Search results for "oligo"

showing 10 items of 1298 documents

Synthesis and activity of phosphinic tripeptide inhibitors of cathepsin C

2004

Phosphinic tripeptide analogues Gly-Xaaψ[P(O)(OH)CH2]-Gly have been developed as inhibitors of cathepsin C (DPP I), a lysosomal, papain-like cysteine protease. The target compounds were synthesised by addition of methyl acrylate to the appropriate phosphinic acids followed by the N-terminus elongation using mixed anhydride procedure. The latter step has been demonstrated to be a suitable method for N-terminal extension of the phosphinic pseudopeptide analogues without requirement of hydroxyphosphinyl protection. The title compounds appeared to be moderate inhibitors of the cathepsin C. However, although designed as transition state analogues, they surprisingly exhibited noncompetitive mode …

Cathepsinchemistry.chemical_classificationnoncompetitive inhibitionStereochemistryphosphinic tripeptidesOrganic ChemistryClinical BiochemistryPharmaceutical ScienceBiological activityPeptideTripeptidePhosphinic AcidsBiochemistryCysteine proteaseChemical synthesisCathepsin CCathepsin CNon-competitive inhibitionchemistryDrug DiscoveryMolecular MedicineProtease InhibitorsOligopeptidesMolecular BiologyBioorganic & Medicinal Chemistry Letters
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Powerful Fluoroalkoxy Molybdenum(V) Reagent for Selective Oxidative Arene Coupling Reaction

2013

We introduce the novel fluoroalkoxy molybdenum(V) reagent 1 which has superior reactivity and selectivity in comparison to MoCl5 or the MoCl5 /TiCl4 reagent mixture in the oxidative coupling reactions of aryls. Common side reactions, such as chlorination and/or oligomer formation, are drastically diminished creating a powerful and useful reagent for oxidative coupling. Theoretical treatment of the reagent interaction with 1,2-dimethoxybenzene-type substrates indicates an inner-sphere electron transfer followed by a radical cationic reaction pathway for the oxidative-coupling process. EPR spectroscopic and electrochemical studies, X-ray analyses, computational investigations, and the experim…

Cationic polymerizationGeneral ChemistryPhotochemistryCombinatorial chemistryOligomerCatalysisCoupling reactionchemistry.chemical_compoundElectron transferchemistryReagentReactivity (chemistry)Oxidative coupling of methaneSelectivityAngewandte Chemie International Edition
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Nuclear receptors modulate the interaction of Sp1 and GC-rich DNA via ternary complex formation

2000

Binding sites for transcription factor Sp1have been implicated in the transcriptional regulation of several genes by hormones or vitamins, and here we show that a GC-rich element contributes to the retinoic acid response of the interleukin 1β promoter. To explain such observations, it has been proposed that nuclear receptors can interact with Sp1 bound to GC-rich DNA. However, evidence supporting this model has remained indirect. So far, nuclear receptors have not been detected in a complex with Sp1 and GC-rich DNA, and the expected ternary complexes in non-denaturing gels were not seen. In search for these missing links we found that nuclear receptors [retinoic acid receptor (RAR), thyroid…

Cell ExtractsTranscriptional ActivationReceptors Retinoic AcidSp1 Transcription FactorRecombinant Fusion ProteinsReceptors Cytoplasmic and NuclearTretinoinRetinoic acid receptor betaBiologyRetinoid X receptorLigandsResponse ElementsTransfectionModels BiologicalBiochemistryAntibodiesCell LineSubstrate SpecificityAnimalsPromoter Regions GeneticMolecular BiologyNuclear receptor co-repressor 1Nuclear receptor co-repressor 2Binding SitesReceptors Thyroid HormoneDNACell BiologyRetinoic acid receptor gammaRetinoid X receptor gammaGC Rich SequenceProtein Structure TertiaryNuclear receptor coactivator 1Retinoic acid receptorDrosophila melanogasterEcdysteroneRetinoid X ReceptorsOligodeoxyribonucleotidesBiochemistryReceptors CalcitriolThermodynamicsResearch ArticleInterleukin-1Protein BindingTranscription FactorsBiochemical Journal
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Streptolysin O: the C-terminal, tryptophan-rich domain carries functional sites for both membrane binding and self-interaction but not for stable oli…

2001

AbstractStreptolysin O belongs to the class of thiol-activated toxins, which are single chain, four-domain proteins that bind to membranes containing cholesterol and then assemble to form large oligomeric pores. Membrane binding involves a conserved tryptophan-rich sequence motif located within the C-terminally located domain 4. In contrast, sites involved in oligomerization and pore formation have been assigned to domains 1 and 3, respectively. We here examined the functional properties of domain 4, which was recombinantly expressed with an N-terminal histidine tag for purification and an additional cysteine residue for covalent labeling. The fluorescently labeled fragment readily bound to…

Cell Membrane PermeabilityMembrane bindingProtein ConformationBiophysicsPlasma protein bindingBiochemistryThiol-activated toxinStructure-Activity RelationshipProtein structureBacterial ProteinsProtein oligomerizationHumansProtein oligomerizationBinding sitePore-forming toxinBinding SitesChemistryErythrocyte MembraneCell BiologyMembraneBiochemistryMutationStreptolysinsBiophysicsPore-forming toxinFluoresceinStreptolysinSequence motifProtein BindingBiochimica et Biophysica Acta (BBA) - Biomembranes
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Assembly mechanism of the oligomeric streptolysin O pore: the early membrane lesion is lined by a free edge of the lipid membrane and is extended gra…

1998

Streptolysin O (SLO) is a bacterial exotoxin that binds to cell membranes containing cholesterol and then oligomerizes to form large pores. Along with rings, arc-shaped oligomers form on membranes. It has been suggested that each arc represents an incompletely assembled oligomer and constitutes a functional pore, faced on the opposite side by a free edge of the lipid membrane. We sought functional evidence in support of this idea by using an oligomerization-deficient, non-lytic mutant of SLO. This protein, which was created by chemical modification of a single mutant cysteine (T250C) with N-(iodoacetaminoethyl)-1-naphthylamine-5-sulfonic acid, formed hybrid oligomers with active SLO on memb…

Cell Membrane PermeabilityProtein ConformationMembrane lipidsBiologyCholesterol-dependent cytolysinComplement Hemolytic Activity AssayOligomerGeneral Biochemistry Genetics and Molecular BiologyMembrane Lipidschemistry.chemical_compoundBacterial ProteinsNaphthalenesulfonatesAnimalsProtein oligomerizationCysteineLipid bilayerMolecular BiologyGeneral Immunology and MicrobiologyGeneral NeuroscienceErythrocyte MembraneCalceinMembranechemistryBiochemistryMutationStreptolysinsBiophysicsStreptolysinRabbitsResearch ArticleThe EMBO Journal
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Oligodendroglial p130Cas Is a Target of Fyn Kinase Involved in Process Formation, Cell Migration and Survival

2014

Oligodendrocytes are the myelinating glial cells of the central nervous system. In the course of brain development, oligodendrocyte precursor cells migrate, scan the environment and differentiate into mature oligodendrocytes with multiple cellular processes which recognize and ensheath neuronal axons. During differentiation, oligodendrocytes undergo dramatic morphological changes requiring cytoskeletal rearrangements which need to be tightly regulated. The non-receptor tyrosine kinase Fyn plays a central role in oligodendrocyte differentiation and myelination. In order to improve our understanding of the role of oligodendroglial Fyn kinase, we have identified Fyn targets in these cells. Pur…

Cell Survival610 Medizinlcsh:MedicineProto-Oncogene Proteins c-fynSignaling PathwaysMiceCell Movement610 Medical sciencesMolecular Cell BiologyAnimalsPhosphorylationlcsh:ScienceBiologyCells CulturedNeuronslcsh:RCell DifferentiationMolecular DevelopmentSignalingAxonsOligodendrogliaCrk-Associated Substrate ProteinCellular Neurosciencelcsh:QCellular TypesMolecular NeuroscienceResearch ArticleDevelopmental BiologyNeurosciencePLoS ONE
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Inulin-Ethylenediamine Coated SPIONs Magnetoplexes: A Promising Tool for Improving siRNA Delivery.

2015

An inulin based polycation (Inu-EDA) has been synthesized by the grafting of ethylenediamine molecules onto inulin backbone. The obtained inulin copolymer has been though to coat SPIONs (IC-SPIONs) and obtain stable magnetoplexes by complexation of IC-SPIONs with a model duplexed siRNA, for improving oligonucleotide transfection efficiency.The physical-chemical characteristics of IC-SPIONs and IC-SPIONs/siRNA magnetoplexes have been investigated by scanning and transmission electron microscopies, dynamic light scattering, FT-IR and qualitative surface elementary analysis. Cell compatibility and internalization in vitro of IC-SPIONs have been evaluated by MTS and fluorescence microscopy resp…

Cell SurvivalSurface PropertiesDrug CompoundingInulinPharmaceutical ScienceTransfectionpolycationchemistry.chemical_compoundDynamic light scatteringMicroscopy Electron TransmissionSpectroscopy Fourier Transform InfraredFluorescence microscopeHumansPharmacology (medical)Particle SizeRNA Small InterferingMagnetite NanoparticlesPharmacologyDrug CarriersChemistryOligonucleotideOrganic ChemistryInulinTransfectionEthylenediaminesHCT116 CellsIn vitroFerrosoferric OxideSPIONsTargeted drug deliveryBiochemistryCell cultureinulin; magnetoplexes; polycation; siRNA; SPIONssiRNABiophysicsMicroscopy Electron ScanningMolecular Medicineinulin magnetoplexes polycation siRNA SPIONsBiotechnologymagnetoplexesPharmaceutical research
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Multiple sclerosis patient-derived CSF induces transcriptional changes in proliferating oligodendrocyte progenitors.

2014

Background: Cerebrospinal fluid (CSF) is in contact with brain parenchyma and ventricles, and its composition might influence the cellular physiology of oligodendrocyte progenitor cells (OPCs) thereby contributing to multiple sclerosis (MS) disease pathogenesis. Objective: To identify the transcriptional changes that distinguish the transcriptional response induced in proliferating rat OPCs upon exposure to CSF from primary progressive multiple sclerosis (PPMS) or relapsing remitting multiple sclerosis (RRMS) patients and other neurological controls. Methods: We performed gene microarray analysis of OPCs exposed to CSF from neurological controls, or definitive RRMS or PPMS disease course. R…

Cell physiologyAdultPathologymedicine.medical_specialtyTranscription GeneticGalectin 3GalectinsImmunocytochemistryBiologyArticleCerebrospinal fluidMultiple Sclerosis Relapsing-RemittingNeural Stem CellsmedicineAnimalsHumansProgenitor cellCells CulturedCell ProliferationCerebrospinal FluidMultiple sclerosisBrainHuman brainBlood ProteinsMultiple Sclerosis Chronic Progressivemedicine.diseaseMicroarray AnalysisNeural stem cellOligodendrocyteRatsUp-RegulationOligodendrogliamedicine.anatomical_structureNeurologyNeurology (clinical)Multiple sclerosis (Houndmills, Basingstoke, England)
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In Vivo Imaging of Partially Reversible Th17 Cell-Induced Neuronal Dysfunction in the Course of Encephalomyelitis

2010

SummaryNeuronal damage in autoimmune neuroinflammation is the correlate for long-term disability in multiple sclerosis (MS) patients. Here, we investigated the role of immune cells in neuronal damage processes in animal models of MS by monitoring experimental autoimmune encephalomyelitis (EAE) by using two-photon microscopy of living anaesthetized mice. In the brainstem, we detected sustained interaction between immune and neuronal cells, particularly during disease peak. Direct interaction of myelin oligodendrocyte glycoprotein (MOG)-specific Th17 and neuronal cells in demyelinating lesions was associated with extensive axonal damage. By combining confocal, electron, and intravital microsc…

Cell signalingPathologymedicine.medical_specialtyEncephalomyelitis Autoimmune ExperimentalEncephalomyelitisImmunologyApoptosisCell CommunicationBiologyReceptors N-Methyl-D-AspartateMyelin oligodendrocyte glycoproteinMiceImmune systemCell MovementmedicineAnimalsImmunology and AllergyNeuroinflammationCells CulturedNeuronsMultiple sclerosisExperimental autoimmune encephalomyelitisInterleukin-17T-Lymphocytes Helper-Inducermedicine.diseaseAxonsCell biologyMice Inbred C57BLInfectious Diseasesnervous systemSynapsesbiology.proteinCalciumIntravital microscopyImmunity
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Endothelial transcriptomic changes induced by oxidized low density lipoprotein disclose an up-regulation of Jak-Stat pathway.

2015

Oxidized low density lipoproteins (oxLDLs) act as an etiological factor in the development of atherosclerosis by modifying the biological properties of endothelial cells through mechanisms of vascular inflammation. To deepen the oxLDL changes at cellular level, a transcriptomic analysis of human umbilical artery endothelial cells (HUAECs) treated with oxLDL was performed to identify the modified signaling pathways. Total RNA was isolated from HUAECs treated with oxLDL (100 μg/ml). Gene expression analysis was carried out using Affymetrix oligonucleotide microarrays. Biological pathway analysis was performed using Ingenuity Pathway Analysis software. Microarray assay demonstrated that oxLDL …

Cell signalingTime FactorsPhysiologyBlotting WesternBiologyReal-Time Polymerase Chain ReactionTransfectionGene Expression Regulation EnzymologicBiological pathwayTranscriptomeRNA interferenceGene expressionHuman Umbilical Vein Endothelial CellsHumansGene Regulatory NetworksProtein Kinase InhibitorsCells CulturedOligonucleotide Array Sequence AnalysisPharmacologyGene Expression ProfilingJAK-STAT signaling pathwaySTAT2 Transcription FactorJanus Kinase 1Janus Kinase 2Cell biologyEndothelial stem cellLipoproteins LDLSTAT1 Transcription FactorMolecular Medicinelipids (amino acids peptides and proteins)RNA InterferenceSignal transductionTranscriptomeSignal TransductionVascular pharmacology
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