Search results for "binding"

showing 10 items of 3896 documents

<title>Shallow electron traps in alkali halide crystals: Mollwo-Ivey relations of the optical absorption bands</title>

2001

Evidences are given that two classes of the transient IR- absorption bands: (a) with max. at 0.27-0.36 eV in NaCl, KCl, KBr, KI and RbCl (due to shallow electron traps according G. Jacobs or due to bound polarons according E.V. Korovkin and T.A. Lebedkina) and (b) with max. at 0.15-0.36 eV in NaI, NaBr, NaCl:I, KCl:I, RbCl:I and RbBr:I (due to on-center STE localized at iodine dimer according M. Hirai and collaborators) are caused by the same defect- atomic alkali impurity center [M+]c0e- (electron e- trapped by a substitutional smaller size alkali cation impurity [M+]c0). The Mollwo-Ivey plots (for the transient IR-absorption bands) of the zero-phonon line energy E0 (for NaCl, KCl, KBr, Rb…

Crystallographychemistry.chemical_compoundChemistryImpurityDimerBinding energyHalideElectronAbsorption (chemistry)Alkali metalPolaronSPIE Proceedings
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Pharmacogenomic determination of genes associated with sensitivity or resistance of tumor cells to curcumin and curcumin derivatives

2010

Curcuma longa L. has long been used as a medicinal plant in traditional Chinese medicine against abdominal disorders. Its active constituent curcumin has anti-inflammatory, chemopreventive and cytotoxic properties. In the present investigation, we have analyzed the cytotoxic activity of curcumin and four derivatives. Among these compounds, ethoxycurcumintrithiadiazolaminomethylcarbonate was the most cytotoxic one. The curcumin-type compounds were not cross-resistant to standard anticancer drugs and were not involved in ATP-binding cassette transporter-mediated multidrug resistance. A combined approach of messenger RNA-based microarray profiling, COMPARE analyses and signaling pathway analys…

CurcuminEndocrinology Diabetes and MetabolismClinical BiochemistryAnti-Inflammatory AgentsATP-binding cassette transporterTraditional Chinese medicineDrug resistanceBiologyPharmacologyBiochemistrychemistry.chemical_compoundCell Line TumormedicineHumansCurcumaMolecular BiologyNutrition and DieteticsCancerbiology.organism_classificationmedicine.diseaseMultiple drug resistancechemistryDrug Resistance NeoplasmPharmacogeneticsPharmacogenomicsCurcuminATP-Binding Cassette TransportersThe Journal of Nutritional Biochemistry
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Specific recognition of fluoride anion using a metallamacrocycle incorporating a uranyl-salen unit

2008

The design and synthesis of a novel fluoride receptor that uses a salen-complexed Lewis acidic uranyl center as the sole binding site is reported here. This receptor binds fluoride anions in DMSO with a high affinity constant (K > 106 M-1) and exhibits a negligible affinity (K < 10 M-1) towards otherwise effective competitors, such as acetate, phosphate and cyanide anions.

CyanideInorganic chemistryAffinity constantGeneral ChemistryPhosphateUranylMedicinal chemistrysupramolecular chemistryCatalysisIonfluoride recognitionchemistry.chemical_compoundchemistryMaterials Chemistrysalen-complexesBinding siteReceptorFluoride
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Miltirone Induces G2/M Cell Cycle Arrest and Apoptosis in CCRF-CEM Acute Lymphoblastic Leukemia Cells

2015

Miltirone (1) is a diterpene quinone extracted from a well-known Chinese traditional herb (Salvia miltiorrhiza). We investigated the cytotoxic effects of miltirone toward sensitive and multidrug-resistant acute lymphoblastic leukemia cell lines. Miltirone inhibited multidrug-resistant P-glycoprotein (P-gp)-overexpressing CEM/ADR5000 cells better than drug-sensitive CCRF-CEM wild-type cells, a phenomenon termed collateral sensitivity. Flow cytometric analyses revealed that miltirone induced G2/M arrest and apoptosis. Furthermore, miltirone stimulated reactive oxygen species (ROS) generation and mitochondrial membrane potential (MMP) disruption, which in turn induced DNA damage and activation…

Cyclin-Dependent Kinase Inhibitor p21ATP Binding Cassette Transporter Subfamily BDNA damagePoly ADP ribose polymeraseCellPharmaceutical ScienceApoptosisSalvia miltiorrhizaAnalytical ChemistryDrug DiscoverymedicineHumansCyclin B1CaspaseMembrane Potential MitochondrialPharmacologyCyclin-dependent kinase 1Molecular StructurebiologyOrganic ChemistryPhenanthrenesPrecursor Cell Lymphoblastic Leukemia-LymphomaMolecular biologyG2 Phase Cell Cycle Checkpointsmedicine.anatomical_structureComplementary and alternative medicineApoptosisCell cultureCaspasesbiology.proteinMolecular MedicineReactive Oxygen SpeciesJournal of Natural Products
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Ikaros-1 couples cell cycle arrest of late striatal precursors with neurogenesis of enkephalinergic neurons

2010

et al.

Cyclin-Dependent Kinase Inhibitor p21CalbindinsEnkephalinNeurogenesiseducationCentral nervous systemCell Cycle ProteinsStriatumSubstance PBiologyEfferent PathwaysCalbindinIkaros Transcription FactorMiceS100 Calcium Binding Protein GmedicineAnimalsProgenitor cellTranscription factorhealth care economics and organizationsHomeodomain ProteinsMice KnockoutNeuronsStem CellsGeneral NeuroscienceNeurogenesisCell DifferentiationEnkephalinsCell cycleCorpus StriatumGenes cdcMice Inbred C57BLmedicine.anatomical_structurenervous systemTrans-ActivatorsNeuroscienceTranscription FactorsThe Journal of Comparative Neurology
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Calmodulin binds to p21(Cip1) and is involved in the regulation of its nuclear localization.

1999

p21(Cip1), first described as an inhibitor of cyclin-dependent kinases, has recently been shown to have a function in the formation of cyclin D-Cdk4 complexes and in their nuclear translocation. The dual behavior of p21(Cip1) may be due to its association with other proteins. Different evidence presented here indicate an in vitro and in vivo interaction of p21(Cip1) with calmodulin: 1) purified p21(Cip1) is able to bind to calmodulin-Sepharose in a Ca(2+)-dependent manner, and this binding is inhibited by the calmodulin-binding domain of calmodulin-dependent kinase II; 2) both molecules coimmunoprecipitate when extracted from cellular lysates; and 3) colocalization of calmodulin and p21(Cip…

Cyclin-Dependent Kinase Inhibitor p21CalmodulinMolecular Sequence DataBiologyBiochemistryCell LineCalmodulinIn vivoCyclinsProto-Oncogene ProteinsmedicineAnimalsCyclin D1Amino Acid SequencePhosphorylationMolecular BiologyCyclinCell NucleusSulfonamidesKinaseColocalizationCyclin-Dependent Kinase 4Cell BiologyImmunogold labellingPrecipitin TestsCyclin-Dependent KinasesCell biologyRatsEnzyme ActivationCell nucleusMicroscopy Electronmedicine.anatomical_structurebiology.proteinNuclear localization sequenceProtein BindingThe Journal of biological chemistry
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The structural plasticity of the C terminus of p21Cip1 is a determinant for target protein recognition.

2003

The cyclin-dependent kinase inhibitory protein p21(Cip1) might play multiple roles in cell-cycle regulation through interaction of its C-terminal domain with a defined set of cellular proteins such as proliferating cell nuclear antigen (PCNA), calmodulin (CaM), and the oncoprotein SET. p21(Cip1) could be described as an intrinsically unstructured protein in solution although the C-terminal domain adopts a well-defined extended conformation when bound to PCNA. However, the molecular mechanism of the interaction with CaM and the oncoprotein SET is not well understood, partly because of the lack of structural information. In this work, a peptide derived from the C-terminal domain of p21(Cip1) …

Cyclin-Dependent Kinase Inhibitor p21Models MolecularMagnetic Resonance SpectroscopyCalmodulinChromosomal Proteins Non-HistoneProtein ConformationPeptideBiologyLigandsBiochemistryBinding CompetitiveDomain (software engineering)Molecular recognitionCalmodulinCyclinsProliferating Cell Nuclear AntigenEscherichia coliHumansHistone ChaperonesMolecular Biologychemistry.chemical_classificationC-terminusCircular DichroismOrganic ChemistryCell CycleProteinsPeptide FragmentsCell biologyDNA-Binding ProteinschemistryBiochemistrybiology.proteinMolecular MedicineTarget proteinAlpha helixBinding domainTranscription FactorsChembiochem : a European journal of chemical biology
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Benzo[a]pyrene represses DNA repair through altered E2F1/E2F4 function marking an early event in DNA damage-induced cellular senescence

2020

AbstractTranscriptional regulation of DNA repair is of outmost importance for the restoration of DNA integrity upon genotoxic stress. Here we report that the potent environmental carcinogen benzo[a]pyrene (B[a]P) activates a cellular DNA damage response resulting in transcriptional repression of mismatch repair (MMR) genes (MSH2, MSH6, EXO1) and of RAD51, the central homologous recombination repair (HR) component, ultimately leading to downregulation of MMR and HR. B[a]P-induced gene repression is caused by abrogated E2F1 signalling. This occurs through proteasomal degradation of E2F1 in G2-arrested cells and downregulation of E2F1 mRNA expression in G1-arrested cells. Repression of E2F1-me…

Cyclin-Dependent Kinase Inhibitor p21SenescenceAcademicSubjects/SCI00010DNA repairDNA damageRAD51E2F4 Transcription FactorBiologyDNA Mismatch Repair03 medical and health sciences0302 clinical medicineCell Line TumorBenzo(a)pyreneGeneticsHumansCellular SenescenceCell Line Transformed030304 developmental biology0303 health sciencesGene regulation Chromatin and EpigeneticsRecombinational DNA RepairEpithelial CellsKv Channel-Interacting ProteinsCell Cycle CheckpointsDNAFibroblastsCell biologyDNA-Binding ProteinsRepressor ProteinsMSH6DNA Repair EnzymesExodeoxyribonucleasesMutS Homolog 2 ProteinGamma RaysMSH2030220 oncology & carcinogenesisCarcinogensMCF-7 CellsDNA mismatch repairRad51 RecombinaseCell agingE2F1 Transcription FactorDNA DamageSignal TransductionNucleic Acids Research
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Post-Translational Regulation of CYP450s Metabolism As Revealed by All-Atoms Simulations of the Aromatase Enzyme.

2019

Phosphorylation by kinases enzymes is a widespread regulatory mechanism able of rapidly altering the function of target proteins. Among these are cytochrome P450s (CYP450), a superfamily of enzymes performing the oxidation of endogenous and exogenous substrates thanks to the electron supply of a redox partner. In spite of its pivotal role, the molecular mechanism by which phosphorylation modulates CYP450s metabolism remains elusive. Here by performing microsecond-long all-atom molecular dynamics simulations, we disclose how phosphorylation regulates estrogen biosynthesis, catalyzed by the Human Aromatase (HA) enzyme. Namely, we unprecedentedly propose that HA phosphorylation at Y361 markedl…

CytochromeFlavin MononucleotideProtein ConformationGeneral Chemical EngineeringFlavin mononucleotide-Oxidative phosphorylationLibrary and Information SciencesMolecular Dynamics Simulation01 natural scienceschemistry.chemical_compoundAromatase0103 physical sciencesPost-translational regulationAromatasePhosphorylationBinding Sites010304 chemical physicsbiologyKinaseGeneral ChemistryMetabolism0104 chemical sciencesComputer Science ApplicationsCell biology010404 medicinal & biomolecular chemistrychemistrySettore CHIM/03 - Chimica Generale E Inorganicabiology.proteinFlavin-Adenine DinucleotidePhosphorylationQuantum TheoryProtein Processing Post-TranslationalNADPJournal of chemical information and modeling
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NADPH-cytochrome P-450 reductase: Preferential inhibition by ellipticine and other type II compounds having little effect on NADPH-cytochrome c reduc…

1980

Abstract Ellipticine (5,11-dimethyl-[6H]-pyrido[4,3b]carbazole) binds with an affinity greater than most other compounds known to interact with P-450. Control and 3-methylcholanthrene-induced aryl hydrocarbon (benzo[ a ]pyrene) hydroxylase (EC 1.14.14.2) and acetanilide 4-hydroxylase and control and phenobarbital-induced ethylmorphine N -demethylase activities are all markedly inhibited by ellipticine to about the same extent. Ellipticine and other Type II compounds (metyrapone, octylamine-1, pyridine and aniline) preferentially inhibit NADPH-cytochrome P-450 reductase activity, while affecting NADPH-cytochrome c reductase activity very little. Butanol-1, a compound having pure Reverse Type…

CytochromeStereochemistryIn Vitro TechniquesReductaseBiochemistryMixed Function OxygenasesMicechemistry.chemical_compoundAlkaloidsCytochrome P-450 Enzyme SystemAnimalsEllipticinesBenzopyrenesBinding siteAcetanilideNADPH-Ferrihemoprotein ReductasePharmacologychemistry.chemical_classificationbiologyCytochrome cDNAElectron acceptorchemistryMicrosomes Liverbiology.proteinMicrosomePyreneBiochemical Pharmacology
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