalsHumansAmino Acid SequenceEcology Evolution Behavior and SystematicsGene LibraryG protein-coupled receptorBinding SitesSequence Homology Amino AcidFuguLampreybiology.organism_classificationPeptide FragmentsVisceraalpha-MSHbiology.proteinCosyntropinSequence Alignmenthuman activitiesBMC Evolutionary Biology
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The Role of Low Complexity Regions in Protein Interaction Modes: An Illustration in Huntingtin

2021

Low complexity regions (LCRs) are very frequent in protein sequences, generally having a lower propensity to form structured domains and tending to be much less evolutionarily conserved than globular domains. Their higher abundance in eukaryotes and in species with more cellular types agrees with a growing number of reports on their function in protein interactions regulated by post-translational modifications. LCRs facilitate the increase of regulatory and network complexity required with the emergence of organisms with more complex tissue distribution and development. Although the low conservation and structural flexibility of LCRs complicate their study, evolutionary studies of proteins …

Protein Conformation alpha-Helical0301 basic medicineNetwork complexityHuntingtinintrinsically disordered regionsAmino Acid MotifsComputational biologyBiologyprotein interactionsArticlecompositionally biased regionsCatalysisProtein–protein interactionlcsh:ChemistryEvolution MolecularInorganic ChemistryLow complexity03 medical and health sciencesProtein DomainsProtein Interaction MappingAnimalsHumansp300-CBP Transcription FactorsAmino Acid SequenceProtein Interaction MapsHuntingtinTissue distributionPhysical and Theoretical Chemistrylcsh:QH301-705.5Molecular BiologySpectroscopyHuntingtin Protein030102 biochemistry & molecular biologyOrganic ChemistryNuclear Proteinsp120 GTPase Activating ProteinGeneral MedicineMultiple modesSynapsinslow complexity regionsComputer Science ApplicationshomorepeatsMicroscopy Electron030104 developmental biologylcsh:Biology (General)lcsh:QD1-999Sequence AlignmentFunction (biology)Protein BindingInternational Journal of Molecular Sciences
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Kinetic analysis and molecular modeling of the inhibition mechanism of roneparstat (SST0001) on human heparanase

2016

Heparanase is a β-d-glucuronidase which cleaves heparan sulfate chains in the extracellular matrix and on cellular membranes. A dysregulated heparanase activity is intimately associated with cell invasion, tumor metastasis and angiogenesis, making heparanase an attractive target for the development of anticancer therapies. SST0001 (roneparstat; Sigma-Tau Research Switzerland S.A.) is a non-anticoagulant 100% N-acetylated and glycol-split heparin acting as a potent heparanase inhibitor, currently in phase I in advanced multiple myeloma. Herein, the kinetics of heparanase inhibition by roneparstat is reported. The analysis of dose-inhibition curves confirmed the high potency of roneparstat (I…

Protein Conformation alpha-Helical0301 basic medicineSST0001Molecular modelhomology modelingAmino Acid MotifsPlasma protein bindingMolecular Dynamics SimulationBiochemistryMolecular Docking SimulationheparanaseSubstrate Specificity03 medical and health scienceschemistry.chemical_compound0302 clinical medicinePolysaccharidesHumansProtein Interaction Domains and MotifsHeparanaseHomology modelingEnzyme InhibitorsGlucuronidaseBinding Siteskinetic inhibition analysisHeparinComputational BiologyHeparan sulfateRecombinant ProteinsAcidobacteriaMolecular Docking SimulationEnzyme bindingKinetics030104 developmental biologyCarbohydrate SequenceFondaparinuxchemistryBiochemistryStructural Homology ProteinDocking (molecular)030220 oncology & carcinogenesisBiophysicsroneparstatThermodynamicsProtein Conformation beta-StrandORIGINAL ARTICLESProtein BindingGlycobiology
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A potential solution to avoid overdose of mixed drugs in the event of Covid-19: Nanomedicine at the heart of the Covid-19 pandemic.

2021

Since 2020, the world is facing the first global pandemic of 21st century. Among all the solutions proposed to treat this new strain of coronavirus, named SARS-CoV-2, the vaccine seems a promising way but the delays are too long to be implemented quickly. In the emergency, a dual therapy has shown its effectiveness but has also provoked a set of debates around the dangerousness of a particular molecule, hydroxychloroquine. In particular, the doses to be delivered, according to the studies, were well beyond the acceptable doses to support the treatment without side effects. We propose here to use all the advantages of nanovectorization to address this question of concentration. Using quantum…

Protein Conformation alpha-HelicalComputer science02 engineering and technologyAzithromycinDrug Delivery SystemsPandemicMaterials ChemistryDrug Dosage CalculationsSpectroscopymedia_common0303 health sciencesEvent (computing)021001 nanoscience & nanotechnologyComputer Graphics and Computer-Aided DesignMolecular Docking SimulationNanomedicineRisk analysis (engineering)Spike Glycoprotein CoronavirusDensity functional theory calculationsNanomedicineThermodynamicsNitrogen OxidesAngiotensin-Converting Enzyme 20210 nano-technologyHydroxychloroquineProtein BindingDrugBoron CompoundsCoronavirus disease 2019 (COVID-19)media_common.quotation_subjectSevere acute respiratory syndrome coronavirus 2 (SARS-CoV-2)Molecular Dynamics SimulationAntiviral AgentsArticle03 medical and health sciencesHumansProtein Interaction Domains and MotifsDual therapyPhysical and Theoretical Chemistry030304 developmental biologyDrug transportBinding SitesSARS-CoV-2Molecular dynamics simulationsCOVID-19NanostructuresCOVID-19 Drug TreatmentKineticsQuantum TheoryProtein Conformation beta-StrandNanovectorizationJournal of molecular graphicsmodelling
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Activation of the p75 neurotrophin receptor through conformational rearrangement of disulphide-linked receptor dimers.

2009

Ligand-mediated dimerization has emerged as a universal mechanism of growth factor receptor activation. Recent structural studies have shown that neurotrophins interact with dimers of the p75 neurotrophin receptor (p75NTR), but the actual mechanism of receptor activation has remained elusive. Here we show that p75NTR forms disulphide-linked dimers independently of neurotrophin binding through the highly conserved Cys257 in its transmembrane domain. Mutation of Cys257 abolished neurotrophin-dependent receptor activity but did not affect downstream signaling by the p75NTR/NgR/Lingo-1 complex in response to MAG, indicating the existence of distinct, ligand-specific activation mechanisms for p7…

Protein ConformationMutantNeuronesReceptor Nerve Growth FactorMiceProtein structureChlorocebus aethiopsNerve Growth FactorLow-affinity nerve growth factor receptorRNA Small InterferingReceptorskin and connective tissue diseasesReceptors neuralsCells CulturedNeuronsCell DeathGeneral NeuroscienceNF-kappa BCell biologyTransmembrane domainSIGNALINGOligopeptidesNeurotrophinProtein BindingSignal Transductionmusculoskeletal diseasesPROTEINSNeuroscience(all)Green Fluorescent ProteinsNerve Tissue ProteinsReceptors Nerve Growth FactorSuperior Cervical GanglionBiologyTransfectionMOLNEUROArticleGrowth factor receptorAnimalsHumansProtein Interaction Domains and MotifsReceptors Growth FactorCysteineBinding SitesMembrane Proteinsbiological factorsRatsnervous systemAnimals NewbornNeurotrophin bindingMutationbiology.proteinsense organsProtein MultimerizationrhoA GTP-Binding ProteinProteïnesNeuron
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Methodological approaches for the analysis of transmembrane domain interactions: A systematic review

2021

The study of protein-protein interactions (PPI) has proven fundamental for the understanding of the most relevant cell processes. Any protein domain can participate in PPI, including transmembrane (TM) segments that can establish interactions with other TM domains (TMDs). However, the hydrophobic nature of TMDs and the environment they occupy complicates the study of intramembrane PPI, which demands the use of specific approaches and techniques. In this review, we will explore some of the strategies available to study intramembrane PPI in vitro, in vivo, and, in silico, focusing on those techniques that could be carried out in a standard molecular biology laboratory regarding its previous e…

Protein FoldingBacteriaChemistryIn silicoProtein domainBiophysicsMembrane ProteinsCell CommunicationCell BiologyComputational biologyBiochemistryTransmembrane proteinIn vitroProtein–protein interactionTransmembrane domainProtein DomainsMembrane proteinProtein foldingProtein Interaction MapsHydrophobic and Hydrophilic InteractionsBiochimica et Biophysica Acta (BBA) - Biomembranes
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Proteome-Wide Characterization of the RNA-Binding Protein RALY-Interactome Using the in Vivo-Biotinylation-Pulldown-Quant (iBioPQ) Approach

2013

RALY is a member of the heterogeneous nuclear ribonucleoproteins, a family of RNA-binding proteins generally involved in many processes of mRNA metabolism. No quantitative proteomic analysis of RALY-containing ribonucleoparticles (RNPs) has been performed so far, and the biological role of RALY remains elusive. Here, we present a workflow for the characterization of RALY's interaction partners, termed iBioPQ, that involves in vivo biotinylation of biotin acceptor peptide (BAP)-fused protein in the presence of the prokaryotic biotin holoenzyme synthetase of BirA so that it can be purified using streptavidin-coated magnetic beads, circumventing the need for specific antibodies and providing e…

ProteomeRecombinant Fusion ProteinsMolecular Sequence DataBiotinRNA-binding proteinBiologyHeterogeneous ribonucleoprotein particleProteomicsPoly(A)-Binding Protein IBiochemistryInteractomeELAV-Like Protein 103 medical and health scienceschemistry.chemical_compound0302 clinical medicineNuclear Matrix-Associated ProteinsBiotinProtein Interaction MappingHumansCarbon-Nitrogen LigasesAmino Acid SequenceProtein Interaction MapsPeptide sequence030304 developmental biology0303 health sciencesEscherichia coli ProteinsHeterogeneous-Nuclear Ribonucleoprotein Group CRNA-Binding ProteinsGeneral ChemistryRepressor ProteinsHEK293 CellsELAV ProteinsGene Expression RegulationBiochemistrychemistryProtein Biosynthesis030220 oncology & carcinogenesisBiotinylationProteomeBiological AssayStreptavidinHeLa CellsProtein BindingJournal of Proteome Research
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