Search results for "binding"

showing 10 items of 3896 documents

Kinetic experiments on the binding of metyrapone to liver microsomes

1969

Kinetic experiments on the inhibition of oxidative microsomal O- and N-demethylations by metyrapone (2-methyl-1, 2-bis(3-pyridyl)-l-propanone, Su 4885) were carried out using mouse liver microsomes as the enzyme source. The model substrates were p-nitroanisole and N-monomethyl-p-nitroaniline. It was shown that the inhibition is competitive. The K i for metyrapone is 0.42 × 10−4 M and for the reduced metabolite of metyrapone 1.15×10−4 M. Their spectral dissooiation constants as determined from difference spectra have almost the same values. From this it is concluded that the degree of inhibition is correlated to the amount of metyrapone bound to cytochrome P-450. Metyrapone does not seem to …

CytochromeStereochemistryMetaboliteMixed Function OxygenasesNitrophenolsMicechemistry.chemical_compoundNon-competitive inhibitionmedicineAnimalsBinding siteBiotransformationPharmacologyAniline CompoundsBinding SitesMetyraponebiologyChemistryProadifenSubstrate (chemistry)General MedicineMetyraponeReceptor–ligand kineticsKineticsBiochemistryMicrosomes LiverMicrosomebiology.proteinCytochromesmedicine.drugNaunyn-Schmiedebergs Archiv f�r Pharmakologie
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All-Atom simulations disclose how cytochrome reductase reshapes the substrate access/egress routes of its partner cyp450s

2020

Cytochromes P450 enzymes (CYP450s) promote the oxidative metabolism of a variety of substrates via the electrons supplied by the cytochrome P450 reductase (CPR) and upon formation of a CPR/CYP450 adduct. In spite of the pivotal regulatory importance of this process, the impact of CPR binding on the functional properties of its partner CYP450 remains elusive. By performing multiple microsecond-long all-Atom molecular dynamics simulations of a 520â »000-Atom model of a CPR/CYP450 adduct embedded in a membrane mimic, we disclose the molecular terms for their interactions, considering the aromatase (HA) enzyme as a proxy of the CYP450 family. Our study strikingly unveils that CPR binding alters…

CytochromeStereochemistryeducationPlasma protein binding-ReductaseMolecular Dynamics Simulation010402 general chemistry01 natural sciencesSubstrate SpecificityElectron Transport03 medical and health sciencesAromataseCytochrome P-450 Enzyme Systemhealth services administrationHumansddc:530General Materials Sciencecardiovascular diseasesP450 EnzymesPhysical and Theoretical Chemistryhealth care economics and organizations030304 developmental biologyNADPH-Ferrihemoprotein Reductase0303 health sciencesOxidative metabolismbiologyChemistrySubstrate (chemistry)Cytochrome P450 reductaseElectron transport chain0104 chemical sciencesAromatase; Cytochrome P-450 Enzyme System; Electron Transport; Humans; Molecular Dynamics Simulation; NADPH-Ferrihemoprotein Reductase; Protein Binding; Substrate SpecificitySettore CHIM/03 - Chimica Generale E Inorganicabiology.proteintherapeuticsProtein Binding
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Presentation of an Immunodominant Immediate-Early CD8+ T Cell Epitope Resists Human Cytomegalovirus Immunoevasion.

2013

Control of human cytomegalovirus (HCMV) depends on CD8+ T cell responses that are shaped by an individual's repertoire of MHC molecules. MHC class I presentation is modulated by a set of HCMV-encoded proteins. Here we show that HCMV immunoevasins differentially impair T cell recognition of epitopes from the same viral antigen, immediate-early 1 (IE-1), that are presented by different MHC class I allotypes. In the presence of immunoevasins, HLA-A- and HLA-B-restricted T cell clones were ineffective, but HLA-C*0702-restricted T cell clones recognized and killed infected cells. Resistance of HLA-C*0702 to viral immunoevasins US2 and US11 was mediated by the alpha3 domain and C-terminal region …

Cytomegalovirus InfectionMaleViral DiseasesvirusesCytomegalovirusEpitopes T-LymphocyteNK cellsAdaptive ImmunityCD8-Positive T-LymphocytesMajor Histocompatibility ComplexInterleukin 21Viral Envelope ProteinsCytotoxic T celllcsh:QH301-705.5Antigen PresentationbiologyViral Immune EvasionImmune cellsRNA-Binding ProteinsInnate ImmunityKiller Cells Naturalmedicine.anatomical_structureInfectious DiseasesCytomegalovirus InfectionsMedicineFemaleResearch Articlelcsh:Immunologic diseases. AllergyT cellImmunologyCD1T cells610StreptamerMicrobiologyImmediate-Early ProteinsImmunomodulationViral ProteinsVirologyMHC class IGeneticsmedicineHumansAntigen-presenting cellMolecular BiologyBiologyImmune EvasionHistocompatibility Antigens Class IImmunityMHC restrictionVirologyProtein Structure Tertiarylcsh:Biology (General)Immunologybiology.proteinParasitologylcsh:RC581-607
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Myc Promoter-Binding Protein-1 (MBP-1) Is a Novel Potential Prognostic Marker in Invasive Ductal Breast Carcinoma

2010

BackgroundAlpha-enolase is a glycolytic enzyme that catalyses the formation of phosphoenolpyruvate in the cell cytoplasm. α-Enolase and the predominantly nuclear Myc promoter-binding protein-1 (MBP-1) originate from a single gene through the alternative use of translational starting sites. MBP-1 binds to the P2 c-myc promoter and competes with TATA-box binding protein (TBP) to suppress gene transcription. Although several studies have shown an antiproliferative effect of MBP-1 overexpression on several human cancer cells, to date detailed observations of α-enolase and MBP-1 relative expression in primary tumors versus normal tissues and their correlation with clinicopathological features ha…

CytoplasmAlpha-enolasePROGRESSIONAged 80 and overRegulation of gene expressionMultidisciplinaryQRGenetics and Genomics/Gene ExpressionMiddle AgedPrognosisPathology/Molecular PathologyNUDE-MICETransport proteinCarcinoma DuctalDNA-Binding ProteinsGene Expression Regulation NeoplasticProtein Transportmedicine.anatomical_structureGLYCOLYTIC ENZYMEOncology/Breast CancerMedicineCELL LUNG-CANCER; ALPHA-ENOLASE; PROTEOMIC ANALYSIS; GLYCOLYTIC ENZYME; NUDE-MICE; GENE; IDENTIFICATION; PROGRESSION; EXPRESSION; METASTASESFemalePROTEOMIC ANALYSISEnolase MBP-1 Breast cancer ImmunohistochemistryResearch ArticleAdultEXPRESSIONScienceCELL LUNG-CANCERBreast NeoplasmsBiologyDNA-binding proteinBiomarkers TumormedicineHumansNeoplasm InvasivenessGeneAgedCell NucleusIDENTIFICATIONBinding proteinALPHA-ENOLASEGENEMolecular biologySettore BIO/18 - GeneticaCell nucleusMETASTASESCytoplasmPhosphopyruvate Hydratasebiology.proteinPLoS ONE
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The differentiation antigen NY-BR-1 is a potential target for antibody-based therapies in breast cancer

2007

Antibody-based cancer immunotherapy relies on the identification and characterization of target antigens and the development of potent antibodies recognizing the target. Here we report the expression analysis and molecular characterization of the differentiation antigen NY-BR-1, which we previously identified by using the SEREX (serological analysis of recombinant cDNA expression libraries) method. Corroborating methodologies, including mRNA quantitation and immunoblotting show that NY-BR-1 is strongly expressed in >70% of 129 breast tumors. Application of a NY-BR-1 specific antibody demonstrated NY-BR-1 expression in primary and metastastic breast cancers. In contrast, most of the breast c…

CytoplasmCancer ResearchPathologymedicine.medical_specialtyRecombinant Fusion Proteinsmedicine.medical_treatmentCellular differentiationGreen Fluorescent ProteinsImmunoblottingBreast NeoplasmsBiologyTargeted therapyBreast cancerAntigenCancer immunotherapyAntigens NeoplasmCell Line TumormedicineHumansRNA MessengerBinding SitesMicroscopy ConfocalReverse Transcriptase Polymerase Chain ReactionCell MembraneAntibodies MonoclonalMembrane ProteinsFlow Cytometrymedicine.diseaseAntigens DifferentiationImmunohistochemistryTumor antigenGene Expression Regulation NeoplasticOncologyCancer researchbiology.proteinImmunohistochemistryFemaleAntibodyHydrophobic and Hydrophilic InteractionsInternational Journal of Cancer
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Nuclear Translocation of Mismatch Repair Proteins MSH2 and MSH6 as a Response of Cells to Alkylating Agents

2000

Mammalian mismatch repair has been implicated in mismatch correction, the prevention of mutagenesis and cancer, and the induction of genotoxicity and apoptosis. Here, we show that treatment of cells specifically with agents inducing O(6)-methylguanine in DNA, such as N-methyl-N'-nitro-N-nitrosoguanidine and N-methyl-N-nitrosourea, elevates the level of MSH2 and MSH6 and increases GT mismatch binding activity in the nucleus. This inducible response occurs immediately after alkylation, is long-lasting and dose-dependent, and results from translocation of the preformed MutSalpha complex (composed of MSH2 and MSH6) from the cytoplasm into the nucleus. It is not caused by an increase in MSH2 gen…

CytoplasmDNA RepairBase Pair MismatchRNA StabilityChromosomal translocationmedicine.disease_causeBiochemistrychemistry.chemical_compoundMismatch Repair Endonuclease PMS2Adenosine TriphosphatasesNuclear ProteinsMethylnitrosoureaNeoplasm ProteinsDNA-Binding ProteinsMutS Homolog 2 ProteinDNA mismatch repairMutL Protein Homolog 1Protein BindingAlkylating AgentsMethylnitronitrosoguanidinecongenital hereditary and neonatal diseases and abnormalitiesGuanineActive Transport Cell NucleusBiologyCell LineO(6)-Methylguanine-DNA MethyltransferaseProto-Oncogene ProteinsDNA Repair ProteinmedicineHumansRNA MessengerneoplasmsMolecular BiologyAdaptor Proteins Signal TransducingCell NucleusMutagenesisnutritional and metabolic diseasesDNACell BiologyDNA MethylationMolecular biologydigestive system diseasesMSH6DNA Repair EnzymesGene Expression RegulationchemistryMSH2Carrier ProteinsGenotoxicityDNADNA DamageHeLa CellsJournal of Biological Chemistry
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DNA binding of L1 is required for human papillomavirus morphogenesis in vivo.

2002

AbstractThe role of putative DNA-binding domains of human papillomavirus (HPV) capsid proteins for DNA encapsidation in vivo is still unknown. We have now analyzed mutants of the major capsid protein L1 of HPV type 33, which are defective for DNA binding, for their ability to encapsidate DNA using an in vivo packaging approach. Since the DNA-binding domain and the nuclear localization signal (NLS) of L1 overlap, both a carboxy-terminal deletion mutant (L1-1/470) and a substitution mutant (L1-1/477M9) were analyzed. L1-1/477M9 has the classical NLS replaced by a noncanonical NLS taken from the human hnRNP protein A1. The mutant proteins were defective for DNA binding in contrast to wild-type…

CytoplasmHMG-boxMutantBiologyKidneypapillomavirusCell Linechemistry.chemical_compoundCapsidVirologyHumansPoint MutationDNA bindingPapillomaviridaeInfectivityCell NucleusVirus AssemblypseudovirionsL1DNA encapsidationMolecular biologyChromatinDNA-Binding ProteinschemistryCapsidCytoplasmDNA ViralchromatinDNANuclear localization sequenceVirology
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Competitive binding of Rab21 and p120RasGAP to integrins regulates receptor traffic and migration

2011

P120RasGAP competes with Rab21 for binding to the cytoplasmic domain of integrin α-subunits, thereby promoting receptor escape from early endosomes and recycling to the plasma membrane.

CytoplasmIntegrinsEndosomeEndocytic cycleIntegrinVesicular Transport ProteinsEndosomesCD49cBinding CompetitiveModels BiologicalArticleCollagen receptor03 medical and health sciencesMice0302 clinical medicineSDG 3 - Good Health and Well-beingCell MovementCell Line TumorAnimalsHumansResearch Articles030304 developmental biology0303 health sciencesbiologyCell Membranep120 GTPase Activating ProteinCell BiologyCell biologyProtein Structure TertiaryIntegrin alpha Mrab GTP-Binding Proteins030220 oncology & carcinogenesisbiology.protein/dk/atira/pure/sustainabledevelopmentgoals/good_health_and_well_beingIntegrin beta 6RabProtein Binding
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Ectodomain shedding of L1 adhesion molecule promotes cell migration by autocrine binding to integrins.

2001

The L1 adhesion molecule plays an important role in axon guidance and cell migration in the nervous system. L1 is also expressed by many human carcinomas. In addition to cell surface expression, the L1 ectodomain can be released by a metalloproteinase, but the biological function of this process is unknown. Here we demonstrate that membrane-proximal cleavage of L1 can be detected in tumors and in the developing mouse brain. The shedding of L1 involved a disintegrin and metalloproteinase (ADAM)10, as transfection with dominant-negative ADAM10 completely abolishes L1 release. L1-transfected CHO cells (L1-CHO) showed enhanced haptotactic migration on fibronectin and laminin, which was blocked …

CytoplasmIntegrinsL1; shedding; ADAM10; cell migration; integrinsADAM10IntegrinGene ExpressionCHO CellsBiologyArticle03 medical and health sciencesParacrine signallingMice0302 clinical medicineCell MovementCricetinaeEndopeptidasesTumor Cells CulturedAnimalsAspartic Acid EndopeptidasesHumansReceptors VitronectinFibrinolysinNeural Cell Adhesion Molecules030304 developmental biology0303 health sciencesBinding SitesMembrane GlycoproteinsCell adhesion moleculeCell MembraneAntibodies MonoclonalBrainCell migrationBiological TransportCell BiologyMolecular biologyPeptide FragmentsCell biologyFibronectinAutocrine CommunicationEctodomainSolubility030220 oncology & carcinogenesisbiology.proteinNeural cell adhesion moleculeAmyloid Precursor Protein SecretasesLeukocyte L1 Antigen ComplexOligopeptidesThe Journal of cell biology
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Activation and translocation of p38 mitogen-activated protein kinase after stimulation of monocytes with contact sensitizers.

2002

Recently we described the induction of tyrosine phosphorylation by contact sensitizers as an early molecular event during the activation of antigen- presenting cells. In this study, the role of the p38 mitogen-activated protein kinase for the activation of human monocytes after exposure to four structurally unrelated contact sensitizers was analyzed in comparison with the irritant benzalkonium chloride and an inductor of oxidative stress (H 2 O 2 ) using immunofluorescence, Western blotting, and enzyme-linked immunosorbent assay techniques. Bio chemical analysis revealed a translocation of p38 from the cytoplasm to the detergent-resistant cell fraction only upon stimulation with contact sen…

CytoplasmMAP Kinase Signaling SystemPyridinesp38 mitogen-activated protein kinasesDermatologyBiologyIn Vitro TechniquesBiochemistryp38 Mitogen-Activated Protein KinasesMonocyteschemistry.chemical_compoundProto-Oncogene ProteinsHumansEnzyme InhibitorsPhosphorylationProtein kinase ATranscription factorMolecular Biologyets-Domain Protein Elk-1KinaseImidazolesTyrosine phosphorylationBiological TransportCell BiologyMolecular biologyDNA-Binding ProteinsEnzyme ActivationIL-1β/irritantchemistryhaptenMitogen-activated protein kinasebiology.proteinIrritantsPhosphorylationSignal transductionMitogen-Activated Protein KinasesBenzalkonium CompoundsHaptenssignal transductionInterleukin-1Transcription FactorsThe Journal of investigative dermatology
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