Search results for "substitut"

showing 10 items of 1337 documents

Synthesis of Tetrasubstituted 4,4'-Biimidazoles

2012

Highly substituted 4,4'-biimidazoles were synthesized, in good to excellent yields, through a multicomponent imidazole ring synthesis by using imidazol-4-yl-ethane-1,2-diones as starting materials. The obtained compounds were preliminarily tested as chromogenic and fluorescent sensors for heavy metals.

Molecular StructureChemistryChromogenicOrganic ChemistryImidazolesHeavy metalsSettore CHIM/06 - Chimica Organica44'-Biimidazoles heavy metals sensors Boulton Katritzky Rearrangement imidazolyl-dione pentaphenyl-substituted 44'-2'4''-terimidazoleRing (chemistry)BiochemistryFluorescenceCombinatorial chemistrychemistry.chemical_compoundOrganic chemistryImidazolePhysical and Theoretical Chemistry
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Study of aromatic nucleophilic substitution with amines on nitrothiophenes in room-temperature ionic liquids: are the different effects on the behavi…

2006

The kinetics of the nucleophilic aromatic substitution of some 2-L-5-nitrothiophenes (para-like isomers) with three different amines (pyrrolidine, piperidine, and morpholine) were studied in three room-temperature ionic liquids ([bmim][BF4], [bmim][PF6], and [bm(2)im][BF4], where bmim = 1-butyl-3-methylimidazolium and bm(2)im = 1-butyl-2,3-dimethylimidazolium). To calculate thermodynamic parameters, a useful instrument to gain information concerning reagent-solvent interactions, the reaction was carried out over the temperature range 293-313 K. The reaction occurs faster in ionic liquids than in conventional solvents (methanol, benzene), a dependence of rate constants on amine concentration…

Molecular StructureChemistryOrganic ChemistryInorganic chemistrySolvationImidazolesTemperatureIonic LiquidsStereoisomerismThiophenesMedicinal chemistryPyrrolidinechemistry.chemical_compoundKineticsReaction rate constantSolubilityNucleophilic aromatic substitutionMorpholineIonic liquidBoratesNucleophilic substitutionSolventsSolvent effectsAminesThe Journal of organic chemistry
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Calculation of binding energy using BLYP/MM for the HIV-1 integrase complexed with the S-1360 and two analogues.

2007

Abstract Integrase (IN) is one of the three human immunodeficiency virus type 1 (HIV-1) enzymes essential for effective viral replication. S-1360 is a potent and selective inhibitor of HIV-1 IN. In this work, we have carried out molecular dynamics (MD) simulations using a hybrid Quantum Mechanics/Molecular Mechanics (QM/MM) approach, to determine the protein–ligand interaction energy for S-1360 and two analogues. Analysis of the MD trajectories reveals that the strongest protein–inhibitor interactions, observed in the three studied complexes, are established with Lys-159 residue and Mg 2+ cation. Calculations of binding energy using BLYP/MM level of theory reveal that there is a direct rela…

Molecular modelStereochemistryProtein ConformationClinical BiochemistryBinding energyPharmaceutical ScienceHIV IntegraseCrystallography X-RayBiochemistryMolecular mechanicsMolecular dynamicsPropaneStructure-Activity RelationshipDrug DiscoveryHumansMagnesiumPyrrolesAmino Acid SequenceHIV Integrase InhibitorsFuransMolecular Biologychemistry.chemical_classificationbiologyChemistryLysineOrganic ChemistryActive siteInteraction energyTriazolesIntegraseEnzymeAmino Acid SubstitutionModels Chemicalbiology.proteinMolecular MedicineBioorganicmedicinal chemistry
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Blood Anticoagulant Activity of Sulphated Ovular Mucins of Amphibians

1957

THE mucin constituting the gelatinous layer which envelops the eggs of Bufo bufo, if digested with papain and then sulphated, shows a marked anticoagulant activity on the fibrinogen and the whole blood plasma1. A similar anticoagulant activity has now been shown by the ovular mucins of other species of amphibians, sulphated without any previous proteolysis.

Multidisciplinarybiologymedicine.diagnostic_testSulfatesurogenital systemChemistryProteolysisMucinMucinsAnticoagulantsFibrinogenbiology.organism_classificationAnticoagulant activityAmphibiansPapainchemistry.chemical_compoundBiochemistrymedicineAnimalsHumanssense organsBufohormones hormone substitutes and hormone antagonistsmedicine.drugWhole bloodNature
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Small molecule inhibitors of Apaf-1-related caspase- 3/-9 activation that control mitochondrial-dependent apoptosis

2006

10 pages, 5 figures.-- PMID: 16341125 [PubMed].-- Available online Dec 9, 2005.

Multiprotein complexCytochromeProtein-protein interactionsApoptosisCaspase 3MitochondrionLigandsCell LineChemical librarychemistry.chemical_compoundPeptide LibraryApoptosomesPeptoidHumansCombinatorial libraries inhibitorApoptosomeProtein PrecursorsMolecular BiologybiologyCaspase 3Intrinsic apoptosisCytochromes cCell BiologyCaspase InhibitorsCaspase 9Recombinant ProteinsMitochondriaCell biologyEnzyme ActivationCaspasa-9Apoptotic Protease-Activating Factor 1chemistryBiochemistryN-substituted GlycinesApoptosisCaspasa-3biology.proteinApoptosomeApaf-1Molecular recognitionSmall moleculeProtein BindingCell Death & Differentiation
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Changes in protein domains outside the catalytic site of the bacteriophage Qβ replicase reduce the mutagenic effect of 5-azacytidine.

2014

ABSTRACT The high genetic heterogeneity and great adaptability of RNA viruses are ultimately caused by the low replication fidelity of their polymerases. However, single amino acid substitutions that modify replication fidelity can evolve in response to mutagenic treatments with nucleoside analogues. Here, we investigated how two independent mutants of the bacteriophage Qβ replicase (Thr210Ala and Tyr410His) reduce sensitivity to the nucleoside analogue 5-azacytidine (AZC). Despite being located outside the catalytic site, both mutants reduced the mutation frequency in the presence of the drug. However, they did not modify the type of AZC-induced substitutions, which was mediated mainly by …

Mutation rateImmunologyMutantRNA-dependent RNA polymeraseBiologyVirus ReplicationMicrobiologyViral ProteinsVirologyCatalytic DomainmedicineGeneticsAllolevivirusNucleoside analogueQ beta Replicasebiology.organism_classification3. Good healthProtein Structure TertiaryViral replicationBiochemistryAmino Acid SubstitutionGenetic Diversity and EvolutionInsect ScienceAzacitidineQ beta ReplicaseBacteriophage QβNucleosidemedicine.drugMutagensJournal of virology
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Distribution of Fitness Effects Caused by Single-Nucleotide Substitutions in Bacteriophage f1

2010

Empirical knowledge of the fitness effects of mutations is important for understanding many evolutionary processes, yet this knowledge is often hampered by several sources of measurement error and bias. Most of these problems can be solved using site-directed mutagenesis to engineer single mutations, an approach particularly suited for viruses due to their small genomes. Here, we used this technique to measure the fitness effect of 100 single-nucleotide substitutions in the bacteriophage f1, a filamentous single-strand DNA virus. We found that approximately one-fifth of all mutations are lethal. Viable ones reduced fitness by 11% on average and were accurately described by a log-normal dist…

Mutation rateMutagenesis (molecular biology technique)InvestigationsBiologymedicine.disease_causeGenomeBacteriophagechemistry.chemical_compoundGeneticsmedicineAnimalsHumansBacteriophagesGeneticsMutationNucleotidesRNADNA virusbiology.organism_classificationBiological EvolutionAmino Acid SubstitutionchemistryMutationMutagenesis Site-DirectedDNA IntergenicDNAGenetics
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SIRT1 prevents genotoxic stress-induced p53 activation in acute myeloid leukemia

2014

SIRT1 is an important regulator of cellular stress response and genomic integrity. Its role in tumorigenesis is controversial. Whereas sirtuin 1 (SIRT1) can act as a tumor suppressor in some solid tumors, increased expression has been demonstrated in many cancers, including hematologic malignancies. In chronic myeloid leukemia, SIRT1 promoted leukemia development, and targeting SIRT1 sensitized chronic myeloid leukemia progenitors to tyrosine kinase inhibitor treatment. In this study, we investigated the role of SIRT1 in acute myeloid leukemia (AML). We show that SIRT1 protein, but not RNA levels, is overexpressed in AML samples harboring activating mutations in signaling pathways. In FMS-l…

Myeloidendocrine system diseasesmedicine.drug_classImmunologyBiologymedicine.disease_causeBiochemistryTyrosine-kinase inhibitorMiceSirtuin 1hemic and lymphatic diseasesmedicineAnimalsHumansGene Knock-In TechniquesKinase activityfood and beveragesMyeloid leukemiaCell BiologyHematologymedicine.diseaseEnzyme ActivationMice Inbred C57BLLeukemia Myeloid Acuteenzymes and coenzymes (carbohydrates)Leukemiamedicine.anatomical_structureGene Knockdown TechniquesCancer researchHeterograftsTumor Suppressor Protein p53Signal transductionCarcinogenesisTyrosine kinasehormones hormone substitutes and hormone antagonistsDNA DamageSignal TransductionBlood
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Ethanol cycle in an ethanologenic bacterium

2002

AbstractA novel redox cycle is suggested, performing interconversion between acetaldehyde and ethanol in aerobically growing ethanologenic bacterium Zymomonas mobilis. It is formed by the two alcohol dehydrogenase (ADH) isoenzymes simultaneously catalyzing opposite reactions. ADH I is catalyzing acetaldehyde reduction. The local reactant ratio at its active site probably is shifted towards ethanol synthesis due to direct channeling of NADH from glycolysis. ADH II is oxidizing ethanol. The net result of the cycle operation is NADH shuttling from glycolysis to the membrane respiratory chain, and ensuring flexible distribution of reducing equivalents between the ADH reaction and respiration.

NADH channelingBiophysicsRespiratory chainBiochemistryZymomonas mobilischemistry.chemical_compoundStructural BiologyGeneticsGlycolysisEthanol metabolismMolecular BiologyAlcohol dehydrogenaseZymomonasEthanolEthanolbiologyFutile cycleRespirationZymomonas mobilisAlcohol dehydrogenaseAcetaldehydeCell BiologyNADbiology.organism_classificationAerobiosisIsoenzymeschemistryBiochemistryFutile cycleChemostatbiology.proteinOxidation-Reductionhormones hormone substitutes and hormone antagonistsFEBS Letters
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2-(2,6-Dihalophenyl)-3-(pyrimidin-2-yl)-1,3-thiazolidin-4-ones as non-nucleoside HIV-1 reverse transcriptase inhibitors.

2004

Several 1,3-thiazolidin-4-ones bearing a 2,6-dihalophenyl group at C-2 and a substituted pyrimidin-2-yl ring at the N-3 were synthesised and evaluated as anti-HIV agents. The results of the in vitro tests showed that some of them were highly effective inhibitors of human immunodeficiency virus type-1 (HIV-1) replication at 10–40 nM concentrations with minimal cytotoxicity. Structure–activity relationship studies revealed that the nature of the substituents at the 2 and 3 positions of the thiazolidinone nucleus had a significant impact on the in vitro anti-HIV activity of this class of potent antiretroviral agents. The compounds had significantly reduced activity against the characteristic N…

NNRTI3-Thiazolidin-4-onesAnti-HIV activity13-Thiazolidin-4-oneNNRTIs; 1; 3-Thiazolidin-4-ones; anti-HIVAnti-HIV Agents1Drug Evaluation PreclinicalMutation MissenseBiologyVirus ReplicationVirusStructure-Activity RelationshipVirologyDrug Resistance ViralmedicineStructure–activity relationshipCytotoxicityPharmacologyReverse-transcriptase inhibitorMolecular Structurevirus diseasesanti-HIVSettore CHIM/08 - Chimica FarmaceuticaMolecular biologyIn vitroReverse transcriptaseThiazolesPyrimidinesViral replicationAmino Acid SubstitutionNNRTIsHIV-1Reverse Transcriptase InhibitorsNucleosidemedicine.drugAntiviral research
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