Search results for "3'"

showing 10 items of 589 documents

CCDC 954558: Experimental Crystal Structure Determination

2013

Related Article: Zachary D. Brown , Petra Vasko , Jeremy D. Erickson , James C. Fettinger , Heikki M. Tuononen , and Philip P. Power|2013|J.Am.Chem.Soc.|135|6257|doi:10.1021/ja4003553

(22''44''66''-Hexamethyl-11':3'1''-terphenyl)-((22''44''66''-hexamethyl-11':3'1''-terphenyl-2'-yl)(methyl)carbonoimidoyl)-germanium n-hexane solvateSpace GroupCrystallographyCrystal SystemCrystal StructureCell ParametersExperimental 3D Coordinates
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CCDC 194089: Experimental Crystal Structure Determination

2003

Related Article: M.Poyatos, E.Mas-Marza, J.A.Mata, M.Sanau, E.Peris|2003|Eur.J.Inorg.Chem.||1215|doi:10.1002/ejic.200390157

(33'-(Pyridine-26-diyl)bis(1-n-butylimidazol-2-ylidene)-CC'N)-tribromo-rhodium(i)Space GroupCrystallographyCrystal SystemCrystal StructureCell ParametersExperimental 3D Coordinates
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CCDC 1831534: Experimental Crystal Structure Determination

2018

Related Article: Qiang Liu, Sun Li, Xiang-Yu Chen, Kari Rissanen, Dieter Enders|2018|Org.Lett.|20|3622|doi:10.1021/acs.orglett.8b01400

(4S5S)-5-(35-di-t-butyl-4-hydroxyphenyl)-1'-phenyl-5H-spiro[1-benzoxepine-43'-indole]-22'(1'H3H)-dioneSpace GroupCrystallographyCrystal SystemCrystal StructureCell ParametersExperimental 3D Coordinates
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CCDC 1019229: Experimental Crystal Structure Determination

2015

Related Article: Andreas M. Bünzli, Edwin C. Constable, Catherine E. Housecroft, Alessandro Prescimone, Jennifer A. Zampese, Giulia Longo, Lidón Gil-Escrig, Antonio Pertegás, Enrique Ortí, Henk J. Bolink|2015|Chemical Science|6|2843|doi:10.1039/C4SC03942D

(6-Phenyl-22'-bipyridine)-bis(5'-(pyridin-2-yl)-11':3'1''-terphenyl-4'-yl)-iridium hexafluorophosphate toluene solvateSpace GroupCrystallographyCrystal SystemCrystal StructureCell ParametersExperimental 3D Coordinates
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CCDC 696570: Experimental Crystal Structure Determination

2008

Related Article: A.Saez, C.Ramirez de Arellano, N.El Aouad, S.Rodriguez, F.Otalvaro, D.Cortes, J.Saez|2008|Acta Crystallogr.,Sect.E:Struct.Rep.Online|64|o1305|doi:10.1107/S1600536808018266

(E)-23'45-tetramethoxystilbeneSpace GroupCrystallographyCrystal SystemCrystal StructureCell ParametersExperimental 3D Coordinates
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CCDC 250842: Experimental Crystal Structure Determination

2005

Related Article: J.-C.Hierso, A.Fihri, V.V.Ivanov, B.Hanquet, N.Pirio, B.Donnadieu, B.Rebiere, R.Amardeil, P.Meunier|2004|J.Am.Chem.Soc.|126|11077|doi:10.1021/ja048907a

(mu~2~-11'-Di-t-butyl-33'44'-tetrakis(diphenylphosphino)ferrocene-PP'P''P''')-bis(dichloro-nickel) dichloromethane solvateSpace GroupCrystallographyCrystal SystemCrystal StructureCell ParametersExperimental 3D Coordinates
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Colorimetic biosensing dispositive based on reagentless hybrid biocomposite: Application to hydrogen peroxide determination

2016

Abstract An efficient approach to enhance the performance of colorimetric biosensors has been developed. The biosensor is based on the co-immobilization of the reagent 3,3′,5,5′-teramethylbencidine (TMB) and the enzyme horseradish peroxidase (HRP) in a PDMS-TEOS-SiO2NPs support. The HRP, in presence of H2O2, catalyzes the oxidation of TMB, producing a blue color. The generated biosensor, doped with the substrate (TMB) and the enzyme (HRP) (entrapped or adsorbed), has been used to determine H2O2 in real samples. Firstly, the immobilization of TMB and HRP in the composite has been studied in order to find the best suitable configuration. The kinetic parameters Vmax (maximum reaction rate) and…

02 engineering and technology010402 general chemistry01 natural sciencesHorseradish peroxidasechemistry.chemical_compoundAdsorptionMaterials ChemistryElectrical and Electronic EngineeringHydrogen peroxideInstrumentationDetection limitChromatographybiologytechnology industry and agricultureMetals and AlloysSubstrate (chemistry)33'55'-Tetramethylbenzidine021001 nanoscience & nanotechnologyCondensed Matter Physics0104 chemical sciencesSurfaces Coatings and FilmsElectronic Optical and Magnetic MaterialschemistryReagentbiology.protein0210 nano-technologyBiosensorSensors and Actuators B: Chemical
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Large-scale identification of functional microRNA targeting reveals cooperative regulation of the hemostatic system.

2018

Essentials MicroRNAs (miRNAs) regulate the molecular networks controlling biological functions such as hemostasis. We utilized novel methods to analyze miRNA-mediated regulation of the hemostatic system. 52 specific miRNA interactions with 11 key hemostatic associated genes were identified. Functionality and drugability of miRNA-19b-3p against antithrombin were demonstrated in vivo. SUMMARY: Background microRNAs (miRNAs) confer robustness to complex molecular networks regulating biological functions. However, despite the involvement of miRNAs in almost all biological processes, and the importance of the hemostatic system for a multitude of actions in and beyond blood coagulation, the role o…

0301 basic medicineComputational biologyBiologyAntithrombinsHemostatics03 medical and health sciencesMiceCell Line TumormicroRNAGene silencingAnimalsHumansGene SilencingBiomarker discoveryGene3' Untranslated RegionsHemostasisThree prime untranslated regionRNARobustness (evolution)Computational BiologyHigh-Throughput Nucleotide SequencingThrombosisHematologyMice Inbred C57BLMicroRNAs030104 developmental biologyHemostasisBiomarkersPlasmidsJournal of thrombosis and haemostasis : JTH
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5' and 3' RACE Method to Obtain Full-Length 5' and 3' Ends of Ciona robusta Macrophage Migration Inhibitory Factors Mif1 and Mif2 cDNA

2019

The 5' and 3' RACE is a method to obtain full-length 5' and 3' ends of cDNA using known cDNA sequences from expressed sequence tags (ESTs), subtracted cDNA, differential display, or library screening. Here is described the identification of full-length 5' and 3' ends of Ciona robusta Mif1 and Mif2 cDNA by using 5' and 3' RACE method.

0301 basic medicineGeneticsExpressed sequence tagCiona robustaDifferential displayBiologyGenome03 medical and health sciencesRace (biology)030104 developmental biology0302 clinical medicine030220 oncology & carcinogenesisComplementary DNA5' and 3' RACE MIF Ciona robustaMacrophage migration inhibitory factor
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miR-128 Is Implicated in Stress Responses by Targeting MAFG in Skeletal Muscle Cells.

2017

MAFG (v-Maf avian musculoaponeurotic fibrosarcoma oncogene homolog G) is a bZIP-type transcriptional regulator that belongs to the small MAF (sMAFs) protein family. By interacting with other bZIP transcription factors, sMAFs can form homo- and heterodimers governing either repressive or activating transcriptional functions. As heterodimeric partner of Nrf2, MAFG positively influences the ARE-dependent antioxidant/xenobiotic pathways, at least in condition of a correct MAFG:Nrf2 balance. MicroRNAs (miRs) participate to different regulatory networks being involved as fine-tuning regulators of gene expression. However, the connections between cellular surveillance to stresses mediated by MAFG:…

0301 basic medicineMafG Transcription FactorMaleAgingProtein familyArticle SubjectNF-E2-Related Factor 2Muscle Fibers SkeletalBiologyTransfectionBiochemistryAntioxidants03 medical and health sciencesMiceGene expressionmicroRNATranscriptional regulationAnimalsHumanslcsh:QH573-671Gene3' Untranslated RegionsGeneticsBinding SitesOncogeneThree prime untranslated regionlcsh:CytologyHEK 293 cellsMembrane ProteinsCell BiologyGeneral MedicineMice Inbred C57BLRepressor ProteinsMicroRNAsOxidative Stress030104 developmental biologyHEK293 CellsHeme Oxygenase-1Research ArticleOxidative medicine and cellular longevity
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