Search results for "MACROMOLECULAR"

showing 10 items of 944 documents

Filopodia-like actin cables position nuclei in association with perinuclear actin in Drosophila nurse cells

2013

Summary Controlling the position of the nucleus is vital for a number of cellular processes from yeast to humans. In Drosophila nurse cells, nuclear positioning is crucial during dumping, when nurse cells contract and expel their contents into the oocyte. We provide evidence that in nurse cells, continuous filopodia-like actin cables, growing from the plasma membrane and extending to the nucleus, achieve nuclear positioning. These actin cables move nuclei away from ring canals. When nurse cells contract, actin cables associate laterally with the nuclei, in some cases inducing nuclear turning so that actin cables become partially wound around the nuclei. Our data suggest that a perinuclear a…

Cell NucleusFilaminsaktiiniCell Membranemacromolecular substancesCadherinsArticleActinsActin CytoskeletonDrospphilaGerm CellsAnimalsDrosophila ProteinsDrosophilaPseudopodiakehitysbiologiaactinDevelopmental Biology
researchProduct

Enzyme-Controlled Nanodevice for Acetylcholine-Triggered Cargo Delivery Based on Janus Au–Mesoporous Silica Nanoparticles

2017

[EN] This work reports a new gated nanodevice for acetylcholine-triggered cargo delivery. We prepared and characterized Janus Au-mesoporous silica nanoparticles functionalized with acetylcholinesterase on the Au face and with supramolecular b-cyclodextrin: benzimidazole inclusion complexes as caps on the mesoporous silica face. The nanodevice is able to selectively deliver the cargo in the presence of acetylcholine via enzyme-mediated acetylcholine hydrolysis, locally lowering the pH and opening the supramolecular gate. Given the key role played by ACh and its relation with Parkinson's disease and other nervous system diseases, we believe that these findings could help design new therapeuti…

Cell SurvivalSupramolecular chemistryNanoparticleNanotechnologymacromolecular substances02 engineering and technology010402 general chemistry01 natural sciencesCatalysisQUIMICA ORGANICACIENCIA DE LOS MATERIALES E INGENIERIA METALURGICAQUIMICA ANALITICAmedicineOrganometallic CompoundsControlled releaseNanotechnologyHumansJanusNanodevicechemistry.chemical_classificationDrug CarriersChemistryHydrolysisQUIMICA INORGANICAOrganic Chemistrybeta-CyclodextrinsGeneral ChemistryMesoporous silicaHydrogen-Ion Concentration021001 nanoscience & nanotechnologyEnzymes ImmobilizedSilicon DioxideControlled releaseMesoporous materialsAcetylcholine0104 chemical sciencesEnzymeDoxorubicinAcetylcholinesteraseNanoparticlesBenzimidazolesGold0210 nano-technologyPorosityAcetylcholinemedicine.drugHeLa Cells
researchProduct

Profilin 1 is required for abscission during late cytokinesis of chondrocytes

2009

Profilins are key factors for dynamic rearrangements of the actin cytoskeleton. However, the functions of profilins in differentiated mammalian cells are uncertain because profilin deficiency is early embryonic lethal for higher eukaryotes. To examine profilin function in chondrocytes, we disrupted the profilin 1 gene in cartilage (Col2pfn1). Homozygous Col2pfn1 mice develop progressive chondrodysplasia caused by disorganization of the growth plate and defective chondrocyte cytokinesis, indicated by the appearance of binucleated cells. Surprisingly, Col2pfn1 chondrocytes assemble and contract actomyosin rings normally during cell division; however, they display defects during late cytokines…

Cell divisionMice Transgenicmacromolecular substancesBiologyMyosinsOsteochondrodysplasiasGeneral Biochemistry Genetics and Molecular BiologyChondrocyteArticleBone and BonesMiceProfilinsChondrocytesMyosinmedicineAnimalsMolecular BiologyActinCytokinesisGeneral Immunology and MicrobiologyGeneral NeuroscienceActin cytoskeletonActinsCell biologymedicine.anatomical_structureCartilageProfilinGene Targetingbiology.proteinLamellipodiumCytokinesis
researchProduct

Structural and regulatory functions of keratins.

2007

The diversity of epithelial functions is reflected by the expression of distinct keratin pairs that are responsible to protect epithelial cells against mechanical stress and to act as signaling platforms. The keratin cytoskeleton integrates these functions by forming a supracellular scaffold that connects at desmosomal cell-cell adhesions. Multiple human diseases and murine knockouts in which the integrity of this system is destroyed testify to its importance as a mechanical stabilizer in certain epithelia. Yet, surprisingly little is known about the precise mechanisms responsible for assembly and disease pathology. In addition to these structural aspects of keratin function, experimental e…

CellIntermediate Filamentsmacromolecular substancesBiologyFocal adhesionEpidermolysis bullosa simplexMicrotubuleOrganelleKeratinmedicineAnimalsHumansCytoskeletonCytoskeletonchemistry.chemical_classificationCell PolarityEpithelial CellsCell BiologyDesmosomesmedicine.diseaseCell biologymedicine.anatomical_structureCell Transformation NeoplasticchemistryKeratinsStress MechanicalFunction (biology)Signal TransductionExperimental cell research
researchProduct

Inclusion complexes of Cethyl-2-methylresorcinarene and pyridine N-oxides: breaking the C–I⋯−O–N+ halogen bond by host–guest complexation

2016

C ethyl-2-Methylresorcinarene forms host–guest complexes with aromatic N-oxides through multiple intra- and intermolecular hydrogen bonds and C–H⋯π interactions. The host shows conformational flexibility to accommodate 3-methylpyridine N-oxide, while retaining a crown conformation for 2-methyl- and 4-methoxypyridine N-oxides highlighting the substituent effect of the guest. N-Methylmorpholine N-oxide, a 6-membered ring aliphatic N-oxide with a methyl at the N-oxide nitrogen, is bound by the equatorial −N–CH3 group located deep in the cavity. 2-Iodopyridine N-oxide is the only guest that manifests intermolecular N–O⋯I–C halogen bond interactions, which are broken down by the host resulting i…

Cethyl-2-methylresorcinarenekemialliset sidoksethost–guest complexationsupramolekulaarinen kemiahalogen bondmacromolecular substanceshalogeenisidospyridine N-oxides
researchProduct

Effect of EDTA and citrate on the functional activity of the first component of complement, C1, and the C1q subcomponent.

1985

The first component of complement, C1, is a calcium-dependent complex of the three distinct subcomponents, C1q, C1r, and C1s. Earlier observations revealed that treatment of C1 with EDTA led to a loss of hemolytic C1 activity even after recalcification. Therefore, it was of interest to study whether EDTA has an additional effect on C1 and its subcomponents, beside its chelating capacity. The chelating effect of EDTA was compared to that of citrate. It was found that treatment of C1 or C1 with EDTA followed by addition of Ca++ led to a loss of hemolytic activity up to 90%, depending on EDTA concentration. Even pretreatment of EDTA with varying amounts of Ca++ did not prevent the inactivation…

Chemical PhenomenaComplement Activating EnzymesMacromolecular SubstancesImmunologyKineticschemistry.chemical_elementCalciumHemolysisDissociation (chemistry)Structure-Activity RelationshipComplement C1medicineImmunology and AllergyStructure–activity relationshipHumansChelationCitratesComplement C1qEdetic AcidComplement C1qHematologymedicine.diseaseHemolysisChemistryKineticsBiochemistrychemistryEdetic AcidCalciumImmunobiology
researchProduct

Chemical and catalytical properties of thermal polymers of amino acids (proteinoids)

1974

The significance of thermal polyamino acids (proteinoids) as abiotic predecessors of proteins is reviewed on the basis of new experimental results. Most proteinoids yield only 50% to 80% amino acid upon acid hydrolysis. They contain 40% to 60% less peptide links than typical proteins, whereas their average nitrogen content is like that of proteins. The arrangement of amino acid residues is nonrandom. The degree of nonrandomness is difficult to determine because unusual crosslinks disturb most of the sequencing methods typically applied in protein chemistry. The products obtained in a polymerization experiment are heterogeneous. They can be separated into a limited number of related fraction…

Chemical PhenomenaMacromolecular SubstancesPolymersOrigin of LifePeptideCatalysisChromatography DEAE-CelluloseProteinoidOrganic chemistryAmino Acid SequenceAmino AcidsMolecular BiologyEcology Evolution Behavior and SystematicsGeneral Environmental Sciencechemistry.chemical_classificationMolecular massHydrolysisProteinsGeneral MedicinePolymerHydrogen-Ion ConcentrationElectrophoresis DiscBiological EvolutionAgricultural and Biological Sciences (miscellaneous)Amino acidMolecular WeightChemistrySolubilitychemistryPolymerizationSpace and Planetary ScienceYield (chemistry)ThermodynamicsGeneral Earth and Planetary SciencesAcid hydrolysisOrigins of Life
researchProduct

Preferential solvation of poly(methyl methacrylate) and a bisphenol A diglycidyl ether by size-exclusion chromatography

2004

The preferential adsorption coefficient, lambda, of poly(methyl methacrylate), PMMA, in solutions formed by an epoxy resin in tetrahydrofuran (THF), was studied by size-exclusion chromatography (SEC). Only PMMA of lowest molar mass was preferentially solvated by epoxy but at low concentrations of epoxy in the mixture. At higher epoxy content PMMA was preferentially solvated by THF. A simultaneous and competitive solvation between the specific interactions PMMA-epoxy and the self association of epoxy at high concentrations would be the responsible of this inversion point. The more compacted coil of PMMA of higher molecular weights in solution could explain the lack of interaction of these po…

Chemical PhenomenaSize-exclusion chromatographymacromolecular substancesBiochemistryAnalytical ChemistryGel permeation chromatographychemistry.chemical_compoundPolymer chemistryPolymethyl MethacrylateBenzhydryl CompoundsMethyl methacrylateFuransBisphenol A diglycidyl etherTetrahydrofuranChromatographyMolar massChemistry PhysicalOrganic Chemistrytechnology industry and agricultureGeneral MedicineEpoxyequipment and suppliesPoly(methyl methacrylate)Molecular Weightbody regionsSolubilitychemistryvisual_artCalibrationChromatography Gelvisual_art.visual_art_mediumEpoxy CompoundsAlgorithmsJournal of Chromatography
researchProduct

Proteins of Muscle and the Cytoskeleton

1994

The contractile elements of striated vertebrate skeletal muscle, the myofibrils, contain thin filaments, which are 6 nm in diameter and consist mainly of actin, and thicker myosin filaments with a diameter of 16 nm (Fig. 10.1). During muscle contraction, the filaments undergo a sliding movement relative to each other (sliding filament mechanism). This is brought about by the reversible formation of bridges between the myosin molecules and the actin filaments, which bind, change their conformation and then dissociate (bridge cycle). The required energy is supplied by the hydrolysis of ATP. The sliding distance (step size) per molecule of ATP hydrolysed is controversial; the most recent measu…

ChemistrySkeletal musclemacromolecular substancesTropomyosinmedicine.anatomical_structureATP hydrolysisMyosinBiophysicsmedicinemedicine.symptomCytoskeletonMyofibrilActinMuscle contraction
researchProduct

High Yield SNAr on 8-Halogenophenyl-BODIPY with Cyclic and Acyclic Polyamines

2014

Selective nucleophilic aromatic substitutions with several polyamines were performed in very good yields on halogeno-phenyl BODIPY derivatives containing an activating nitro group.

ChemistryStereochemistryOrganic Chemistrymacromolecular substancesFluorescenceMedicinal chemistrychemistry.chemical_compoundNucleophileNucleophilic aromatic substitutionYield (chemistry)Nucleophilic substitutionNitroPhysical and Theoretical ChemistryBODIPYEuropean Journal of Organic Chemistry
researchProduct