Search results for " Amin"

showing 10 items of 944 documents

Geometrical and conformational preferences of the 9‐fluorenylmethoxycarbonyl‐amino moiety

2004

Structural parameters, originating from x-ray crystallographic data, have been compiled for 13 derivatives of amino acids, peptides and related compounds, which contain a total of 14 Fmoc-NH- moieties. For these moieties, molecular geometries and conformations--described by the omegao, theta1, theta2 and theta3' torsion angles--were analysed and compared with the corresponding parameters for the Z-NH- and Boc-NH-moieties (290 and 553, respectively). To gain a deeper insight into the conformational features of the Fmoc-NH- moiety, ab initio free molecule calculations were performed for fully relaxed minima. Also the potential energy surface as a function of the torsion angles (theta3', theta…

crystal structureStereochemistryAb initioMolecular ConformationCrystal structureCrystallography X-RayBiochemistryBoc amino protectionStructure-Activity RelationshipfluoreneStructural BiologyAb initio quantum chemistry methodsDrug DiscoveryMoleculeMoietyurethane geometryFmoc amino protectionAmino AcidsMolecular BiologyPharmacologyFluorenesMolecular StructureChemistryHydrogen bondab initio calculationsOrganic ChemistryHydrogen BondingGeneral MedicineZ amino protectionMolecular geometryPotential energy surfaceMolecular MedicineCrystallizationPeptidesN‐terminally protected peptidesJournal of Peptide Science
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4-Methyl-N-(4-methylpyridin-2-yl)-N-(3,4,5,6-tetrahydro-2H-pyran-4-yl)pyridin-2-amine

2016

In the title compound, C17H21N3O, the pyridine rings make a dihedral angle of 84.44 (5)°. In the crystal, a C—H...N interaction forms a chain of molecules propagating along the twofold screw axis.

crystal structureTertiary amine010405 organic chemistryChemistrytertiary amineGeneral MedicineCrystal structureDihedral angle010402 general chemistry01 natural sciences0104 chemical sciencesCrystalCrystallographychemistry.chemical_compoundScrew axisPyridinelcsh:QD901-999pyridinaminepalladium-catalysed arylaminationlcsh:CrystallographyIUCrData
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Novel 2,6-disubstituted phenylboronic compounds - Synthesis, crystal structures, solution behaviour and reactivity

2015

Abstract 2,6-Diformylphenylboronic acid has been synthesized and characterized both in the solid state as well as in solution. In crystal, an unusual structural pattern has been found with the formation of intermolecular hydrogen bonds by B(OH) 2 and CHO groups as well as water molecules. In solution tautomeric equilibrium with the formation of oxaborole ring by one of the formyl groups was proved on the basis of multinuclear NMR spectroscopy. The title compound reacts with secondary mono- and diamines to form various types of substituted benzoxaboroles, which have been characterized by XRD and spectroscopic methods.

crystal structureboronic acidsChemistryHydrogen bondOrganic ChemistryCrystal structureNuclear magnetic resonance spectroscopyRing (chemistry)BiochemistryTautomerreductive aminationtautomeric equilibriaInorganic ChemistryCrystalbenzoxaborolesPolymer chemistryMaterials ChemistryMoleculeReactivity (chemistry)Physical and Theoretical ChemistryJournal of Organometallic Chemistry
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Amino acid profile of four varieties of durum wheat grown in Sicily

2015

The major use of durum wheat is for pasta products, particularly in the European and North American countries, whereas in other areas (Middle East and North Africa) also it is used as couscous and for various types of bread. The durum wheat is therefore a staple food in the Mediterranean and is one of the commodities that characterize the dietary pattern of the Mediterranean diet. During the year 2012 were made in Ciminna (Palermo) in Sicily, four fields of experimental cultivation using four different varieties of durum wheat cultivated in Sicily: Simeto, Iride, Duilio and Saragolla. For each variety were set up two different kinds of cultivation tecniques, in order to verify the influence…

durum wheat Amino acid profile nutritionSettore BIO/09 - Fisiologia
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The endopolygalacturonase 1 from botrytis cinerea activates grapevine defense reactions unrelated to its enzyumatic activity

2003

A purified glycoprotein from Botrytis cinerea(strain T4), identified as endopolygalacturonase 1 (T4BcPG1) by mass spectrometry analysis, has been shown to activate defense reactions in grapevine (Vitis vinifera cv. Gamay). These reactions include calcium influx, production of active oxygen species, activation of two mitogen-activated protein kinases, defense gene transcript accumulation, and phytoalexin production. Most of these defense reactions were also activated in grapevine in response to purified oligogalacturonides (OGA) with a degree of polymerization of 9 to 20. In vivo, these active OGA might be a part of the released products resulting from endopolygalacturonase activity on plan…

elicitor; endopolygalacturonase 1; Botrytis cinerea; plant defenceplant defencePhysiologyMolecular Sequence DataOligosaccharidesBiologyCell wallBotrytis cinereaGene Expression Regulation PlantSequence Homology Nucleic Acid[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular Biology[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyVitisAmino Acid SequencePectinaseendopolygalacturonase 1ComputingMilieux_MISCELLANEOUSBotrytis cinereachemistry.chemical_classificationelicitorBase SequenceSequence Homology Amino AcidKinasePhytoalexinfood and beveragesGeneral MedicineHydrogen Peroxidebiology.organism_classificationImmunity InnateElicitorEnzyme ActivationEnzymePolygalacturonasechemistryBiochemistryCalciumBotrytisMitogen-Activated Protein KinasesGlycoproteinAgronomy and Crop Science
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Stereoselective Synthesis and Pharmacological Evaluation of 2,4-Bridged Piperidine Derivatives Designed to Activate the κ-Opioid Receptor

2021

endo-configurationdiastereoselective reductive aminationenantiomeric excessstructure-affinity relationshipNOESY spectrumKOR agonistconformational restrictionchiral HPLCSettore CHIM/08 - Chimica Farmaceutica2-azabicyclo[3.3.1]octanecis/trans configuration
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Type II keratin cDNAs from the rainbow trout: implications for keratin evolution.

2002

From a teleost fish, the rainbow trout Oncorhynchus mykiss, we have cloned and sequenced cDNAs encoding five different type II keratins. The corresponding protein spots, as separated by 2D-PAGE of trout cytoskeletal preparations, have been identified by peptide mass mapping using MALDI mass spectrometry. Three of the sequenced keratins are expressed in the epidermis (subtype IIe), and two in simple epithelia and mesenchymal cells (subtype IIs). The IIs keratins are both orthologs of human K8. This leaves unsequenced only the trace component S3 of the biochemically established trout keratin catalog. A phylogenetic tree has been constructed from a multiple alignment of the rod domains of the …

endocrine systemCancer Researchanimal structuresDNA ComplementaryMolecular Sequence Datamacromolecular substancesPeptide MappingType II keratinEvolution MolecularMesodermSpecies SpecificityAntibody SpecificityKeratinAnimalsHumansProtein IsoformsAmino Acid SequenceCloning MolecularMolecular BiologyZebrafishPhylogenyZebrafishchemistry.chemical_classificationGeneticsMammalsMultiple sequence alignmentintegumentary systembiologyPhylogenetic treeSequence Homology Amino AcidLampreyAntibodies MonoclonalLampreysEpithelial CellsCell Biologybiology.organism_classificationProtein Structure TertiaryTroutchemistryOrgan SpecificityOncorhynchus mykissSpectrometry Mass Matrix-Assisted Laser Desorption-IonizationSharksKeratinsRainbow troutEpidermisSequence AlignmentDevelopmental BiologyDifferentiation; research in biological diversity
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Identification of a Functional Homolog of the Yeast Copper Homeostasis Gene ATX1 from Arabidopsis1

1998

Abstract A cDNA clone encoding a homolog of the yeast (Saccharomyces cerevisiae) gene Anti-oxidant 1(ATX1) has been identified from Arabidopsis. This gene, referred to as CopperCHaperone(CCH), encodes a protein that is 36% identical to the amino acid sequence of ATX1 and has a 48-amino acid extension at the C-terminal end, which is absent from ATX1 homologs identified in animals. ATX1-deficient yeast (atx1) displayed a loss of high-affinity iron uptake. Expression of CCH in the atx1 strain restored high-affinity iron uptake, demonstrating thatCCH is a functional homolog of ATX1. When overexpressed in yeast lacking the superoxide dismutase geneSOD1, both ATX1 and CCHprotected the cell from t…

endocrine systemDNA ComplementarySaccharomyces cerevisiae ProteinsPhysiologyMolecular Sequence DataSaccharomyces cerevisiaeSOD1ArabidopsisGene ExpressionSaccharomyces cerevisiaePlant ScienceFungal ProteinsGene productSuperoxide dismutaseOzoneCopper Transport ProteinsComplementary DNAArabidopsisGene expressionGeneticsHomeostasisAmino Acid SequenceCation Transport ProteinsBase SequenceSequence Homology Amino AcidbiologyArabidopsis ProteinsGenetic Complementation Testbiology.organism_classificationYeastOxidative StressBiochemistrybiology.proteinCarrier ProteinsCopperResearch ArticlePlant Physiology
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Origin of Insulin Receptor-Like Tyrosine Kinases in Marine Sponges

1999

One autapomorphic character restricted to all Metazoa including Porifera [sponges] is the existence of transmembrane receptor tyrosine kinases (RTKs). In this study we screened for molecules from one subfamily within the superfamily of the insulin receptors. The subfamily includes the insulin receptors (InsR), the insulin-like growth factor I receptors, and the InsR-related receptors--all found in vertebrates--as well as the InsR-homolog from Drosophila melanogaster. cDNAs encoding putative InsRs were isolated from the hexactinellid sponge Aphrocallistes vastus, the demosponge Suberites domuncula, and the calcareous sponge Sycon raphanus. Phylogenetic analyses of the catalytic domains of th…

endocrine systemDNA ComplementarySubfamilyMolecular Sequence DataReceptor tyrosine kinaseEvolution MolecularMiceDemospongeCatalytic DomainBotanyAnimalsHumansAmino Acid SequenceSycon raphanusCloning MolecularPhylogenyCephalochordateBase SequenceSequence Homology Amino Acidbiologygeodia cydonium; adhesion receptors; evolutionnutritional and metabolic diseasesSequence Analysis DNAbiology.organism_classificationReceptor InsulinPoriferaRatsSuberites domunculaInsulin receptorSpongeBiochemistrybiology.proteinGeneral Agricultural and Biological Scienceshormones hormone substitutes and hormone antagonistsThe Biological Bulletin
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Transgenic overexpression of corticotropin releasing hormone provides partial protection against neurodegeneration in an in vivo model of acute excit…

2008

Abstract Corticotropin releasing hormone (CRH) is the central modulator of the mammalian hypothalamic–pituitary–adrenal (HPA) axis. In addition, CRH affects other processes in the brain including learning, memory, and synaptic plasticity. Moreover, CRH has been shown to play a role in nerve cell survival under apoptotic conditions and to serve as an endogenous neuroprotectant in vitro . Employing mice overexpressing murine CRH in the CNS, we observed a differential response of CRH-overexpressing mice (CRH-COE hom -Nes) to acute excitotoxic stress induced by kainate compared with controls (CRH-COE con -Nes). Interestingly, CRH-overexpression reduced the duration of epileptic seizures and pre…

endocrine systemmedicine.medical_specialtyIndolesRNA UntranslatedCorticotropin-Releasing HormoneExcitotoxicityMice TransgenicNerve Tissue ProteinsBiologymedicine.disease_causeNeuroprotectionHippocampusNestinCorticotropin-releasing hormoneMiceIntermediate Filament ProteinsNeurotrophic factorsNeurofilament ProteinsSeizuresInternal medicineGlial Fibrillary Acidic Proteinpolycyclic compoundsmedicineExcitatory Amino Acid AgonistsReaction TimeAnimalsNeuroinflammationBrain-derived neurotrophic factorAnalysis of VarianceKainic AcidCell DeathGeneral NeuroscienceBrain-Derived Neurotrophic FactorNeurodegenerationProteinsLong-term potentiationmedicine.diseaseDisease Models AnimalEndocrinologynervous systemGene Expression RegulationNerve DegenerationNeurotoxicity SyndromesPlant Lectinshormones hormone substitutes and hormone antagonistsNeuroscience
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