Search results for "Caps"

showing 10 items of 745 documents

Produzione di semi sintetici di Capparis spinosa (L.). Innovazione e tradizione

2011

The caper bush (Capparis spinosa L.) is a rupiculous species. It is widespread on rocky areas and it grows on different soil associations. Caper can be propagated from fresh seeds, gathered from ripe fruit, or by stem cuttings both methods with unsatisfying results, due to the low germination percentage and to the season-dependent answer of the cutting technique. The aim of the present research has been to evaluate the attitude, for caper in vitro propagules , to be encapsulated. Micro cuttings from in vitro plantlets, were dissected and put on two different Murashige and Skoog liquid media enriched with 4% sodium alginate and 1,4% di CaCl2 separately, for the encapsulation. The synthetic s…

Micropropagation encapsulation alginate conversion regrowth.Settore AGR/04 - Orticoltura E Floricoltura
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A novel rat CVB1-VP1 monoclonal antibody 3A6 detects a broad range of enteroviruses

2018

AbstractEnteroviruses (EVs) are common RNA viruses that cause diseases ranging from rash to paralytic poliomyelitis. For example, EV-A and EV-C viruses cause hand-foot and mouth disease and EV-B viruses cause encephalitis and myocarditis, which can result in severe morbidity and mortality. While new vaccines and treatments for EVs are under development, methods for studying and diagnosing EV infections are still limited and therefore new diagnostic tools are required. Our aim was to produce and characterize new antibodies that work in multiple applications and detect EVs in tissues and in vitro. Rats were immunized with Coxsackievirus B1 capsid protein VP1 and hybridomas were produced. Hybr…

Models Molecular0301 basic medicineBiolääketieteet - BiomedicineProtein Conformationmedicine.drug_classImmunoelectron microscopylcsh:MedicineEnzyme-Linked Immunosorbent AssayCoxsackievirusmedicine.disease_causeMonoclonal antibodyenterovirusesArticleEpitopeEpitopesMice03 medical and health sciencesProtein DomainsEnterovirus InfectionsmedicineantibodiesAnimalsHumanslcsh:ScienceMultidisciplinary030102 biochemistry & molecular biologybiologyPolioviruslcsh:Rvasta-aineetAntibodies Monoclonalbiology.organism_classificationAntibodies NeutralizingImmunohistochemistryVirologyEnterovirus B HumanRats3. Good healthenterovirukset030104 developmental biologyKasvibiologia mikrobiologia virologia - Plant biology microbiology virologybiology.proteinImmunohistochemistrylcsh:QCapsid ProteinsAntibodyClone (B-cell biology)Protein BindingScientific Reports
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Molecular evolutionary analysis of type-1 human astroviruses identifies putative sites under selection pressure on the capsid protein

2017

Human astroviruses (HAstV) are important enteric pathogens that can be classified into eight sero/genotypes (HAstV-1 to -8). Although the various HAstV types show global spread, type-1 strains tend to be predominant. Molecular analysis of the genomic region encoding the capsid protein (ORF2) has revealed discrete sequence variation, with different lineages within each HAstV type and at least three major lineages have been identified within HAstV-1. Longitudinal epidemiological surveillance has revealed temporal shift of the various HAstV-1 lineages. Metadata analysis of HAstV-1 sequences available in the databases also revealed temporal shifts of the circulation of HAstV-1 lineages, suggest…

Models Molecular0301 basic medicineMicrobiology (medical)Settore MED/07 - Microbiologia E Microbiologia ClinicaGenotypeProtein ConformationAstroviru030106 microbiologyBiologyMicrobiologyAstrovirusEvolution MolecularOpen Reading Frames03 medical and health sciencesProtein structureGeneticPhylogeneticsAstroviridae InfectionsGenetic variationGenotypePhylogenetic analyseGeneticsHumansAmino Acid SequenceSelection GeneticPeptide sequenceMolecular BiologyPhylogenyEcology Evolution Behavior and SystematicsGeneticsGenetic evolutionSelection pressure analysiGenetic Variationbiology.organism_classificationEcology Evolution Behavior and SystematicOpen reading frame030104 developmental biologyInfectious DiseasesCapsidAstroviridaeCapsid ProteinsCapsid protein structureHAstV-1
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The use of low-resolution phasing followed by phase extension from 7.6 to 2.5 Å resolution with noncrystallographic symmetry to solve the structure o…

2011

P2, the major capsid protein of bacteriophage PM2, adopts the double β-barrel fold characteristic of the PRD1-adenoviral lineage. The 2.5 Å resolution X-ray data obtained by analysis of the two major lattices of a multiple crystal of P2 were phased by molecular replacement, using as a search model structure factors to 7.6 Å resolution obtained from electron density cut from the map of the entire PM2 virion. Phase extension to 2.5 Å resolution used solely sixfold cycling averaging and solvent flattening. This represents an atypical example of an oligomeric protein for which the structure has been determined at high resolution by bootstrapping from low-resolution initial phases.

Models Molecular0303 health sciencesElectron densitybiologyLow resolution030303 biophysicsGeneral MedicineCrystallography X-Raybiology.organism_classificationBacteriophage PM2PhaserFlatteningProtein Structure TertiaryBacteriophage03 medical and health sciencesCrystallographyCapsidStructural BiologyBacteriophagesCapsid ProteinsMolecular replacementProtein Structure Quaternary030304 developmental biologyActa Crystallographica Section D Biological Crystallography
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Effective stiffening of DNA due to nematic ordering causes DNA molecules packed in phage capsids to preferentially form torus knots.

2012

Observation that DNA molecules in bacteriophage capsids preferentially form torus type of knots provided a sensitive gauge to evaluate various models of DNA arrangement in phage heads. Only models resulting in a preponderance of torus knots could be considered as close to reality. Recent studies revealed that experimentally observed enrichment of torus knots can be qualitatively reproduced in numerical simulations that include a potential inducing nematic arrangement of tightly packed DNA molecules within phage capsids. Here, we investigate what aspects of the nematic arrangement are crucial for inducing formation of torus knots. Our results indicate that the effective stiffening of DNA by …

Models MolecularBacteriophages/genetics; Capsid/chemistry; DNA Viral/chemistry; Models Molecular; Virus AssemblyvirusesBacteriophageQuantitative Biology::Subcellular Processeschemistry.chemical_compoundCapsidstomatognathic systemLiquid crystalStructural BiologyGeneticsMoleculeBacteriophagesDna viralQuantitative Biology::BiomoleculesbiologyVirus Assemblyfood and beveragesTorusbiology.organism_classificationVirologyQuantitative Biology::GenomicsMathematics::Geometric TopologyStiffeningsurgical procedures operativechemistryCapsidDNA ViralBiophysicsDNANucleic acids research
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Extracellular Albumin and Endosomal Ions Prime Enterovirus Particles for Uncoating That Can Be Prevented by Fatty Acid Saturation

2019

ABSTRACT There is limited information about the molecular triggers leading to the uncoating of enteroviruses under physiological conditions. Using real-time spectroscopy and sucrose gradients with radioactively labeled virus, we show at 37°C, the formation of albumin-triggered, metastable uncoating intermediate of echovirus 1 without receptor engagement. This conversion was blocked by saturating the albumin with fatty acids. High potassium but low sodium and calcium concentrations, mimicking the endosomal environment, also induced the formation of a metastable uncoating intermediate of echovirus 1. Together, these factors boosted the formation of the uncoating intermediate, and the infectiv…

Models MolecularEchovirusHot TemperatureEndosomevirusesImmunologycryoEM structurerasvahapotEndosomesBiologymedicine.disease_causeMicrobiologyDivalentCell Line03 medical and health sciencesVirologyAlbuminsChlorocebus aethiopsExtracellularmedicineAnimalsalbumin030304 developmental biologychemistry.chemical_classificationalbumiinit0303 health sciencesbiokemiaionitenterovirus030302 biochemistry & molecular biologyCryoelectron MicroscopyFatty AcidsFatty acidRNAVirus-Cell InteractionsEnterovirus B HumanenteroviruksetchemistryCapsidvirologia13. Climate actionInsect ScienceBiophysicsCapsid ProteinsuncoatingLow sodium
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Subphthalocyanines: addressing water-solubility, nano-encapsulation, and activation for optical imaging of B16 melanoma cells

2014

Water-soluble disulfonato-subphthalocyanines (SubPcs) or hydrophobic nano-encapsulated SubPcs are efficient probes for the fluorescence imaging of cells. 20 nm large liposomes (TEM and DLS) incorporated about 13% SubPc. Moreover, some of these fluorophores were found to be pH activatable.

Models MolecularFluorescence-lifetime imaging microscopyNanostructureIndolesMelanoma ExperimentalIsoindoles010402 general chemistryPhotochemistryCrystallography X-Ray01 natural sciencesCatalysisMiceMaterials ChemistryMoleculeAnimals[CHIM]Chemical SciencesSolubilityFluorescent DyesLiposomeAqueous solutionMolecular Structure010405 organic chemistryChemistryMetals and AlloysWaterGeneral ChemistryHydrogen-Ion Concentration0104 chemical sciencesSurfaces Coatings and FilmsElectronic Optical and Magnetic MaterialsMolecular ImagingNanostructuresNano encapsulationSolubilityLiposomesCeramics and CompositesMolecular imaging
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Molecular and structural characterization of fluorescent human parvovirus B19 virus-like particles

2005

Although sharing a T = 1 icosahedral symmetry with other members of the Parvoviridae family, it has been suggested that the fivefold channel of the human parvovirus B19 VP2 capsids is closed at its outside end. To investigate the possibility of placing a relatively large protein moiety at this site of B19, fluorescent virus-like particles (fVLPs) of B19 were developed. The enhanced green fluorescent protein (EGFP) was inserted at the N-terminus of the structural protein VP2 and assembly of fVLPs from this fusion protein was obtained. Electron microscopy revealed that these fluorescent protein complexes were very similar in size when compared to wild-type B19 virus. Further, fluorescence cor…

Models MolecularImmunoprecipitationRecombinant Fusion ProteinsvirusesGreen Fluorescent ProteinsBiophysicsFluorescence correlation spectroscopyEndosomesSpodopteraBiologyMicroscopy Atomic ForceBiochemistryFluorescenceCell LineGreen fluorescent proteinParvoviridae InfectionsBimolecular fluorescence complementationCell Line Tumorhemic and lymphatic diseasesParvovirus B19 HumanAnimalsHumansImmunoprecipitationMolecular BiologyParvoviridaeImmune SeraVirus AssemblyVirionvirus diseasesCell Biologybiology.organism_classificationFusion proteinMolecular biologyNanostructuresCell biologyTransport proteinProtein TransportCapsidCapsid Proteins
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A self-assembled M8L6 cubic cage that selectively encapsulates large aromatic guests.

2011

Porphyrins cubed: A series of self-assembled M8L6 cubic cages that enclose a volume in excess of 1300 A3 were synthesized (see scheme). The porphyrinic walls of the cubes provide favorable sites for pnp interactions, leading to selectivity between large and chemically similar aromatic guests: three molecules of coronene are incorporated and the higher fullerenes C70nC84 are selectively bound in the presence of

Models MolecularMagnetic Resonance SpectroscopyMolecular StructureCapsulesGeneral ChemistryCrystallography X-RayHydrocarbons AromaticCatalysisCoroneneHigher fullerenesSelf assembledchemistry.chemical_compoundchemistryNickelPolymer chemistryPhysics::Atomic and Molecular ClustersMoleculePolycyclic CompoundsFullerenesCageSelectivityAngewandte Chemie (International ed. in English)
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Bacteriophage P23-77 capsid protein structures reveal the archetype of an ancient branch from a major virus lineage.

2013

Summary It has proved difficult to classify viruses unless they are closely related since their rapid evolution hinders detection of remote evolutionary relationships in their genetic sequences. However, structure varies more slowly than sequence, allowing deeper evolutionary relationships to be detected. Bacteriophage P23-77 is an example of a newly identified viral lineage, with members inhabiting extreme environments. We have solved multiple crystal structures of the major capsid proteins VP16 and VP17 of bacteriophage P23-77. They fit the 14 Å resolution cryo-electron microscopy reconstruction of the entire virus exquisitely well, allowing us to propose a model for both the capsid archi…

Models MolecularProtein ConformationViral proteinLineage (evolution)virusesCrystallography X-Raymedicine.disease_causeArticleVirusViral AssemblyBacteriophage03 medical and health sciencesProtein structureStructural BiologymedicineBacteriophagesMolecular Biology030304 developmental biologySequence (medicine)0303 health sciencesbiology030306 microbiologyCryoelectron Microscopyta1183ta1182biology.organism_classificationVirology3. Good healthCapsidEvolutionary biologyCapsid ProteinsCrystallizationStructure (London, England : 1993)
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