Search results for "STABILITY"

showing 10 items of 3085 documents

Room Temperature Instability of E′γ Centers Induced by γ Irradiation in Amorphous SiO2

2008

We study by optical absorption measurements the stability of E'(gamma) centers induced in amorphous silica at room temperature by gamma irradiation up to 79 kGy. A significant portion of the defects spontaneously decay after the end of irradiation, thus allowing the partial recovery of the transparency loss initially induced by irradiation. The decay kinetics observed after gamma irradiation with a 0.6 kGy dose closely resembles that measured after exposure to 2000 pulses of pulsed ultraviolet (4.7 eV) laser light of 40 mJ/cm(2) energy density per pulse. In this regime, annealing is ascribed to the reaction of the induced E'(gamma) centers with diffusing H(2) of radiolytic origin. At higher…

CrystallographyTemperature instabilityChemistryAnalytical chemistrysistemi amorfi difetti di puntoPhysical and Theoretical ChemistryAmorphous silicaγ irradiationAmorphous solidGamma irradiationThe Journal of Physical Chemistry A
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On/Off Photoswitching in a Cyanide-Bridged {Fe2Co2} Magnetic Molecular Square

2013

International audience; A repeatable bidirectional paramagnetic ↔ diamagnetic photomagnetic effect has been observed in the cyanide-bridged Fe-Co square complex {[Fe{B(pz)(4)}(CN)(3)](2)[Co(bik)(2)](2)}(ClO(4))(2)*3H(2)O [B(pz)(4) = tetrapyrazolylborate, bik = bis(1-methylimidazol-2-yl)ketone]. Magnetic measurements and low-temperature single-crystal X-ray diffraction experiments have shown that a complete electron transfer from the diamagnetic Fe(II)-Co(III) state to the paramagnetic Fe(III)-Co(II) metastable state is induced by 808 nm laser light irradiation, whereas the diamagnetic state is recovered in an almost quantitative yield under irradiation at 532 nm.

CyanideINDUCED ELECTRON-TRANSFERTRANSITIONSRELAXATION010402 general chemistryPhotochemistry01 natural sciencesBiochemistryCOBALT-IRON CYANIDECatalysisPHOTOINDUCED MAGNETIZATIONParamagnetismchemistry.chemical_compoundElectron transferColloid and Surface ChemistryMetastability[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyIrradiationALKALI-METAL-IONPRUSSIAN BLUE ANALOGS010405 organic chemistryChemistryRelaxation (NMR)Photomagnetic effectGeneral Chemistry3. Good health0104 chemical sciencesCOSOLID-STATECrystallographyDiamagnetismJournal of the American Chemical Society
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Reinforced cyclam derivatives functionalized on the bridging unit

2016

International audience; A new synthetic method has been developed for the preparation of reinforced cyclams (1,4,8,11-tetraazacyclotetradecane) C-functionalized on the bridging unit, by using a "one pot" reaction starting from the appropriate bis-aminal cyclam intermediate. The high reactivity of quaternized aminal moiety toward nucleophilic agent has been used to elaborate a new class of cross-bridged and side-bridged cyclam derivatives containing cyanide group on the ethylene bridge. Several chelators and corresponding copper(II) complexes have been prepared and characterized by X-ray diffraction. These new constrained polyazamacrocycles are valuable precursors of bifunctional chelating a…

CyanideRadiometals010402 general chemistry01 natural sciencesCatalysisCopper(ii) complexesCoordination complexContinuous symmetry measureschemistry.chemical_compoundNucleophileBifunctional chelator[SDV.IDA]Life Sciences [q-bio]/Food engineeringCyclamMaterials ChemistryOrganic chemistryMoietyChelationBifunctionalPolyhedrachemistry.chemical_classification010405 organic chemistry[ SDV.IDA ] Life Sciences [q-bio]/Food engineeringGeneral ChemistryCombinatorial chemistry0104 chemical sciencesCoordination chemistrychemistryAminalTherapyStability
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Light-controlled reversible modulation of frontier molecular orbital energy levels in trifluoromethylated diarylethenes

2017

Among bistable photochromic molecules, diarylethenes (DAEs) possess the distinct feature that upon photoisomerization they undergo a large modulation of their π-electronic system, accompanied by a marked shift of the HOMO/LUMO energies and hence oxidation/reduction potentials. The electronic modulation can be utilized to remote-control charge- as well as energy-transfer processes and it can be transduced to functional entities adjacent to the DAE core, thereby regulating their properties. In order to exploit such photoswitchable systems it is important to precisely adjust the absolute position of their HOMO and LUMO levels and to maximize the extent of the photoinduced shifts of these energ…

Cyclic voltammetryBistabilityPhotoisomerizationQuantum yields010402 general chemistryPhotochemistryDiarylethene01 natural sciencesCatalysischemistry.chemical_compoundPhotochromismMoleculeMolecular orbitalHOMO/LUMOquantum yieldsFrontier molecular orbital energiesTrifluoromethyl010405 organic chemistryChemistryFrontier molecular orbital energieOrganic Chemistryfrontier molecular orbital energiesGeneral ChemistryphotochromismPhotochromismcyclic voltammetry0104 chemical sciencesdiarylethenes540 Chemie und zugeordnete WissenschaftenDiarylethenesddc:540IsomerizationChemistry - A European Journal
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Binding properties of mono-6-amino-beta-cyclodextrin towards p-nitroaniline derivatives: a polarimetric study

Cyclodextrins host-guest interactions stability constants polarimetric investigationSettore CHIM/06 - Chimica Organica
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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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Regulation of ribonucleotide reductase in response to iron deficiency

2011

Ribonucleotide reductase (RNR) is an essential enzyme required for DNA synthesis and repair. Although iron is necessary for class Ia RNR activity, little is known about the mechanisms that control RNR in response to iron deficiency. In this work, we demonstrate that yeast cells control RNR function during iron deficiency by redistributing the Rnr2–Rnr4 small subunit from the nucleus to the cytoplasm. Our data support a Mec1/Rad53-independent mechanism in which the iron-regulated Cth1/Cth2 mRNA-binding proteins specifically interact with the WTM1 mRNA in response to iron scarcity, and promote its degradation. The resulting decrease in the nuclear-anchoring Wtm1 protein levels leads to the re…

CytoplasmSaccharomyces cerevisiae ProteinsDeoxyribonucleoside triphosphateRibonucleoside Diphosphate ReductaseRNA StabilityProtein subunitSaccharomyces cerevisiaeCell Cycle ProteinsSaccharomyces cerevisiaeProtein Serine-Threonine KinasesBiologyResponse ElementsArticleTristetraprolinGene Expression Regulation FungalRibonucleotide ReductasesHumansRNA MessengerMolecular BiologyTranscription factorCell NucleusDNA synthesisIntracellular Signaling Peptides and ProteinsFungal geneticsRNA-Binding ProteinsRNA FungalIron DeficienciesCell Biologybiology.organism_classificationDNA-Binding ProteinsRepressor ProteinsCheckpoint Kinase 2Protein SubunitsProtein TransportRibonucleotide reductaseBiochemistryCytoplasmTranscription Factors
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Gene expression is circular: factors for mRNA degradation also foster mRNA synthesis.

2013

SummaryMaintaining proper mRNA levels is a key aspect in the regulation of gene expression. The balance between mRNA synthesis and decay determines these levels. We demonstrate that most yeast mRNAs are degraded by the cytoplasmic 5′-to-3′ pathway (the “decaysome”), as proposed previously. Unexpectedly, the level of these mRNAs is highly robust to perturbations in this major pathway because defects in various decaysome components lead to transcription downregulation. Moreover, these components shuttle between the cytoplasm and the nucleus, in a manner dependent on proper mRNA degradation. In the nucleus, they associate with chromatin—preferentially ∼30 bp upstream of transcription start-sit…

CytoplasmSaccharomyces cerevisiae ProteinsTranscription GeneticRNA StabilityGenes FungalRNA polymerase IIRNA-binding proteinSaccharomyces cerevisiaeGenètica molecularGeneral Biochemistry Genetics and Molecular Biology03 medical and health sciencesGene Expression ProcessTranscription (biology)Gene Expression Regulation FungalGene expressionP-bodiesmedicineRNA Messenger030304 developmental biologyRegulation of gene expressionCell Nucleus0303 health sciencesbiologyBiochemistry Genetics and Molecular Biology(all)030302 biochemistry & molecular biologyRNA-Binding ProteinsRNA FungalMolecular biologyCell biologyCell nucleusmedicine.anatomical_structureExoribonucleasesbiology.proteinRNARNA Polymerase IICell
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Dysregulation of DNA methylation induced by past arsenic treatment causes persistent genomic instability in mammalian cells

2015

The mechanisms by which arsenic-induced genomic instability is initiated and maintained are poorly understood. To investigate potential epigenetic mechanisms, in this study we evaluated global DNA methylation levels in V79 cells and human HaCaT keratinocytes at several time points during expanded growth of cell cultures following removal of arsenite exposures. We have found altered genomic methylation patterns that persisted up to 40 cell generations in HaCaT cells after the treatments were withdrawn. Moreover, mRNA expression levels were evaluated by RT-PCR for DNMT1, DNMT3A, DNMT3B, HMLH1, and HMSH2 genes, demonstrating that the down regulation of DNMT3A and DNMT3B genes, but not DNMT1, o…

DNA (Cytosine-5-)-Methyltransferase 1KeratinocytesDNA methylationArsenitesarsenicNuclear ProteinsFibroblastsgenomic instabilityArticleDNA Methyltransferase 3ASettore BIO/18 - GeneticaCricetulusLong Interspersed Nucleotide ElementsMutS Homolog 2 Protein5-MethylcytosineAnimalsDNA (Cytosine-5-)-MethyltransferasesMutL Protein Homolog 1Promoter Regions GeneticCells CulturedAdaptor Proteins Signal Transducing
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Compromised repair of radiation-induced DNA double-strand breaks in Fanconi anemia fibroblasts in G2

2020

Fanconi anemia (FA) is a rare chromosomal instability syndrome with various clinical features and high cancer incidence. Despite being a DNA repair disorder syndrome and a frequently observed clinical hypersensitivity of FA patients towards ionizing radiation, the experimental evidence regarding the efficiency of radiation-induced DNA double-strand break (DSB) repair in FA is very controversial. Here, we performed a thorough analysis of the repair of radiation-induced DSBs in G1 and G2 in FA fibroblasts of complementation groups A, C, D1 (BRCA2), D2, E, F, G and P (SLX4) in comparison to normal human lung and skin fibroblasts. γH2AX, 53BP1, or RPA foci quantification after X-irradiation was…

DNA End-Joining RepairBiologyBiochemistryFanconi Anemia Complementation Group F ProteinHistonesRecombinases03 medical and health scienceschemistry.chemical_compound0302 clinical medicineFanconi anemiaChromosome instabilitymedicineHumansDNA Breaks Double-StrandedFanconi Anemia Complementation Group G ProteinMolecular BiologyCells Cultured030304 developmental biologyBRCA2 ProteinChromosome Aberrations0303 health sciencesFanconi Anemia Complementation Group A ProteinFanconi Anemia Complementation Group D2 ProteinX-RaysCell CycleFanconi Anemia Complementation Group C ProteinRecombinational DNA RepairChromosomeDNACell BiologyFibroblastsCell cyclemedicine.diseaseFanconi Anemia Complementation Group E ProteinComplementationKineticsenzymes and coenzymes (carbohydrates)Fanconi Anemiachemistry030220 oncology & carcinogenesisPremature chromosome condensationMutationCancer researchChromatidTumor Suppressor p53-Binding Protein 1DNADNA Repair
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