Search results for "Complex."

showing 10 items of 5824 documents

Multiphysics Optimization for Water-Cooled Breeding Blanket Design Enhancement

2021

The commercial feasibility of the first fusion power plant generation adopting D-T plasma is strongly dependent upon the self-sustainability in terms of tritium fueling. Within such a kind of reactor, the component selected to house the tritium breeding reactions is the breeding blanket, which is further assigned to heat power removal and radiation shielding functions. As a consequence of both its role and position, the breeding blanket is heavily exposed to both surface and volumetric heat loads and, hence, its design requires a typical multiphysics approach, from the neutronics to the thermo-mechanics. During last years, a great deal of effort has been put in the optimization of the breed…

DEMO WCLL Breeding Blanket optimization Complex Method RCC-MRxSettore ING-IND/19 - Impianti Nucleari
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Cascade complex formation by phosphate in the cobalt(II)/[30]aneN10 anaerobic system

1993

Abstract The interaction of phosphate with the mono- and binuclear cobalt(II) complexes of [30]aneN 10 (1,4,7,10,13,16,19,22,25,28-decaazacyclotriacontane) has been studied by potentiometry in 0.15 mol dm −3 NaClO 4 solution at 298.15 K under anaerobic conditions. The stable species [CoH 2 ([30]aneN 10 )PO 4 ] + , [CoH 4 ([30]aneN 10 )PO 4 ] 3+ , [Co 2 H([30]aneN 10 )PO 4 ] 2+ , [Co 2 H 2 ([30]aneN 10 )PO 4 ] 3+ and [Co 2 H 3 ([30]aneN 10 )PO 4 ] 4+ , where the phosphate anion is directly bound to the metal ions or acts as a second sphere ligand, are formed and their stability constants have been determined. The results obtained allowed for the selection of suitable conditions for the study…

DIOXYGEN CARRIERS; DIOXYGEN BINDING; Co(II) COMPLEXES; POLYAMINE LIGANDS; DITOPIC POLYAMINES; OPEN-CHAIN POLYAZAALKANES; THERMODYNAMICS; ANION COORDINATION CHEMISTRY; INCLUSION COMPLEXESINCLUSION COMPLEXESMetal ions in aqueous solutionComplex formationInorganic chemistryDIOXYGEN BINDINGchemistry.chemical_elementMedicinal chemistryCo(II) COMPLEXESInorganic Chemistrychemistry.chemical_compoundOPEN-CHAIN POLYAZAALKANESANION COORDINATION CHEMISTRYTHERMODYNAMICSMaterials ChemistryDIOXYGEN CARRIERSPhysical and Theoretical ChemistryLigandPhosphatePhosphate anionchemistryDITOPIC POLYAMINESChemical equilibriumAnaerobic exerciseCobaltPOLYAMINE LIGANDS
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The APC/C cofactor Cdh1 prevents replicative stress and p53-dependent cell death in neural progenitors

2013

The E3-ubiquitin ligase APC/C-Cdh1 is essential for endoreduplication but its relevance in the mammalian mitotic cell cycle is still unclear. Here we show that genetic ablation of Cdh1 in the developing nervous system results in hypoplastic brain and hydrocephalus. These defects correlate with enhanced levels of Cdh1 substrates and increased entry into the S phase in neural progenitors. However, cell division is prevented in the absence of Cdh1 due to hyperactivation of cyclin-dependent kinases, replicative stress, induction of p53, G2 arrest and apoptotic death of these progenitor cells. Concomitant ablation of p53 rescues apoptosis but not replicative stress, resulting in the presence of …

DNA ReplicationMaleProgrammed cell deathCell divisionNeurogenesisGeneral Physics and AstronomyApoptosisCell Cycle ProteinsBiologyAnaphase-Promoting Complex-CyclosomeCdh1 ProteinsGeneral Biochemistry Genetics and Molecular BiologyMice03 medical and health sciences0302 clinical medicineNeural Stem CellsAnimalsProgenitor cell030304 developmental biologyProgenitorMice KnockoutNeuronschemistry.chemical_classification0303 health sciencesDNA ligaseMultidisciplinaryCell CycleNeurogenesisBrainOrgan SizeGeneral ChemistryCell cycle3. Good healthCell biologyMice Inbred C57BLchemistrySynaptic plasticityFemaleTumor Suppressor Protein p53Cell Division030217 neurology & neurosurgeryNature Communications
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Replication origins and pause sites in sea urchin mitochondrial DNA

1992

We have used a combination of one- and two-dimensional agarose gel electrophoresis, and solution hybridization to strand-specific probes, to map the replication origin of sea urchin mitochondrial DNA and to investigate the structure of replication intermediates. These assays are consistent with replication initiating unidirectionally from the D-loop region by D-loop expansion, as in vertebrates. A prominent site of initiation of lagging-strand synthesis lies at, or near to, the boundary between the genes for ATPase 6 and COIII, which is also close to a pause site for leading-strand synthesis. These findings suggest a role for pause sites in the regulation of mitochondrial transcription and …

DNA ReplicationMitochondrial DNAMacromolecular SubstancesRestriction MappingEukaryotic DNA replicationBiologyOrigin of replicationPre-replication complexDNA MitochondrialDNA RibosomalGeneral Biochemistry Genetics and Molecular BiologyElectron Transport Complex IVRNA TransferControl of chromosome duplicationAnimalsElectrophoresis Gel Two-DimensionalGeneral Environmental ScienceElectrophoresis Agar GelGeneral Immunology and MicrobiologyTer proteinChromosome MappingNADH DehydrogenaseGeneral MedicineMolecular biologyCell biologyRNA RibosomalSea UrchinsNucleic Acid ConformationOrigin recognition complexSolution hybridizationGeneral Agricultural and Biological SciencesProceedings of the Royal Society of London. Series B: Biological Sciences
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Chromatin remodeling regulation by small molecules and metabolites.

2010

The eukaryotic genome is a highly organized nucleoprotein structure comprising of DNA, histones, non-histone proteins, and RNAs, referred to as chromatin. The chromatin exists as a dynamic entity, shuttling between the open and closed forms at specific nuclear regions and loci based on the requirement of the cell. This dynamicity is essential for the various DNA-templated phenomena like transcription, replication, and repair and is achieved through the activity of ATP-dependent chromatin remodeling complexes and covalent modifiers of chromatin. A growing body of data indicates that chromatin enzymatic activities are finely and specifically regulated by a variety of small molecules derived f…

DNA ReplicationS-AdenosylmethionineTranscription GeneticInositol PhosphatesBiophysicsBiochemistryChromatin remodelingchemistry.chemical_compoundAdenosine TriphosphateStructural BiologyAcetyl Coenzyme AGeneticsAnimalsHumansMolecular Biologychromatin small moleculesbiologyGenome HumanDNA replicationDNAChromatin Assembly and DisassemblyNADMi-2/NuRD complexChromatinNucleoproteinChromatinHistoneBiochemistrychemistrybiology.proteinNAD+ kinaseDNABiochimica et biophysica acta
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Multiple roles for ISWI in transcription, chromosome organization and DNA replication.

2003

ISWI functions as the ATPase subunit of multiple chromatin-remodeling complexes. These complexes use the energy of ATP hydrolysis to slide nucleosomes and increase chromatin fluidity, thereby modulating the access of transcription factors and other regulatory proteins to DNA. Here we discuss recent progress toward understanding the biological functions of ISWI, with an emphasis on its roles in transcription, chromosome organization and DNA replication.

DNA ReplicationTranscriptional ActivationHMG-boxTranscription GeneticBiophysicsBiologyBiochemistryATP-dependent chromatin remodeling ISWI Transcription Replication Chromosome structureChromatin remodelingChromosomesAdenosine TriphosphateControl of chromosome duplicationStructural BiologyGeneticsNucleosomeAnimalsHumansTranscription factorGeneticsAdenosine TriphosphatasesDNA replicationChromatin Assembly and DisassemblyChromatinSettore BIO/18 - GeneticaGene Expression RegulationOrigin recognition complexTranscription FactorsBiochimica et biophysica acta
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THE INTERACTION OF NATIVE DNA WITH Ni(II), Cu(II) and Zn(II) COMPLEXES OF 5-TRIETHYL AMMONIUM METHYL SALICYLIDENE ORTHO-PHENYLENDIIMINE

2009

DNA binding Metal complexes Intercalators
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NLRP3 controls ATM activation in response to DNA damage

2020

The DNA damage response (DDR) is essential to preserve genomic integrity and acts as a barrier to cancer. The ATM pathway orchestrates the cellular response to DNA double strand breaks (DSBs), and its attenuation is frequent during tumorigenesis. Here, we show that NLRP3, a Pattern Recognition Receptor known for its role in the inflammasome complex formation, interacts with the ATM kinase to control the early phase of DDR, independently of its inflammasome activity. NLRP3 down-regulation in human bronchial epithelial cells impairs ATM pathway activation as shown by an altered ATM substrate phosphorylation profile, and due to impaired p53 activation, confers resistance to acute genomic stres…

DNA damage[SDV]Life Sciences [q-bio]medicine.disease_cause03 medical and health sciencesSubstrate-level phosphorylationchemistry.chemical_compound0302 clinical medicineDNA Damage Signalingmedicine[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular Biology[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology030304 developmental biologyCancer0303 health sciencesInnate immune systemintegumentary systemChemistryNLRP3 receptorPattern recognition receptorInflammasome3. Good healthCell biology[SDV] Life Sciences [q-bio]030220 oncology & carcinogenesisCarcinogenesisInflammasome complexDNAmedicine.drug
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Mutations in CTC1, encoding conserved telomere maintenance component 1, cause Coats plus

2012

Coats plus is a highly pleiotropic disorder particularly affecting the eye, brain, bone and gastrointestinal tract. Here, we show that Coats plus results from mutations in CTC1, encoding conserved telomere maintenance component 1, a member of the mammalian homolog of the yeast heterotrimeric CST telomeric capping complex. Consistent with the observation of shortened telomeres in an Arabidopsis CTC1 mutant and the phenotypic overlap of Coats plus with the telomeric maintenance disorders comprising dyskeratosis congenita, we observed shortened telomeres in three individuals with Coats plus and an increase in spontaneous γ 3H2AX-positive cells in cell lines derived from two affected individual…

DNA polymeraseMolecular Sequence DataTelomere-Binding ProteinsHistones/metabolismHDE GENHDE NEU PEDCST complexCEREBRORETINAL MICROANGIOPATHY FAMILIAL SYNDROME CALCIFICATIONS CYSTS PROTEIN DNA LEUKOENCEPHALOPATHY EVOLUTION DEFECTSHistoneschemistry.chemical_compoundAbnormalities Multiple/geneticsGeneticsmedicineAbnormalities MultipleGenetic Predisposition to DiseaseGeneticsTelomere-binding proteinTelomere/pathologyddc:618biologyBase SequenceGenetic Predisposition to Disease/geneticsDNA replicationSequence Analysis DNATelomeremedicine.diseaseFlow CytometryTelomereCell biologyRetinal Telangiectasis/genetics/pathologychemistrySequence Analysis DNA/methodsbiology.proteinRetinal TelangiectasisPrimaseTelomere-Binding Proteins/geneticsDNADyskeratosis congenitaNature Genetics
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Purification of Leuconostoc mesenteroides citrate lyase and cloning and characterization of the citCDEFG gene cluster

1998

ABSTRACT A citrate lyase (EC 4.1.3.6 ) was purified 25-fold from Leuconostoc mesenteroides and was shown to contain three subunits. The first 42 amino acids of the β subunit were identified, as well as an internal peptide sequence spanning some 20 amino acids into the α subunit. Using degenerated primers from these sequences, we amplified a 1.2-kb DNA fragment by PCR from Leuconostoc mesenteroides subsp. cremoris . This fragment was used as a probe for screening a Leuconostoc genomic bank to identify the structural genes. The 2.7-kb gene cluster encoding citrate lyase of L. mesenteroides is organized in three open reading frames, citD , citE , and citF , encoding, respectively, the three ci…

DNA BacterialATP citrate lyaseMolecular Sequence DataGene ExpressionBiologymedicine.disease_causeMicrobiologyBacterial ProteinsCarbon-Sulfur LigasesMultienzyme ComplexesGene clusterAcyl Carrier ProteinEscherichia colimedicineLeuconostocAmino Acid SequenceCloning MolecularMolecular BiologyEscherichia coliBase SequenceSequence Homology Amino AcidStructural geneOxo-Acid-LyasesSequence Analysis DNALyasebiology.organism_classificationEnzymes and ProteinsMolecular biologyOxaloacetate decarboxylaseBiochemistryGenes BacterialLeuconostoc mesenteroidesMultigene FamilyCoenzyme A-TransferasesLeuconostoc
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