Search results for "structure-activity"

showing 10 items of 746 documents

Sildenafil protects epithelial cell through the inhibition of xanthine oxidase and the impairment of ROS production

2009

Recent reports suggest that xanthine oxidase (XO), a modified form of the native xanthine dehydrogenase enzyme, plays an important role in various forms of ischemic and vascular injuries, inflammatory diseases, and chronic heart failure. The XO inhibitors allopurinol and its oxidation product oxypurinol held considerable promises in the treatment of these conditions both in experimental animals and in human clinical trials. More recently, an endothelium-based protective effect of sildenafil, a well-known type-5 phosphodiesterase inhibitor, has been reported in preconditioning prior to ischemia/reperfusion in healthy human subjects. Based on the structural similarities between allopurinol an…

Xanthine OxidasePurinonesEndotheliumCell SurvivalSildenafilIschemiaAllopurinolPharmacologyBiochemistryPiperazinesSildenafil CitrateStructure-Activity Relationshipchemistry.chemical_compoundSettore BIO/10 - BiochimicaTumor Cells CulturedmedicineHumansSulfonesXanthine oxidaseNADPH oxidasebiologybusiness.industryEpithelial CellsGeneral Medicinemedicine.diseasemedicine.anatomical_structurechemistryBiochemistryPurinesCell cultureSettore BIO/14 - Farmacologiabiology.proteinReactive Oxygen SpeciesZaprinastbusinessXanthine oxidase ROS production oxidative stress inhibition sildenafil zaprinast human mammary epithelial cellsmedicine.drugFree Radical Research
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Structure-function analysis of peroxisomal ATP-binding cassette transporters using chimeric dimers

2014

Background: Peroxisomal ABC transporters are predicted to function as homodimers in mammals. [br/] Results: ABCD1 interacts with ABCD2. Chimeric proteins mimicking full-length dimers represent novel tools for functional study. Artificial homodimers and heterodimers are functional. [br/] Conclusion: Interchangeability between ABCD1 and ABCD2 is confirmed, but PUFA transport depends on ABCD2. [br/] Significance: For the first time, heterodimers in mammals are proven to be functional.[br/] ABCD1 and ABCD2 are two closely related ATP-binding cassette half-transporters predicted to homodimerize and form peroxisomal importers for fatty acyl-CoAs. Available evidence has shown that ABCD1 and ABCD2 …

[SDV.BA] Life Sciences [q-bio]/Animal biologyprotéine chimereanimal diseasesATP-binding cassette transporterProximity ligation assayProtein Chimerabiochimie structurale[ SDV.BA ] Life Sciences [q-bio]/Animal biologyPolymerase Chain ReactionBiochemistryGreen fluorescent proteininteraction moléculaireMice[ CHIM.OTHE ] Chemical Sciences/Otherhomodimèrereproductive and urinary physiologyAnimal biologyhétérodimèrechemistry.chemical_classification[SDV.BA]Life Sciences [q-bio]/Animal biologymammifèreTransfectionPeroxisomeprotéine de fusionBiochemistry[CHIM.OTHE] Chemical Sciences/OtherDimerizationPlasmidsABC Transporter;Fatty Acid;Peroxisome;Protein Chimera;Protein-Protein Interactiontransporteur abcBiologyPeroxisomeCell LineProtein–protein interactionStructure-Activity RelationshipMembrane BiologyBiologie animaleparasitic diseasesAutre (Chimie)PeroxisomesAnimalsHumansMolecular BiologyDNA PrimersBase SequenceABCD2fungiABCD1Fatty acidCell BiologyFusion proteinRatsProtein-Protein InteractionABC TransporterchemistryATP-Binding Cassette TransportersOther[CHIM.OTHE]Chemical Sciences/OtherFatty Acid
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Rbt1 Protein Domains Analysis in Candida albicans Brings Insights into Hyphal Surface Modifications and Rbt1 Potential Role during Adhesion and Biofi…

2013

Cell wall proteins are central to the virulence of Candida albicans. Hwp1, Hwp2 and Rbt1 form a family of hypha-associated cell surface proteins. Hwp1 and Hwp2 have been involved in adhesion and other virulence traits but Rbt1 is still poorly characterized. To assess the role of Rbt1 in the interaction of C. albicans with biotic and abiotic surfaces independently of its morphological state, heterologous expression and promoter swap strategies were applied. The N-terminal domain with features typical of the Flo11 superfamily was found to be essential for adhesiveness to polystyrene through an increase in cell surface hydrophobicity. A 42 amino acid-long domain localized in the central part o…

[SDV]Life Sciences [q-bio]lcsh:MedicinebiofilmCell membraneadhésionCandida albicanslcsh:ScienceCandida albicansRecombination Genetic0303 health sciencesFungal proteinMultidisciplinaryCandida albicans;cell wall;protein;Rbt1;adhesion;biofilmbiologyFlow Cytometry3. Good healthCell biologyTransport proteinProtein Transportadhesionmedicine.anatomical_structureprotéineparoi cellulaireHydrophobic and Hydrophilic InteractionsResearch ArticleProtein domainSaccharomyces cerevisiaeHyphaeSaccharomyces cerevisiaeFungal ProteinsStructure-Activity Relationship03 medical and health sciencesCell AdhesionmedicineHumansAmino Acid SequenceCell adhesion030304 developmental biologySequence Homology Amino Acid030306 microbiologyCell Membranelcsh:Rfungibiology.organism_classificationRbt1Protein Structure TertiaryMembrane proteinBiofilmsPolystyrenescell walllcsh:Qprotein
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Study of relationships between the structure of aroma compounds and their retention-release between vapour phase and dairy gels

2010

An integrated approach physicochemistry and structures activity relationships has been carried out to study the aroma compounds retention-release phenomenon in a fat free dairy gel added with pectin. This study aimed to identify the molecular properties that govern this phenomenon assuming that modifying the structure leads automatically to a change in the retention-release of aroma compounds. For this purpose, we have determined the partition coefficients of 28 aroma compounds in water, in pectin gels and in dairy gels supplemented or not supplemented with pectin, at equilibrium conditions using the PRV method (Phase Ratio Variation). Then, we have performed a structure-retention relations…

[SPI.GPROC] Engineering Sciences [physics]/Chemical and Process Engineering[ SDV.AEN ] Life Sciences [q-bio]/Food and NutritionQsar/qsprCOMPOSE D'ARÔMEAroma compoundComposé d’arôme[SDV.IDA] Life Sciences [q-bio]/Food engineeringCoefficient de partagePartition coefficientPectinHeadspaceRetention-releasePrvStructure-activity/structure-property relationshipsRétention-libérationRETENTION-LIBERATION[SDV.IDA]Life Sciences [q-bio]/Food engineeringPectine[SPI.GPROC]Engineering Sciences [physics]/Chemical and Process EngineeringDairy gelRELATIONS STRUCTURE-ACTIVITE/STRUCTURE-PROPRIETEGel laitierRelations structure-activité/structure-propriété[SDV.AEN]Life Sciences [q-bio]/Food and Nutrition
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α-Aminoalkylphosphonates as a tool in experimental optimisation of P1 side chain shape of potential inhibitors in S1 pocket of leucine- and neutral a…

2005

Abstract The synthesis and biological activity studies of the series of structurally different α-aminoalkylphosphonates were performed in order to optimise the shape of the side chain of the potential inhibitors in S1 pocket of leucine aminopeptidase [E.C.3.4.11.1]. Analysis of a series of compounds with aromatic, aliphatic and alicyclic P1 side chains enabled to find out the structural features, optimal for that fragment of inhibitors of LAP. The most active among all investigated compounds were the phosphonic analogues of homo-tyrosine ( K i  = 120 nM) and homo-phenylalanine ( K i  = 140 nM), which even as racemic mixtures were better inhibitors in comparison with the best till now-phosph…

aminophosphonatesStereochemistryleucine aminopeptidaseOrganophosphonatesKidneyAminopeptidasesChemical synthesisAminopeptidaseLeucyl AminopeptidaseStructure-Activity RelationshipAlicyclic compoundLeucineDrug DiscoverySide chainAnimalsLeucyl aminopeptidasePharmacologychemistry.chemical_classificationBinding SitesMolecular StructureAminopeptidase NOrganic ChemistryBiological activityGeneral MedicineHydrogen-Ion Concentrationaminopeptidase NinhibitorEnzymechemistryLeucineEuropean Journal of Medicinal Chemistry
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Regulation of the alpha-secretase ADAM10 by its prodomain and proprotein convertases.

2001

SPECIFIC AIMSTo identify the proprotein convertases responsible for maturation of the α-secretase ADAM10, we investigated the influence of PC7 and furin on ADAM10 processing and the resulting effect on amyloid precursor protein cleavage. We also examined the functional role of the ADAM10 prodomain by coexpression of a prodomain-deleted ADAM10 mutant together with its prodomain in trans.PRINCIPAL FINDINGS1. ADAM10 is proteolytically processed by PC7 and furinThe disintegrin metalloproteinase ADAM10 possesses α-secretase activity as well as a potential proprotein convertase recognition sequence (RKKR) after its prodomain. By amino-terminal sequencing of ADAM10 purified from bovine kidney plas…

animal structuresADAM10Blotting WesternKidneyTransfectionBiochemistryCell LineAmyloid beta-Protein PrecursorStructure-Activity RelationshipZymogenEndopeptidasesGeneticsAmyloid precursor proteinAnimalsAspartic Acid EndopeptidasesHumansSubtilisinsProtein PrecursorsMolecular BiologyFurinFurinbiologyChemistryProprotein convertaseEmbryo MammalianRecombinant ProteinsEnzyme ActivationBiochemistryAlpha secretaseMutagenesisbiology.proteinCattleAmyloid Precursor Protein SecretasesProprotein ConvertasesAmyloid precursor protein secretaseBiotechnologyFASEB journal : official publication of the Federation of American Societies for Experimental Biology
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Hsp60, a Novel Target for Antitumor Therapy: Structure-Function Features and Prospective Drugs Design

2013

Heat shock protein 60 kDa (Hsp60) is a chaperone classically believed to be involved in assisting the correct folding of other mitochondrial proteins. Hsp60 also plays a role in cytoprotection against cell stressors, displaying for example, antiapoptotic potential. Despite the plethora of studies devoted to the mechanism of Hsp60's function, especially in prokaryotes, fundamental issues still remain unexplored, including the definition of its role in cancer. Key questions still unanswered pertain to the differences in structure-function features that might exist between the well-studied prokaryotic GroEL and the largely unexplored eukaryotic Hsp60 proteins. In this article we discuss these …

animal structuresBinding pocketCellAntineoplastic Agentschemical and pharmacologic phenomenaComputational biologyBiologyBioinformaticsFunctional domaincomplex mixturesChaperoninStructure-Activity RelationshipNeoplasmsHeat shock proteinDrug DiscoverymedicineHumansPharmacologyCompound dockingSettore BIO/16 - Anatomia UmanaCell growthfungiSettore CHIM/06 - Chimica OrganicaChaperonin 60Hsp60Settore CHIM/08 - Chimica FarmaceuticaCytoprotectionGroELmedicine.anatomical_structureSettore CHIM/03 - Chimica Generale E InorganicaCancer treatmentDrug DesignChaperone (protein)biology.proteinHSP60Protein foldingEpolactaeneCurrent Pharmaceutical Design
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New 1,2,4-oxadiazole nortopsentin derivatives with cytotoxic activity

2019

New analogs of nortopsentin, a natural 2,4-bis(3&prime

anti-cancer agentCell SurvivalAnti-cancer agentsPharmaceutical ScienceAntineoplastic AgentsAntiproliferative activity01 natural sciencesArticlechemistry.chemical_compoundStructure-Activity RelationshipMarine alkaloidsSettore BIO/10 - BiochimicaDrug DiscoveryMoietyHumansPharmacology Toxicology and Pharmaceutics (miscellaneous)lcsh:QH301-705.5Cell ProliferationIndole testMolecular Structure010405 organic chemistryAcridine orangeImidazoles2 4-oxadiazole derivativesnortopsentin analogs2 4-oxadiazole derivatives; Anti-cancer agents; Antiproliferative activity; Marine alkaloids; Nortopsentin analogs 1; Antineoplastic Agents; Caco-2 Cells; Cell Cycle Checkpoints; Cell Proliferation; Cell Survival; HCT116 Cells; Humans; Imidazoles; MCF-7 Cells; Molecular Structure; Structure-Activity RelationshipPhosphatidylserineCell Cycle CheckpointsNortopsentin analogs 1HCT116 CellsSettore CHIM/08 - Chimica Farmaceutica0104 chemical sciences124-oxadiazole derivative010404 medicinal & biomolecular chemistrychemistryBiochemistry124-oxadiazole derivativeslcsh:Biology (General)ApoptosisCell cultureCancer cellMCF-7 CellsMarine alkaloid2 4-oxadiazole derivativeCaco-2 CellsEthidium bromide
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Dipeptides of S-Substituted Dehydrocysteine as Artzyme Building Blocks: Synthesis, Complexing Abilities and Antiproliferative Properties †

2021

Background: Dehydropeptides are analogs of peptides containing at least one conjugate double bond between α,β-carbon atoms. Its presence provides unique structural properties and reaction centre for chemical modification. In this study, the series of new class of dipeptides containing S-substituted dehydrocysteine with variety of heterocyclic moieties was prepared. The compounds were designed as the building blocks for the construction of artificial metalloenzymes (artzymes). Therefore, the complexing properties of representative compounds were also evaluated. Furthermore, the acknowledged biological activity of natural dehydropeptides was the reason to extend the study for antiproliferativ…

antiproliferative activityBALB 3T3 CellsDouble bondPotentiometric titrationSulforhodamine BTriazoleAntineoplastic Agents010402 general chemistry01 natural sciencesCatalysisArticlelcsh:ChemistryInorganic ChemistryMiceStructure-Activity Relationshipchemistry.chemical_compoundElimination reactionCell Line TumorAnimalsHumansChelationCysteinePhysical and Theoretical Chemistrydehydrocysteinelcsh:QH301-705.5Molecular BiologySpectroscopyCell Proliferationchemistry.chemical_classification010405 organic chemistryOrganic ChemistryChemical modificationDipeptidesGeneral MedicineHydrogen-Ion ConcentrationCombinatorial chemistryEnzymes0104 chemical sciencesComputer Science Applicationsdehydropeptideslcsh:Biology (General)lcsh:QD1-999chemistrycomplexing agentaddition-elimination reactionDrug Screening Assays AntitumorCopperConjugateInternational Journal of Molecular Sciences
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Synthesis and antiproliferative activity of the ring system [1,2]oxazolo[4,5-g]indole.

2012

Brand new ring: A series of 27 derivatives of the new ring system [1,2]oxazolo[4,5-g]indole were conveniently prepared and tested at the NCI for antiproliferative studies. Several of them showed good inhibitory activity toward all tested cell lines, reaching GI50 values generally at the micromolar and sub-micromolar levels and in some cases at nanomolar concentrations. The mean GI50 values, calculated on the full panel, were in the range 0.25-7.08 μM.

antiproliferative activityIndolesStereochemistryhydroxylamine hydrochloridesAntineoplastic AgentsRing (chemistry)Biochemistrychemistry.chemical_compoundStructure-Activity RelationshipCell Line TumorNeoplasms2]oxazolo[4Drug Discoveryantiproliferative activity; combretastatin A-4; enaminoketones; hydroxylamine hydrochlorides; [1; 2]oxazolo[4; 5-g]indolesStructure–activity relationshipHumanscombretastatin A-4General Pharmacology Toxicology and PharmaceuticsOxazolesCell ProliferationPharmacologyCombretastatin A-4Indole testantiproliferative activity combretastatin A-4 enaminoketones hydroxylamine hydrochlorides[12]oxazolo[45-g]indolesOrganic ChemistrySettore CHIM/08 - Chimica Farmaceuticachemistry5-g]indolesenaminoketonesMolecular Medicine[1Drug Screening Assays AntitumorChemMedChem
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