Search results for "nicotinamide"

showing 10 items of 76 documents

CCDC 1058519: Experimental Crystal Structure Determination

2015

Related Article: Alexandre Abhervé, Mario Palacios-Corella, Juan Modesto Clemente-Juan, Raphael Marx, Petr Neugebauer, Joris van Slageren, Miguel Clemente-León, Eugenio Coronado|2015|J.Mater.Chem.C|3|7936|doi:10.1039/C5TC01089F

Space GroupCrystallographyCrystal Systemtris(tetra-n-butylammonium) bis(mu-N-(13-dioxy-2-(oxymethyl)propan-2-yl)-26-di(1H-pyrazol-1-yl)isonicotinamide)-hexakis(mu-oxo)-dodecaoxo-manganese-hexa-molybdenum NN-dimethylacetamide solvate hydrateCrystal StructureCell ParametersExperimental 3D Coordinates
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Do dynamic effects play a significant role in enzymatic catalysis? A theoretical analysis of formate dehydrogenase.

2010

A theoretical study of the protein dynamic effects on the hydride transfer between the formate anion and nicotinamide adenine dinucleotide (NAD + ), catalyzed by formate dehydrogenase (FDH), is presented in this paper. The analysis of free downhill molecular dynamic trajectories, performed in the enzyme and compared with the reaction in aqueous solution, has allowed the study of the dynamic coupling between the reacting fragments and the protein or the solvent water molecules, as well as an estimation of the dynamic effect contribution to the catalytic effect from calculation of the transmission coefficient in the enzyme and in solution. The obtained transmission coefficients for the enzyme…

StereochemistryFDHNicotinamide adenine dinucleotideFormate dehydrogenaseenzyme catalysisChemical reactionrare-event trajectoriesCatalysisEnzyme catalysischemistry.chemical_compoundMolecular dynamicsReaction rate constantGrote–Hynes theoryComputational chemistryFormatedynamic effectsNuclear Magnetic Resonance BiomolecularAqueous solutionMolecular StructureOrganic ChemistryGeneral ChemistryModels TheoreticalNADFormate Dehydrogenasesmolecular dynamicsKineticschemistryAlgorithmsChemistry (Weinheim an der Bergstrasse, Germany)
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A redox-sensitive nanofluidic diode based on nicotinamide-modified asymmetric nanopores

2017

[EN] We demonstrate a redox-sensitive nanofluidic diode whose ion rectification is modulated by the oxidation and reduction of chemical moieties incorporated on its surface. To achieve this goal, we have first synthesized the chemical compounds 1-(4-aminobutyl)-3-carbamoylpyridin-1-ium (Nic-BuNH2) and 3-carbamoyl-1-(2,4-dinitrophenyl)pyridinium (Nic-DNP). Then, the surface of track-etched single asymmetric nanopores is decorated with the redox-sensitive Nic-BuNH2 and Nic-DNP molecules using carbodiimide coupling chemistry and Zincke reaction, respectively. The success of the modification reactions is monitored through the changes in the current¿voltage (I¿V) curves prior to and after pore f…

Track-etchingReducing agent02 engineering and technology010402 general chemistryPhotochemistry01 natural sciencesRedoxIonchemistry.chemical_compoundMaterials ChemistryMoleculeOrganic chemistryRedox reactionSurface chargeElectrical and Electronic EngineeringNicotinamideInstrumentationCurrent rectificationMetals and Alloys021001 nanoscience & nanotechnologyCondensed Matter Physics0104 chemical sciencesSurfaces Coatings and FilmsElectronic Optical and Magnetic MaterialsNanoporechemistrySurface functionalizationFISICA APLICADASurface modificationPyridiniumSynthetic nanopores0210 nano-technologySensors and Actuators B: Chemical
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Is At Least One Vitamin Helping Our Vasculature?

2014

See related article, pp 1290–1298 Cardiovascular risk factors such as diabetes mellitus, arterial hypertension, chronic smoking, and hypercholesterolemia are cardiovascular risk factors known to be associated with endothelial dysfunction, a condition that may predict long-term progression of atherosclerosis as well as cardiovascular event rates (for review, see Munzel et al1) Although the mechanisms underlying this phenomenon are complex and multifactorial, there is growing body of evidence that oxidative stress attributable to increased production of reactive oxygen–derived free radicals may play a pivotal role in this process.2 Increased superoxide production by enzyme systems such as the…

Vitaminmedicine.medical_specialtybusiness.industryVitamin Emedicine.medical_treatmentmedicine.diseasemedicine.disease_causeCalcitriol receptorchemistry.chemical_compoundB vitaminsEndocrinologychemistryInternal medicineDiabetes mellitusInternal MedicinemedicineEndothelial dysfunctionbusinessNicotinamide adenine dinucleotide phosphateOxidative stressHypertension
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The catalytic mechanism of glyceraldehyde 3-phosphate dehydrogenase from Trypanosoma cruzi elucidated via the QM/MM approach

2013

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) has been identified as a key enzyme involved in glycolysis processes for energy production in the Trypanosoma cruzi parasite. This enzyme catalyses the oxidative phosphorylation of glyceraldehyde 3-phosphate (G3P) in the presence of inorganic phosphate (Pi) and nicotinamide adenosine dinucleotide (NAD+). The catalytic mechanism used by GAPDH has been intensively investigated. However, the individual roles of Pi and the C3 phosphate of G3P (Ps) sites, as well as some residues such as His194 in the catalytic mechanism, remain unclear. In this study, we have employed Molecular Dynamics (MD) simulations within hybrid quantum mechanical/molecular …

biocatalysisEnzims proteolíticsParàsitsStereochemistryTrypanosoma cruziGeneral Physics and AstronomyDehydrogenaseMolecular Dynamics SimulationNicotinamide adenine dinucleotideOxidative PhosphorylationSubstrate Specificityglyceraldehyde 3 phosphate dehydrogenaseQM/MMchemistry.chemical_compoundstomatognathic systemGlyceraldehydePhysical and Theoretical Chemistrynicotinamide adenine dinucleotideGlyceraldehyde 3-phosphate dehydrogenasechemistry.chemical_classificationbiologyGlyceraldehyde-3-Phosphate DehydrogenasesActive siteNADmolecular dynamicsEnzymechemistryBiochemistryBiocatalysisbiology.proteinQuantum TheoryNAD+ kinaseOxidation-ReductionPhysical Chemistry Chemical Physics
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CCDC 667553: Experimental Crystal Structure Determination

2008

Related Article: J.Kavalirova, M.Korabik, P.Stachova, J.Moncol, R.Sillanpaa, T.Lis, D.Miklos, M.Melnik, J.Mrozinski, D.Valigura|2008|Polyhedron|27|1333|doi:10.1016/j.poly.2007.12.030

catena-((mu~2~-NN-Diethylnicotinamide-NO)-tetrakis(mu~2~-2-nitrobenzoato-OO')-di-copper(ii))Space GroupCrystallographyCrystal SystemCrystal StructureCell ParametersExperimental 3D Coordinates
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Abstract 1390: A combination of natural polyphenols, a NAD+ booster, and a Toll-like receptor 2/6 agonist exerts high radioprotection in normal tissu…

2021

Abstract Ionizing radiation damages cells via direct ionization of DNA and other cellular targets as well as by indirect effects through reactive oxygen species. The response to radiation exposure depends on the cell type and dose of radiation, inherent tissue sensitivity and repair, and modulating intracellular factors that include cell cycle status, O2 pressure, and levels of thiols and other antioxidants. Potentially protective agents against exposure to harmful radiation have been investigated for decades. However, no ideal radioprotector is currently available. A wide range of phytochemicals are antioxidants and, thus, potentially radioprotective. Topical administration of Pterostilben…

chemistry.chemical_classificationAgonistCancer ResearchReactive oxygen speciesPterostilbeneNicotinamidemedicine.drug_classSilibininPharmacologychemistry.chemical_compoundOncologychemistryIn vivoNicotinamide ribosidemedicineNAD+ kinaseCancer Research
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Protochlorophyllide Reduction: Mechanisms and Evolution¶

2007

Protochlorophyllide (Pchlide) reductases are key enzymes in the process of chlorophyll biosynthesis. In this review, current knowledge on the molecular organization, substrate specificity and assembly of the light-dependent reduced nicotinamide adenine dinucleotide phosphate:Pchlide oxidoreductases are discussed. Characteristics of light-independent enzymes are also described briefly, and the possible reasons for the selection of light-dependent enzymes during the course of evolution are discussed.

chemistry.chemical_classificationEnzymeReduced nicotinamide-adenine dinucleotideProtochlorophyllideBiochemistrychemistrySubstrate specificityGeneral MedicinePhysical and Theoretical ChemistryChlorophyll biosynthesisBiologyBiochemistryPhotochemistry and Photobiology
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A p300 and SIRT1 Regulated Acetylation Switch of C/EBPP Controls Mitochondrial Function

2018

Cellular metabolism is a tightly controlled process in which the cell adapts fluxes through metabolic pathways in response to changes in nutrient supply. Among the transcription factors that regulate gene expression and thereby cause changes in cellular metabolism is the basic leucine-zipper (bZIP) transcription factor CCAAT/enhancer-binding protein alpha (C/EBPα). Protein lysine acetylation is a key post-translational modification (PTM) that integrates cellular metabolic cues with other physiological processes. Here we show that C/EBPα is acetylated by the lysine acetyl transferase (KAT) p300 and deacetylated by the lysine deacetylase (KDAC) Sirtuin1 (SIRT1). SIRT1 is activated in times of…

chemistry.chemical_compoundMitochondrial biogenesischemistryTranscription (biology)AcetylationGene expressionLysineNAD+ kinaseNicotinamide adenine dinucleotideTranscription factorCell biologySSRN Electronic Journal
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Assessment of Intake of Nicotinic Acid and Nicotinamide in Relation to Tolerable Upper Intake Levels

2018

chemistry.chemical_compoundNicotinic agonistNicotinamidechemistryFood supplementbusiness.industryDietary Reference IntakePhysiologyMedicinebusinessRisk assessmentNiacinEuropean Journal of Nutrition & Food Safety
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