Search results for "DASES"

showing 10 items of 485 documents

1,2,4-Oxadiazole topsentin analogs as staphylococcal biofilm inhibitors targeting the bacterial transpeptidase sortase A

2020

The inhibition or prevention of biofilm formation represents an emerging strategy in the war against antibiotic resistance, interfering with key players in bacterial virulence. This approach includes the inhibition of the catalytic activity of transpeptidase sortase A (Srt A), a membrane enzyme responsible for covalently attaching a wide variety of adhesive matrix molecules to the peptidoglycan cell wall in Gram-positive strains. A new series of seventeen 1,2,4-oxadiazole derivatives was efficiently synthesized and screened as potential new anti-virulence agents. The ability of inhibiting biofilm formation was evaluated against both Gram-positive and Gram-negative pathogens. Remarkably, all…

Indoles124-Oxadiazoles Antibiofilm activity Sortase A inhibitors Anti-virulence agents Marine alkaloids Topsentin analogs01 natural scienceslaw.inventionchemistry.chemical_compoundMarine alkaloidslawDrug DiscoveryPathogenchemistry.chemical_classificationOxadiazoles0303 health sciencesChemistry4-OxadiazolesImidazolesGeneral MedicineStaphylococcal InfectionsAminoacyltransferasesAnti-Bacterial AgentsCysteine EndopeptidasesAnti-virulence agentsBiochemistrySortase AAntibiofilm activityPseudomonas aeruginosaTopsentin analogsRecombinant DNA124-Oxadiazoles; Anti-virulence agents; Antibiofilm activity; Marine alkaloids; Sortase A inhibitors; Topsentin analogsStaphylococcus aureus12Sortase A inhibitorsCell LineCell wall03 medical and health sciencesAntibiotic resistanceBacterial Proteins124-OxadiazolesHumansPseudomonas Infections030304 developmental biologyPharmacology010405 organic chemistryOrganic ChemistryBiofilmSettore CHIM/08 - Chimica Farmaceutica0104 chemical sciencesEnzymeBiofilmsPeptidoglycan
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Development of novel dipeptide-like rhodesain inhibitors containing the 3-bromoisoxazoline warhead in a constrained conformation.

2015

Novel dipeptide-like rhodesain inhibitors containing the 3-bromoisoxazoline warhead in a constrained conformation were developed; some of them possess K(i) values in the micromolar range. We studied the structure-activity relationship of these derivatives and we performed docking studies, which allowed us to find out the key interactions established by the inhibitors with the target enzyme. Biological results indicate that the nature of the P2 and P3 substituents and their binding to the S2/S3 pockets is strictly interdependent.

InhibitorMolecular modelCell SurvivalClinical BiochemistryTrypanosoma brucei bruceiAntiprotozoal AgentsPharmaceutical ScienceMolecular modelingCysteine Proteinase InhibitorsBiochemistryCell Linechemistry.chemical_compoundMiceStructure-Activity RelationshipCysteine ProteasesDrug DiscoveryAnimalsMolecular Biology3-Bromo isoxazolinechemistry.chemical_classificationDipeptide-likeDipeptideBinding SitesOrganic ChemistryDipeptidesIsoxazolesCombinatorial chemistryProtein Structure TertiaryMolecular Docking SimulationCysteine EndopeptidasesEnzymeRhodesainchemistryWarheadDocking (molecular)Drug DesignMolecular MedicineRhodesain Dipeptide-like 3-Bromo isoxazoline Inhibitor Molecular modelingBioorganicmedicinal chemistry
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A novel target of lithium therapy.

2000

Phosphatases converting 3'-phosphoadenosine 5'-phosphate (PAP) into adenosine 5'-phosphate are of fundamental importance in living cells as the accumulation of PAP is toxic to several cellular systems. These enzymes are lithium-sensitive and we have characterized a human PAP phosphatase as a potential target of lithium therapy. A cDNA encoding a human enzyme was identified by data base screening, expressed in Escherichia coli and the 33 kDa protein purified to homogeneity. The enzyme exhibits high affinity for PAP (K(m)1 microM) and is sensitive to subtherapeutic concentrations of lithium (IC(50)=0.3 mM). The human enzyme also hydrolyzes inositol-1, 4-bisphosphate with high affinity (K(m)=0…

Inositol-14-bisphosphateDNA ComplementaryBicinePhosphataseMolecular Sequence DataBiophysicschemistry.chemical_elementSaccharomyces cerevisiaeLithiummedicine.disease_causeBiochemistrychemistry.chemical_compoundStructural BiologyNucleotidasesComplementary DNAPhosphataseGeneticsmedicineEscherichia coliHumansAmino Acid SequenceCloning MolecularMolecular BiologyEscherichia coliIC50Chromatography High Pressure Liquidchemistry.chemical_classificationExpressed Sequence TagsBase Sequence3′-Phosphoadenosine 5′-phosphateCell BiologyMolecular biologyAdenosineAdenosine MonophosphatePhosphoric Monoester HydrolasesAdenosine DiphosphateEnzymechemistryBiochemistryLithiummedicine.drugHumanFEBS letters
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Proteolytic processing of Bacillus thuringiensis Vip3A proteins by two Spodoptera species

2014

Abstract Vip3 proteins have been described to be secreted by Bacillus thuringiensis during the vegetative growth phase and to display a broad insecticidal spectrum against lepidopteran larvae. Vip3Aa protoxin has been reported to be significantly more toxic to Spodoptera frugiperda than to Spodoptera exigua and differences in the midgut processing have been proposed to be responsible. In contrast, we have found that Vip3Ae is essentially equally toxic against these two species. Proteolysis experiments were performed to study the stability of Vip3A proteins to peptidase digestion and to see whether the differences found could explain differences in toxicity against these two Spodoptera speci…

InsecticidesPhysiologyProteolysisBacterial ProteinSpodopteraSpodopteraMicrobiologyVegetative insecticidal proteinBacterial ProteinsSpecies SpecificitySpodoptera exiguaBacillus thuringiensisExiguamedicineAnimalsPest Control BiologicalMidgut peptidaseInsecticideChymotrypsinbiologymedicine.diagnostic_testAnimalMedicine (all)Serine EndopeptidasesfungiSpodoptera frugiperdaMidgutbiology.organism_classificationTrypsinSerine EndopeptidaseSerine peptidaseBiochemistryMode of actionLarvaInsect Sciencebiology.proteinDigestionDigestive Systemmedicine.drugJournal of Insect Physiology
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Interaction of antibodies to proteinase 3 (classic anti-neutrophil cytoplasmic antibody) with human renal tubular epithelial cells: impact on signali…

2002

Abstract Among the anti-neutrophil cytoplasmic Abs (ANCA), those targeting proteinase 3 (PR3) have a high sensitivity and specificity for Wegener’s granulomatosis (WG). A pathogenetic role for these autoantibodies has been proposed due to their capacity of activating neutrophils in vitro. Recently, PR3 was also detected in human renal tubular epithelial cells (TEC). In the present study, the effect of murine monoclonal anti-PR3 Abs (anti-PR3) and purified c-ANCA targeting PR3 from WG serum on isolated human renal tubular cell signaling and inflammatory mediator release was characterized. Priming of TEC with TNF-α resulted in surface expression of PR3, as quantified in immunofluorescence stu…

Intracellular Fluidmedicine.medical_specialtyMyeloblastinImmunologyImmunofluorescencePhosphatidylinositolsAutoantigensDinoprostoneFlow cytometryAntibodies Antineutrophil CytoplasmicAntigen-Antibody ReactionsThromboxane A2Proteinase 3SuperoxidesInternal medicinemedicineCyclic AMPImmunology and AllergyHumanscardiovascular diseasesCells CulturedArachidonic Acidmedicine.diagnostic_testbiologyHydrolysisImmune SeraCell MembraneSerine EndopeptidasesAntibodies MonoclonalEpithelial CellsLipid signalingIn vitroCell biologyEndocrinologyKidney Tubulesbiology.proteinCyclooxygenaseSignal transductionInflammation MediatorsIntracellularSignal TransductionJournal of immunology (Baltimore, Md. : 1950)
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Yeast Dun1 Kinase Regulates Ribonucleotide Reductase Inhibitor Sml1 in Response to Iron Deficiency

2014

Iron is an essential micronutrient for all eukaryotic organisms because it participates as a redox-active cofactor in many biological processes, including DNA replication and repair. Eukaryotic ribonucleotide reductases (RNRs) are Fe-dependent enzymes that catalyze deoxyribonucleoside diphosphate (dNDP) synthesis. We show here that the levels of the Sml1 protein, a yeast RNR large-subunit inhibitor, specifically decrease in response to both nutritional and genetic Fe deficiencies in a Dun1-dependent but Mec1/Rad53- and Aft1-independent manner. The decline of Sml1 protein levels upon Fe starvation depends on Dun1 forkhead-associated and kinase domains, the 26S proteasome, and the vacuolar pr…

Iron-Sulfur ProteinsProteasome Endopeptidase ComplexSaccharomyces cerevisiae ProteinsDeoxyribonucleoside triphosphateRibonucleotideIronDeoxyribonucleotidesGenes FungalSaccharomyces cerevisiaeCell Cycle ProteinsSaccharomyces cerevisiaeRibonucleotide reductase inhibitorProtein Serine-Threonine KinasesBiologyProtein degradationchemistry.chemical_compoundTristetraprolinRibonucleotide ReductasesAspartic Acid EndopeptidasesPhosphorylationMolecular BiologyCheckpoint Kinase 2Binding SitesKinaseIntracellular Signaling Peptides and ProteinsArticlesCell Biologybiology.organism_classificationDNA-Binding ProteinsDeoxyribonucleosideCheckpoint Kinase 2chemistryBiochemistryProteolysisGene DeletionTranscription FactorsMolecular and Cellular Biology
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Priming for JA-dependent defenses using hexanoic acid is an effective mechanism to protect Arabidopsis against B. cinerea

2011

Abstract Soil drench treatments with hexanoic acid can effectively protect Arabidopsis plants against Botrytis cinerea through a mechanism based on a stronger and faster accumulation of JA-dependent defenses. Plants impaired in ethylene, salicylic acid, abscisic acid or glutathion pathways showed intact protection by hexanoic acid upon B. cinerea infection. Accordingly, no significant changes in the SA marker gene PR-1 in either the SA or ABA hormone balance were observed in the infected and treated plants. In contrast, the JA signaling pathway showed dramatic changes after hexanoic acid treatment, mainly when the pathogen was present. The impaired JA mutants, jin1-2 and jar1 , were unable …

Jasmonic acid pathwaysPhysiologyMutantArabidopsisCyclopentanesPlant ScienceMicrobiologyDefensinschemistry.chemical_compoundBotrytis cinereaAnti-Infective AgentsPlant Growth RegulatorsHexanoic AcidGene Expression Regulation PlantArabidopsisEndopeptidasesPlant ImmunityOxylipinsCaproatesGlucansAbscisic acidPlant DiseasesPlant ProteinsBotrytis cinereaHexanoic acidbiologyArabidopsis ProteinsJasmonic acidCallosefungiAlternariafood and beveragesArabidopsis mutantsEthylenesPlants Genetically Modifiedbiology.organism_classificationGlutathionePlant LeaveschemistryBiochemistryPrimingMutationBotrytisSalicylic AcidAgronomy and Crop ScienceSalicylic acidAbscisic AcidSignal Transduction
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Proteomic Analyses Reveal an Acidic Prime Side Specificity for the Astacin Metalloprotease Family Reflected by Physiological Substrates

2011

Astacins are secreted and membrane-bound metalloproteases with clear associations to many important pathological and physiological processes. Yet with only a few substrates described their biological roles are enigmatic. Moreover, the lack of knowledge of astacin cleavage site specificities hampers assay and drug development. Using PICS (proteomic identification of protease cleavage site specificity) and TAILS (terminal amine isotopic labeling of substrates) degradomics approaches >3000 cleavage sites were proteomically identified for five different astacins. Such broad coverage enables family-wide determination of specificities N- and C-terminal to the scissile peptide bond. Remarkably, me…

KeratinocytesModels MolecularProteomicsVascular Endothelial Growth Factor AProteasesmedicine.medical_treatmentProteolysisMolecular Sequence DataBiologyCleavage (embryo)BiochemistryCell LineSubstrate SpecificityAnalytical Chemistry03 medical and health sciencesTandem Mass SpectrometrymedicineHumansAmino Acid SequenceMolecular BiologyPeptide sequencePhylogeny030304 developmental biologyEnzyme Precursors0303 health sciencesProteaseStaining and LabelingEdman degradationmedicine.diagnostic_testResearch030302 biochemistry & molecular biologyTioproninMetalloendopeptidasesTerminal amine isotopic labeling of substratesRecombinant ProteinsKineticsBiochemistryProteolysisKallikreinsAstacinPeptidesSequence AlignmentChromatography LiquidMolecular & Cellular Proteomics
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The α and β Subunits of the Metalloprotease Meprin Are Expressed in Separate Layers of Human Epidermis, Revealing Different Functions in Keratinocyte…

2007

The zinc endopeptidase meprin (EC 3.4.24.18) is expressed in brush border membranes of intestine and kidney tubules, intestinal leukocytes, and certain cancer cells, suggesting a role in epithelial differentiation and cell migration. Here we show by RT-PCR and immunoblotting that meprin is also expressed in human skin. As visualized by immunohistochemistry, the two meprin subunits are localized in separate cell layers of the human epidermis. Meprin alpha is expressed in the stratum basale, whereas meprin beta is found in cells of the stratum granulosum just beneath the stratum corneum. In hyperproliferative epidermis such as in psoriasis vulgaris, meprin alpha showed a marked shift of expre…

KeratinocytesPathologymedicine.medical_specialtyCell SurvivalCellular differentiationStratum granulosumHuman skinCell CountDermatologyBiologyBiochemistryCell Line03 medical and health sciencesmedicineHumansMolecular Biology030304 developmental biologyCell Proliferation0303 health sciencesMeprin AEpidermis (botany)integumentary systemCell growth030302 biochemistry & molecular biologyMetalloendopeptidasesCell DifferentiationCell BiologyCell biologymedicine.anatomical_structureEpidermal CellsGene Expression RegulationKallikreinsEpidermisKeratinocyteStratum basaleJournal of Investigative Dermatology
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Processing of procollagen III by meprins: new players in extracellular matrix assembly?

2010

Meprins α and β, a subgroup of zinc metalloproteinases belonging to the astacin family, are known to cleave components of the extracellular matrix, either during physiological remodeling or in pathological situations. In this study we present a new role for meprins in matrix assembly, namely the proteolytic processing of procollagens. Both meprins α and β release the N- and C-propeptides from procollagen III, with such processing events being critical steps in collagen fibril formation. In addition, both meprins cleave procollagen III at exactly the same site as the procollagen C-proteinases, including bone morphogenetic protein-1 (BMP-1) and other members of the tolloid proteinase family. …

Keratinocytesmacromolecular substancesDermatologyMatrix metalloproteinaseCleavage (embryo)BiochemistryBone Morphogenetic Protein 1Substrate SpecificityExtracellular matrix03 medical and health sciencesDermismedicineHumansEnhancerMolecular BiologyCells Cultured030304 developmental biology0303 health sciencesExtracellular Matrix Proteinsintegumentary systemChemistryExtracellular matrix assembly030302 biochemistry & molecular biologyMetalloendopeptidasesCell BiologyDermisFibroblastsFibrosisProcollagen peptidasemedicine.anatomical_structureCollagen Type IIIHEK293 CellsBiochemistryKeloidAstacinThe Journal of investigative dermatology
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