Search results for "binding site"

showing 10 items of 856 documents

GABAA-receptor Subtypes: Clinical Efficacy and Selectivity of Benzodiazepine Site Ligands

1997

The main inhibitory neurotransmitter receptor of the brain, the gamma-aminobutyric acid type A receptor (GABA[A]), mediates the actions of several classes of clinically important drugs, such as benzodiazepines, barbiturates and general anaesthetics. This review summarizes the current knowledge on how classical benzodiazepines and novel nonbenzodiazepine compounds act on the benzodiazepine site of GABA(A) receptors and on their clinical pharmacology related to anxiolytic, sedative, hypnotic and cognitive effects or side-effects. Partial agonism, receptor subtype selectivity and novel binding sites are discussed as possible strategies to develop new drugs with fewer adverse effects than are s…

ZolpidemPyridinesmedicine.drug_classNonbenzodiazepinePharmacologyLigandsAnxiolyticHypnoticBenzodiazepines03 medical and health sciences0302 clinical medicineReceptors GABAmedicineHumansHypnotics and Sedatives030304 developmental biologyNeurotransmitter Agents0303 health sciencesBenzodiazepineBinding SitesGABAA receptorbusiness.industryGeneral Medicine3. Good healthZolpidemMechanism of actionSedativemedicine.symptombusiness030217 neurology & neurosurgerymedicine.drugAnnals of Medicine
researchProduct

Flavour retention and release from protein solutions

2006

International audience; This paper briefly presents the main results obtained up to now on protein–flavour binding and release in relation with flavour perception. Among the food proteins, β-lactoglobulin is the most extensively studied for its binding properties, which involve both hydrophobic and hydrogen binding. Recent developments using molecular modelling and Quantitative Structure–Activity Relationship confirmed the existence of two different binding sites for flavour compounds on β-lactoglobulin. During the aroma release process in the mouth, not only free aroma compounds are released but also those reversibly bound by the protein, pointing out the fact that flavour perception is on…

[SDV.BIO]Life Sciences [q-bio]/BiotechnologyPROTEINSFlavourBioengineeringLactoglobulins01 natural sciencesApplied Microbiology and Biotechnology0404 agricultural biotechnologyComputational chemistryCyclohexenesHumansBinding siteAromaStrong bindingFlavorBinding SitesbiologyFLAVOUR RELEASETerpenesChemistry010401 analytical chemistryBinding propertiesfood and beveragesSerum Albumin Bovine04 agricultural and veterinary sciencesHydrogen-Ion ConcentrationMilk Proteinsbiology.organism_classification040401 food science0104 chemical sciences[SDV.BIO] Life Sciences [q-bio]/BiotechnologyFlavoring AgentsBiochemistryBenzaldehydesTasteFLAVOUR BINDINGSoybean ProteinsFood TechnologyLimoneneProtein BindingBiotechnology
researchProduct

Biochemical and structural features of a novel cyclodextrinase from cow rumen metagenome.

2007

A novel enzyme, RA.04, belonging to the alpha-amylase family was obtained after expression of metagenomic DNA from rumen fluid (Ferrer et al.: Environ. Microbiol. 2005, 7, 1996-2010). The purified RA.04 has a tetrameric structure (280 kDa) and exhibited maximum activity (5000 U/mg protein) at 70 degrees C and was active within an unusually broad pH range from 5.5 to 9.0. It maintained 80% activity at pH 5.0 and 9.5 and 75 degrees C. The enzyme hydrolyzed alpha-D-(1,4) bonds 13-fold faster than alpha-D-(1,6) bonds to yield maltose and glucose as the main products, and it exhibited transglycosylation activity. Its preferred substrates, in the descending order, were maltooligosaccharides (C3-C…

alpha-CyclodextrinsRumenGlycoside HydrolasesStarchAmylopectinOligosaccharidesApplied Microbiology and BiotechnologyCatalysisSubstrate Specificitychemistry.chemical_compoundBacterial ProteinsAmyloseCyclomaltodextrinaseAnimalsMaltoseGlucansChromatography High Pressure Liquidchemistry.chemical_classificationBinding Sitesbiologybeta-CyclodextrinsTemperatureActive sitePullulanStarchGeneral MedicineMaltoseHydrogen-Ion ConcentrationEnzymechemistryBiochemistryAmylopectinbiology.proteinMolecular MedicineCattleElectrophoresis Polyacrylamide GelAmylosegamma-CyclodextrinsBiotechnology journal
researchProduct

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
researchProduct

Procollagen C-proteinase Enhancer Stimulates Procollagen Processing by Binding to the C-propeptide Region Only*

2011

Background: Procollagen C-proteinase enhancer-1 (PCPE-1) is an extracellular glycoprotein that increases activity of certain zinc metalloproteinases involved in tissue development and repair. Results: PCPE-1 binds uniquely to the C-propeptide region of the procollagen molecule. Conclusion: PCPE-1 enhances proteolysis by binding solely to the procollagen C-propeptides. Significance: These data may lead to future applications in the development of antifibrotic therapies.

animal structuresGlycosylationBiologyBiochemistryBone morphogenetic protein 1Protein Structure SecondaryBone Morphogenetic Protein 103 medical and health scienceschemistry.chemical_compoundMetalloprotease0302 clinical medicineHumansBinding siteEnhancerMolecular Biology030304 developmental biologyCell Line TransformedGlycoproteinschemistry.chemical_classification0303 health sciencesMetalloproteinaseExtracellular Matrix ProteinsBinding Sitesintegumentary systemCell BiologyEnzymatic ProcessingFibrosisExtracellular MatrixProcollagen peptidaseCollagen Type IIIchemistryBiochemistry030220 oncology & carcinogenesisembryonic structuresEnzymologyCollagenGlycoproteinProtein Processing Post-TranslationalTriple helixThe Journal of Biological Chemistry
researchProduct

Context-dependent Pax-5 repression of a PU.1/NF-κB regulated reporter gene in B lineage cells

2001

Enhancers located in the 3' end of the locus in part regulate immunoglobulin heavy chain (IgH) gene expression. One of these enhancers, HS 1,2, is developmentally regulated by DNA binding proteins like NF-kappaB, Pax-5 and the protein complex NF-alphaP in B lineage cells. Here we report that NF-alphaP is the ets protein PU.1. A glutathione-S-transferase (GST)-pulldown assay demonstrated that PU.1 can physically interact with NF-kappaB in solution. Experiments in COS cells showed that PU.1 and NF-kappaB (p50/c-Rel) can activate transcription of an enhancer linked reporter gene. The paired domain protein Pax-5 has previously been shown to repress enhancer-dependent transcription. Additional c…

animal structuresLymphomaTranscription GeneticEnhancer RNAsBiologyDNA-binding proteinMiceSOX4Genes ReporterTranscription (biology)CricetinaeProto-Oncogene ProteinsGene expressionGeneticsAnimalsCell LineageBinding siteEnhancerCells CulturedB-LymphocytesReporter geneNF-kappa BPAX5 Transcription FactorNuclear ProteinsGeneral MedicineMolecular biologyGlobinsDNA-Binding ProteinsEnhancer Elements GeneticGene Expression RegulationCOS Cellsembryonic structuresTrans-ActivatorsTranscription FactorsGene
researchProduct

The Sea Urchin sns Insulator Blocks CMV Enhancer following Integration in Human Cells

2001

Insulators are a new class of genetic elements that attenuate enhancer function directionally. Previously, we characterized in sea urchin a 265-bp-long insulator, termed sns. To test insulator activity following stable integration in human cells, we placed sns between the CMV enhancer and a tk promoter up-stream of a GFP transgene of plasmid or retroviral vectors. In contrast to controls, cells transfected or transduced with insulated constructs displayed a barely detectable fluorescence. Southern blot and PCR ruled out vector rearrangement following integration into host DNA; RNase protection confirmed the enhancer blocking activity. Finally, we demonstrate that two cis-acting sequences, p…

animal structuresSea UrchinVirus IntegrationTransgeneMolecular Sequence DataBiophysicsCytomegalovirusSettore BIO/11 - Biologia MolecolareSimian virus 40BiologyTransfectionPolymerase Chain ReactionBiochemistrySodium ChannelsNAV1.8 Voltage-Gated Sodium ChannelPlasmidTumor Cells CulturedAnimalsHumansEnhancer trapDNA Polymerase Chain ReactionEnhancerBinding Sites; DNA Polymerase Chain Reaction; Recombinant Proteins; Sea Urchins;Tumor Cells Cultured; Enhancer Elements Genetic; Virus Integration;Molecular BiologyVirus IntegrationSouthern blotBinding SitesBase SequenceBinding SiteCell BiologyTransfectionRecombinant ProteinMolecular biologyRecombinant ProteinsChromatinSettore BIO/18 - GeneticaEnhancer Elements GeneticSea UrchinsDNA ViralBiochemical and Biophysical Research Communications
researchProduct

Polycationic Monomeric and Homodimeric Asymmetric Monomethine Cyanine Dyes with Hydroxypropyl Functionality—Strong Affinity Nucleic Acids Binders

2021

New analogs of the commercial asymmetric monomethine cyanine dyes thiazole orange (TO) and thiazole orange homodimer (TOTO) with hydroxypropyl functionality were synthesized and their properties in the presence of different nucleic acids were studied. The novel compounds showed strong, micromolar and submicromolar affinities to all examined DNA ds-polynucleotides and poly rA–poly rU. The compounds studied showed selectivity towards GC-DNA base pairs over AT-DNA, which included both binding affinity and a strong fluorescence response. CD titrations showed aggregation along the polynucleotide with well-defined supramolecular chirality. The single dipyridinium-bridged dimer showed intercalatio…

antiproliferative activityCircular dichroismSupramolecular chiralityDimerIntercalation (chemistry)cyanine dye010402 general chemistry01 natural sciencesBiochemistryMicrobiologyArticlechemistry.chemical_compoundCell Line TumorHumansCyanineDNA bindingColoring AgentsBiologyMolecular BiologyBinding Sites010405 organic chemistrycyanine dye ; DNA binding ; RNA binding ; fluorescence ; circular dichroism ; antiproliferative activityDNARNA bindingCombinatorial chemistryQR1-502Intercalating Agents3. Good health0104 chemical sciencescircular dichroismchemistryPolynucleotideNucleic acidcyanine dye; DNA binding; RNA binding; fluorescence; circular dichroism; antiproliferative activityfluorescenceDNA
researchProduct

Novel Insights into the Cellular Localization and Regulation of the Autophagosomal Proteins LC3A, LC3B and LC3C

2020

Macroautophagy is a conserved degradative process for maintaining cellular homeostasis and plays a key role in aging and various human disorders. The microtubule-associated protein 1A/1B light chain 3B (MAP1LC3B or LC3B) is commonly analyzed as a key marker for autophagosomes and as a proxy for autophagic flux. Three paralogues of the LC3 gene exist in humans: LC3A, LC3B and LC3C. The molecular function, regulation and cellular localization of LC3A and LC3C have not been investigated frequently, even if a similar function to that described for LC3B appears likely. Here, we have selectively decapacitated LC3B by three separate strategies in primary human fibroblasts and analyzed the evoked e…

autophagysequestosome 1 (p62)LC3CATG8GABARAPGABARAPCellular homeostasisProtein lipidationsirtuin 1ArticleCell LineAntibody SpecificityHumansSirtuinsAmino Acid SequenceLC3BRNA Small InterferingLC3Alcsh:QH301-705.5PhylogenyCellular localizationCell NucleusBinding SitesbiologyChemistrySirtuin 1AutophagosomesAutophagy-Related Protein 8 FamilyGeneral MedicineFibroblastsLipidsCell biologyProtein Transportlcsh:Biology (General)Gene Knockdown TechniquesSirtuinbiology.proteinApoptosis Regulatory ProteinsMicrotubule-Associated ProteinsATG8MAP1LC3BSubcellular FractionsCells
researchProduct

Pneumococcal HxxHxH triad – Copper(II) interactions – How important is the ‘x’?

2019

Abstract PhtA, a Streptococcus pneumoniae polyhistidine triad protein, which contributes to virulence by interacting with components of the immune system, by being involved in adherence of bacteria and in Zn(II) uptake, contains five copies of the HxxHxH sequence. Since this motif is also present in numerous Cu(II) binding proteins, we decided to focus on the bioinorganic chemistry of copper(II) with three of such PhtA repeats, in order to understand which of the PhtA triads binds Cu(II) with the highest affinity and explain if Cu(II) would be able to outcompete Zn(II) from its native binding site under physiological metal concentrations.

biology010405 organic chemistryChemistryStereochemistryVirulencechemistry.chemical_elementBioinorganic chemistry010402 general chemistrymedicine.disease_causebiology.organism_classification01 natural sciencesDNA-binding proteinCopper0104 chemical sciencesInorganic ChemistryMetalvisual_artStreptococcus pneumoniaeMaterials Chemistrymedicinevisual_art.visual_art_mediumPhysical and Theoretical ChemistryBinding siteBacteriaInorganica Chimica Acta
researchProduct