Search results for "binding site"

showing 10 items of 856 documents

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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Toxicity and mode of action of Bacillus thuringiensis Cry proteins in the Mediterranean corn borer, Sesamia nonagrioides (Lefebvre)

2006

ABSTRACT Sesamia nonagrioides is one of the most damaging pests of corn in Spain and other Mediterranean countries. Bt corn expressing the Bacillus thuringiensis Cry1Ab toxin is being grown on about 58,000 ha in Spain. Here we studied the mode of action of this Cry protein on S. nonagrioides (binding to specific receptors, stability of binding, and pore formation) and the modes of action of other Cry proteins that were found to be active in this work (Cry1Ac, Cry1Ca, and Cry1Fa). Binding assays were performed with 125 I- or biotin-labeled toxins and larval brush border membrane vesicles (BBMV). Competition experiments indicated that these toxins bind specifically and that Cry1Aa, Cry1Ab, an…

Cell Membrane PermeabilityMembrane permeabilityBacterial ToxinsBacillus thuringiensisSesamia nonagrioidesBacterial ToxinBacterial ProteinZea maysApplied Microbiology and BiotechnologyOstriniaHemolysin ProteinsZea mayBacterial ProteinsEndotoxinBacillus thuringiensisBotanyInvertebrate MicrobiologyAnimalsBacillus thuringiensiBinding siteMode of actionPest Control BiologicalGenetically modified maizeBacillus thuringiensis ToxinsEcologybiologyMicrovilliAnimalfungifood and beveragesHemolysin Proteinbiology.organism_classificationPlants Genetically ModifiedEndotoxinsLepidopteraCry1AcBiochemistryLarvaFood ScienceBiotechnology
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Kinetic modelling of passive transport and active efflux of a fluoroquinolone across Caco-2 cells using a compartmental approach in NONMEM.

2005

The purpose was to develop a general mathematical model for estimating passive permeability and efflux transport parameters from in vitro cell culture experiments. The procedure is applicable for linear and non-linear transport of drug with time,10 or10% of drug transport, negligible or relevant back flow, and would allow the adequate correction in the case of relevant mass balance problems. A compartmental kinetic approach was used and the transport barriers were described quantitatively in terms of apical and basolateral clearances. The method can be applied when sink conditions are not achieved and it allows the evaluation of the location of the transporter and its binding site. In this …

Cell Membrane PermeabilityTime FactorsPassive transportHealth Toxicology and MutagenesisXenobiotic transportToxicologyKinetic energyBiochemistrySubstrate SpecificityHumansP-glycoproteinPharmacologyBinding SitesbiologyDose-Response Relationship DrugChemistryMembrane Transport ProteinsBiological TransportGeneral MedicineApical membraneModels TheoreticalNONMEMKineticsBiochemistryVerapamilbiology.proteinEffluxCaco-2 CellsBiological systemIn vitro cell cultureFluoroquinolonesXenobiotica; the fate of foreign compounds in biological systems
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Tightly bound to DNA proteins: possible universal substrates for intranuclear processes.

2011

Tightly bound to DNA proteins (TBPs) are a protein group that remains attached to DNA after its deproteinization by phenol, chloroform or salting-out. TBP are bound to DNA with covalent phosphotriester or non-covalent ion and hydrogen bonds. They appear to be a vast protein group involved in numerous intranuclear processes. The TBPs fraction co-purified with DNA deproteinized by mild procedures is extremely heterogeneous, tissue and species-specific. The protein fraction co-purified with DNA after harsh deproteinization procedures appears to be formed from few polypeptides common to different species and tissues. Interaction sites between DNA and TBPs depend on the physiological status of t…

Cell NucleusTranscription GeneticHydrogen bondPhosphataseCellGeneral MedicineBiologyNuclear matrixModels BiologicalPhosphoric Monoester HydrolasesDNA-Binding Proteinschemistry.chemical_compoundmedicine.anatomical_structurechemistryBiochemistrySpecies SpecificityTranscription (biology)Covalent bondOrgan SpecificityGeneticsmedicineAnimalsBinding siteDNASerpinsGene
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Ensemble-based ADME-Tox profiling and virtual screening for the discovery of new inhibitors of the Leishmania mexicana cysteine protease CPB2.8ΔCTE

2018

Abstract: In an effort to identify novel molecular warheads able to inhibit Leishmania mexicana cysteine protease CPB2.8CTE, fused benzo[b]thiophenes and ,'-triketones emerged as covalent inhibitors binding the active site cysteine residue. Enzymatic screening showed a moderate-to-excellent activity (12%-90% inhibition of the target enzyme at 20m). The most promising compounds were selected for further profiling including in vitro cell-based assays and docking studies. Computational data suggest that benzo[b]thiophenes act immediately as non-covalent inhibitors and then as irreversible covalent inhibitors, whereas a reversible covalent mechanism emerged for the 1,3,3'-triketones with a Y-to…

Cell SurvivalLeishmania mexicanaProtozoan ProteinsADME-Tox; Benzo[b]thiophenes; Cysteine protease; Leishmaniasis; TriketonesThiophenesCysteine Proteinase Inhibitors010402 general chemistry01 natural sciencesBiochemistryLeishmania mexicanaCysteine Proteinase InhibitorsCell LineInhibitory Concentration 50Structure-Activity RelationshipCysteine ProteasesCatalytic DomainDrug DiscoveryHumansStructure–activity relationshipcysteine proteaseBinding siteADME-Tox; benzo[b]thiophenes; cysteine protease; leishmaniasis; triketones; Biochemistry; Molecular MedicineBiologyleishmaniasisPharmacologychemistry.chemical_classificationVirtual screeningBinding Sitesbiology010405 organic chemistryPharmacology. TherapyOrganic Chemistrytriketonesbiology.organism_classificationCysteine protease0104 chemical sciencesMolecular Docking SimulationChemistryEnzymeBiochemistrychemistryDocking (molecular)ADME-ToxMolecular Medicinebenzo[b]thiophenes
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Synthesis and biological evaluation of a D-ring-contracted analogue of lamellarin D

2017

A D-ring contracted analogue of the strongly cytotoxic marine pyrrole alkaloid lamellarin D was synthesized and investigated for its antiproliferative action towards a wild type and a multidrug resistant (MDR) cancer cell line. The compound was found to inhibit tumor cell growth at submicromolar concentrations and showed a lower relative resistance in the MDR cell line than the antitumor drug camptothecin to which lamellarin D shows cross resistance and with which lamellarin D shares the same binding site.

Cell SurvivalStereochemistryClinical BiochemistryPharmaceutical ScienceAntineoplastic Agents010402 general chemistryHeterocyclic Compounds 4 or More Rings01 natural sciencesBiochemistrychemistry.chemical_compoundCoumarinsCell Line TumorDrug DiscoverymedicineHumansCytotoxic T cellheterocyclic compoundsBinding siteMolecular BiologyBinding Sites010405 organic chemistryChemistryAlkaloidOrganic ChemistryWild typeIsoquinolinesProtein Structure Tertiary0104 chemical sciencesG2 Phase Cell Cycle CheckpointsMolecular Docking SimulationMultiple drug resistanceDNA Topoisomerases Type IDrug Resistance NeoplasmMutagenesisCell cultureLamellarin DM Phase Cell Cycle CheckpointsMolecular MedicineTopoisomerase I InhibitorsCamptothecinmedicine.drugBioorganic & Medicinal Chemistry
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Computational identification of cell-specific variable regions in ChIP-seq data.

2019

ABSTRACT Chromatin immunoprecipitation followed by sequencing (ChIP-seq) is used to identify genome-wide DNA regions bound by proteins. Several sources of variation can affect the reproducibility of a particular ChIP-seq assay, which can lead to a misinterpretation of where the protein under investigation binds to the genome in a particular cell type. Given one ChIP-seq experiment with replicates, binding sites not observed in all the replicates will usually be interpreted as noise and discarded. However, the recent discovery of high-occupancy target (HOT) regions suggests that there are regions where binding of multiple transcription factors can be identified. To investigate these regions,…

Cell typeAcademicSubjects/SCI00010Computational biologyPlasma protein bindingBiologyGenomeCell LineEvolution Molecular03 medical and health scienceschemistry.chemical_compoundMice0302 clinical medicineNarese/3Cell Line TumorGeneticsAnimalsHumansEpigeneticsBinding sitePromoter Regions GeneticTranscription factorEmbryonic Stem Cells030304 developmental biology0303 health sciencesPrincipal Component AnalysisBinding SitesNucleotidesGenetic VariationPromoterGenomicsChromatinchemistryCpG siteMCF-7 CellsChromatin Immunoprecipitation SequencingMethods OnlineR-Loop StructuresK562 CellsChromatin immunoprecipitation030217 neurology & neurosurgeryFunction (biology)DNATranscription FactorsNucleic acids research
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MOLECULAR BASIS OF DRUG PHOTOTOXICITY: PHOTOSENSITIZED CELL DAMAGE BY THE MAJOR PHOTOPRODUCT OF TIAPROFENIC ACID

1994

Tiaprofenic acid is a photosensitizing nonsteroidal anti-inflammatory drug, whose major photoproduct (decarboxytiaprofenic acid) is also a potent photosensitizer. Because of the lack of the carboxylate moiety, this photoproduct is more lipophilic and might bind more efficiently to cell membranes, thereby causing phototoxic damage. To verify the feasibility of this hypothesis, we have prepared the 3H-labeled analogs of tiaprofenic acid and its photoproduct and examined the binding, persistence and phototoxicity of the photoproduct using poorly metabolizing (fibroblasts) and actively metabolizing cells (hepatocytes). The photoproduct of tiaprofenic acid accumulates in both cell types as it is…

Cell typePhotochemistryCellBiochemistryIn vivomedicineHumansPhotosensitizerPhysical and Theoretical ChemistryCell damageCells CulturedBinding SitesPhotosensitizing AgentsChemistryGeneral MedicineFibroblastsmedicine.diseasePhotobleachingmedicine.anatomical_structureBiochemistrybiological sciencessense organsPropionatesPhototoxicityTiaprofenic acidmedicine.drugPhotochemistry and Photobiology
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Subcellular targeting of multiligand-binding protein gC1qR.

1999

Abstract gC1q receptor, a protein originally described as the cell surface receptor for the globular heads of complement factor C1q, has been found to bind human H-kininogen with high affinity and specificity. Therefore, gC1qR has been considered candidate kininogen docking site on the surfaces of platelets, neutrophils and endothelial cells. Recent work demonstrating that gC1qR is an intracellular protein that is tightly associated with mitochondria rather than targeted to the cell surface has challenged this view. To further probe cellular trafficking routes of gC1qR, we overexpressed human gC1qR in a mammalian cell and monitored cell surface exposure of recombinant gC1qR by virtue of its…

CellComplement factor IBiologyLigandsMitochondrial ProteinsCell surface receptormedicineAnimalsHumansBinding siteReceptorPharmacologyBinding SitesMembrane GlycoproteinsBinding proteinComplement C1qBiological TransportTransfectionMolecular biologyCell biologyReceptors Complementmedicine.anatomical_structureHyaluronan ReceptorsCell cultureCOS CellsCarrier ProteinsProtein Processing Post-Translationalcirculatory and respiratory physiologySubcellular FractionsImmunopharmacology
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Noncompetitive agonism at nicotinic acetylcholine receptors; functional significance for CNS signal transduction.

1995

The alkaloids (-)physostigmine (Phy), galanthamine (Gal) and codeine (Cod), and several derivatives and homologous compounds, can act as noncompetitive agonists (NCA) of nicotinic acetylcholine receptors (nAChR) from Torpedo electrocytes, frog and mammalian muscle cells, clonal rat pheochromocytoma cells, cultured hippocampal neurons and several ectopic expression systems, by interacting with a binding site on the alpha-subunits of these nAChRs that is insensitive to the natural transmitter, acetylcholine (ACh), and ACh-competitive agonists and antagonists. Several endogenous ligands, including opioid-type compounds, can also act via this site, albeit at higher concentrations than is typica…

Central Nervous SystemPharmacologyReceptors NicotinicLigandsBiochemistrylaw.inventionEvolution MolecularlawMuscarinic acetylcholine receptormedicineAnimalsHumansNicotinic AgonistsBinding siteReceptorMolecular BiologyAcetylcholine receptorBinding SitesMolecular StructureChemistryCell BiologyAcetylcholineCell biologyNicotinic agonistnervous systemSignal transductionAcetylcholineTorpedomedicine.drugSignal TransductionJournal of receptor and signal transduction research
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