Search results for "DOMAIN"

showing 10 items of 2485 documents

Boundary elements analysis of adhesively bonded piezoelectric active repair

2009

Abstract This paper presents the analysis of active piezoelectric patches for cracked structures by the boundary element method. A two-dimensional boundary integral formulation based on the multidomain technique is used to model cracks and to assemble the multi-layered piezoelectric patches to the host damaged structures. The fracture mechanics behavior of the repaired structures is analyzed for both perfect and imperfect interface between patches and host beams. The imperfect interface, representing the adhesive between two different layers, is modeled by using a “spring model” that involves linear relationships between the interface tractions, in normal and tangential directions, and the …

CantileverMaterials scienceFissurePiezoelectric sensorbusiness.industryMechanical EngineeringDomain decomposition methodsFracture mechanicsStructural engineeringPiezoelectric materialPiezoelectricityImperfect bondingmedicine.anatomical_structureDiscontinuity (geotechnical engineering)Mechanics of MaterialsActive repairmedicineGeneral Materials ScienceBoundary Element analysiSettore ING-IND/04 - Costruzioni E Strutture AerospazialibusinessBoundary element methodEngineering Fracture Mechanics
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Late Carnian-Early Norian ammonoids from the GSSP candidate section Pizzo Mondello (Sicani mountain, Sicily).

2012

A small collection of ammonoids from the Upper Triassic Scillato Formation at Pizzo Mondello (Agrigento, Sicily) is studied. The specimens were collected in a framework of a project aimed at providing an integrated high-resolution bio-chronostratigraphic support to the Upper Carnian-Norian magnetostratigraphic scale defined at this site, that is located in an historical area from which G.G. Gemmellaro collected the Upper Triassic of ammonoids monographed at the beginning of the XX century. The specimens from Pizzo Mondello were bed-by-bed sampled and represent the first collection of Upper Triassic ammonoids described from Sicily since Gemmellaro time. Quite several levels of the Pizzo Mond…

Carnian/Norian boundarySicanian Domainlcsh:QE1-996.5AmmonoidsBiostratigraphyUpper Triassic; Carnian/Norian boundary; Ammonoids; Biostratigraphy; Sicily; Sicanian Domain; Scillato FormationScillato FormationSettore GEO/01 - Paleontologia E Paleoecologialcsh:GeologyUpper Triassic Norian GSSP Ammonoidea Pizzo Mondello Sicilylcsh:PaleontologyUpper TriassicSicilylcsh:QE701-760
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Fractional p-Laplacian evolution equations

2016

Abstract In this paper we study the fractional p-Laplacian evolution equation given by u t ( t , x ) = ∫ A 1 | x − y | N + s p | u ( t , y ) − u ( t , x ) | p − 2 ( u ( t , y ) − u ( t , x ) ) d y for  x ∈ Ω ,  t > 0 , 0 s 1 , p ≥ 1 . In a bounded domain Ω we deal with the Dirichlet problem by taking A = R N and u = 0 in R N ∖ Ω , and the Neumann problem by taking A = Ω . We include here the limit case p = 1 that has the extra difficulty of giving a meaning to u ( y ) − u ( x ) | u ( y ) − u ( x ) | when u ( y ) = u ( x ) . We also consider the Cauchy problem in the whole R N by taking A = Ω = R N . We find existence and uniqueness of strong solutions for each of the above mentioned problem…

Cauchy problemDirichlet problemApplied MathematicsGeneral Mathematics010102 general mathematicsMathematical analysis01 natural sciences010101 applied mathematicsBounded functionDomain (ring theory)Neumann boundary conditionp-LaplacianInitial value problemUniqueness0101 mathematicsMathematicsMathematical physicsJournal de Mathématiques Pures et Appliquées
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Protein targeting to the plasma membrane of adult skeletal muscle fiber: an organized mosaic of functional domains.

2001

The plasma membrane of differentiated skeletal muscle fibers comprises the sarcolemma, the transverse (T) tubule network, and the neuromuscular and muscle-tendon junctions. We analyzed the organization of these domains in relation to defined surface markers, beta-dystroglycan, dystrophin, and caveolin-3. These markers were shown to exhibit highly organized arrays along the length of the fiber. Caveolin-3 and beta-dystroglycan/dystrophin showed distinct, but to some extent overlapping, labeling patterns and both markers left transverse tubule openings clear. This labeling pattern revealed microdomains over the entire plasma membrane with the exception of the neuromuscular and muscle-tendon j…

Caveolin 3Muscle Fibers SkeletalNeuromuscular JunctionMuscle ProteinsProtein Sorting Signalsmedicine.disease_causeCaveolinsT-tubuleDystrophinMiceMembrane MicrodomainsViral Envelope ProteinsProtein targetingmedicineMyocyteAnimalsDystroglycansMuscle SkeletalGlycoproteinsSarcolemmaMembrane GlycoproteinsbiologyCell MembraneSkeletal muscleCell BiologyMolecular biologyTransport proteinCell biologyRatsCytoskeletal ProteinsProtein Transportmedicine.anatomical_structureTubulebiology.proteinFemaleDystrophinExperimental cell research
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The Odyssey of Hsp60 from Tumor Cells to Other Destinations Includes Plasma Membrane-Associated Stages and Golgi and Exosomal Protein-Trafficking Mod…

2012

BACKGROUND: In a previous work we showed for the first time that human tumor cells secrete Hsp60 via exosomes, which are considered immunologically active microvesicles involved in tumor progression. This finding raised questions concerning the route followed by Hsp60 to reach the exosomes, its location in them, and whether Hsp60 can be secreted also via other mechanisms, e.g., by the Golgi. We addressed these issues in the work presented here. PRINCIPAL FINDINGS: We found that Hsp60 localizes in the tumor cell plasma membrane, is associated with lipid rafts, and ends up in the exosomal membrane. We also found evidence that Hsp60 localizes in the Golgi apparatus and its secretion is prevent…

Cell Physiologyanimal structuresAnatomy and PhysiologyHistologylcsh:MedicineGolgi ApparatusBiologyExosomesBiochemistrysymbols.namesakeCytosolMembrane MicrodomainsDiagnostic MedicineCell Line TumorOrganelleMolecular Cell BiologyPathologyHumansSecretionlcsh:ScienceLipid raftBiologyhsp60 exosomeOrganellesMultidisciplinarylcsh:RfungiChaperonin 60Golgi apparatusMicrovesiclesCellular StructuresTransport proteinCell biologyProtein TransportMembrane proteinSubcellular OrganellesTumor progressionsymbolsCytochemistryMedicinelcsh:QMembranes and SortingExtracellular SpaceBiomarkersResearch ArticleGeneral PathologyPLoS ONE
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Ensemble-based ADME-Tox profiling and virtual screening for the discovery of new inhibitors of the Leishmania mexicana cysteine protease CPB2.8ΔCTE

2018

Abstract: In an effort to identify novel molecular warheads able to inhibit Leishmania mexicana cysteine protease CPB2.8CTE, fused benzo[b]thiophenes and ,'-triketones emerged as covalent inhibitors binding the active site cysteine residue. Enzymatic screening showed a moderate-to-excellent activity (12%-90% inhibition of the target enzyme at 20m). The most promising compounds were selected for further profiling including in vitro cell-based assays and docking studies. Computational data suggest that benzo[b]thiophenes act immediately as non-covalent inhibitors and then as irreversible covalent inhibitors, whereas a reversible covalent mechanism emerged for the 1,3,3'-triketones with a Y-to…

Cell SurvivalLeishmania mexicanaProtozoan ProteinsADME-Tox; Benzo[b]thiophenes; Cysteine protease; Leishmaniasis; TriketonesThiophenesCysteine Proteinase Inhibitors010402 general chemistry01 natural sciencesBiochemistryLeishmania mexicanaCysteine Proteinase InhibitorsCell LineInhibitory Concentration 50Structure-Activity RelationshipCysteine ProteasesCatalytic DomainDrug DiscoveryHumansStructure–activity relationshipcysteine proteaseBinding siteADME-Tox; benzo[b]thiophenes; cysteine protease; leishmaniasis; triketones; Biochemistry; Molecular MedicineBiologyleishmaniasisPharmacologychemistry.chemical_classificationVirtual screeningBinding Sitesbiology010405 organic chemistryPharmacology. TherapyOrganic Chemistrytriketonesbiology.organism_classificationCysteine protease0104 chemical sciencesMolecular Docking SimulationChemistryEnzymeBiochemistrychemistryDocking (molecular)ADME-ToxMolecular Medicinebenzo[b]thiophenes
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Vitamin E transport, membrane incorporation and cell metabolism: Is α-tocopherol in lipid rafts an oar in the lifeboat?

2010

International audience; Vitamin E is composed of closely related compounds, including tocopherols and tocotrienols. Studies of the last decade provide strong support for a specific role of alpha-tocopherol in cell signalling and the regulation of gene expression. It produces significant effects on inflammation, cell proliferation and apoptosis that are not shared by other vitamin E isomers with similar antioxidant properties. The different behaviours of vitamin E isomers might relate, at least in part, to the specific effects they exert at the plasma membrane. alpha-Tocopherol is not randomly distributed throughout the phospholipid bilayer of biological membranes, and as compared with other…

Cell deathAntioxidant[ SDV.AEN ] Life Sciences [q-bio]/Food and Nutrition[SDV]Life Sciences [q-bio]medicine.medical_treatmentalpha-TocopherolSignal transductionBiologyAntioxidants03 medical and health scienceschemistry.chemical_compoundMembrane Microdomains0302 clinical medicineATP Binding Cassette Transporter Subfamily B Member 3medicineHumansVitamin ETocopherolATP Binding Cassette Transporter Subfamily B Member 2Protein PrecursorsLipid bilayerLipid raftLDL-Receptor Related Proteins030304 developmental biology0303 health sciencesTocopherolVitamin ECell MembraneBiological TransportBiological membraneLipid metabolismPeptide FragmentsCell biology[SDV] Life Sciences [q-bio]Lipid raftIntestinal AbsorptionLiverReceptors LDLBiochemistrychemistryATP-Binding Cassette Transporterslipids (amino acids peptides and proteins)Antioxidantalpha-Tocopherol[SDV.AEN]Life Sciences [q-bio]/Food and Nutrition030217 neurology & neurosurgeryFood ScienceBiotechnologyMolecular Nutrition & Food Research
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Vascular niche factor PEDF modulates Notch-dependent stemness in the adult subependymal zone.

2009

We sought to address the fundamental question of how stem cell microenvironments can regulate self-renewal. We found that Notch was active in astroglia-like neural stem cells (NSCs), but not in transit-amplifying progenitors of the murine subependymal zone, and that the level of Notch transcriptional activity correlated with self-renewal and multipotency. Moreover, dividing NSCs appeared to balance renewal with commitment via controlled segregation of Notch activity, leading to biased expression of known (Hes1) and previously unknown (Egfr) Notch target genes in daughter cells. Pigment epithelium-derived factor (PEDF) enhanced Notch-dependent transcription in cells with low Notch signaling,…

Cell divisionTranscription GeneticNotch signaling pathwayGene ExpressionBiologyMicePEDFEpendymaSubependymal zoneBasic Helix-Loop-Helix Transcription FactorsAnimalsNuclear Receptor Co-Repressor 1Nerve Growth FactorsProgenitor cellHES1Receptor Notch1Eye ProteinsCells CulturedSerpinsHomeodomain ProteinsNeuronsTranscription Factor HES-1General NeuroscienceAge FactorsTranscription Factor RelACell DifferentiationNeural stem cellErbB ReceptorsAdult Stem CellsTranscription Factor HES-1NeuroscienceSignal TransductionNature neuroscience
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The Functional Role of the Second NPXY Motif of the LRP1 β-Chain in Tissue-type Plasminogen Activator-mediated Activation of N-Methyl-D-aspartate Rec…

2008

The low density lipoprotein receptor-related protein 1 (LRP1) emerges to play fundamental roles in cellular signaling pathways in the brain. One of its prominent ligands is the serine proteinase tissue-type plasminogen activator (tPA), which has been shown to act as a key activator of neuronal mitogen-activated protein kinase pathways via the N-methyl-D-aspartate (NMDA) receptor. However, here we set out to examine whether LRP1 and the NMDA receptor might eventually act in a combined fashion to mediate tPA downstream signaling. By blocking tPA from binding to LRP1 using the receptor-associated protein, we were able to completely inhibit NMDA receptor activation. Additionally, inhibition of …

Cell signalingAmino Acid MotifsPDZ domainIntracellular SpaceBiologyReceptors N-Methyl-D-AspartateBiochemistryProtein Structure SecondaryCell LineRats Sprague-DawleyMiceStructure-Activity RelationshipAnimalsHumansAmino Acid SequencePhosphorylationRNA Small InterferingReceptorProtein kinase AMolecular BiologyMitogen-Activated Protein Kinase 1NeuronsMitogen-Activated Protein Kinase 3Activator (genetics)Intracellular Signaling Peptides and ProteinsMembrane ProteinsReceptor Cross-TalkCell BiologyLRP1RatsCell biologyEnzyme ActivationBiochemistryTissue Plasminogen ActivatorDisks Large Homolog 4 ProteinCalciumDisks Large Homolog 4 ProteinGuanylate KinasesPlasminogen activatorLow Density Lipoprotein Receptor-Related Protein-1PlasmidsSignal TransductionJournal of Biological Chemistry
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α-Secretase Activity of the Disintegrin Metalloprotease ADAM 10: Influences of Domain Structure

2001

Disintegrin metalloproteases from different organisms form the ADAM (a disintegrin and metalloprotease) family. All members display a common domain organization and possess four potential functions: proteolysis, cell adhesion, cell fusion, and cell signaling. Members of the ADAM family are responsible for the proteolytic cleavage of transmembrane proteins and release of their extracellular domain. The proteolytic process is referred to as ectodomain shedding, which is activated by phorbol esters and inhibited by hydroxamic acid-based inhibitors. We have shown that the disintegrin metalloprotease ADAM 10 has both constitutive and regulated alpha-secretase activity. Expression of a dominant n…

Cell signalingDisintegrinsMolecular Sequence DataProtein domainBiologyGeneral Biochemistry Genetics and Molecular BiologyADAM10 ProteinAmyloid beta-Protein PrecursorHistory and Philosophy of ScienceEndopeptidasesDisintegrinAnimalsAspartic Acid EndopeptidasesHumansProtease InhibitorsAmino Acid SequenceCell adhesionMetalloproteinaseGeneral NeuroscienceHEK 293 cellsMembrane ProteinsMetalloendopeptidasesRecombinant ProteinsTransmembrane proteincarbohydrates (lipids)ADAM ProteinsBiochemistryEctodomainbiology.proteinAmyloid Precursor Protein SecretasesProtein Processing Post-TranslationalAnnals of the New York Academy of Sciences
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