Search results for "Complementary"

showing 10 items of 1156 documents

Cytotoxic Acacic Acid Glycosides from the Roots of Albizia coriaria

2009

Two new oleanane-type saponins, coriariosides A (1) and B (2), along with a known saponin, gummiferaoside C (3), were isolated from the roots of Albizia coriaria. Their structures were established by extensive analysis of 1D and 2D NMR experiments (COSY, ROESY, TOCSY, HSQC, and HMBC) and mass spectrometry. Compounds 1 and 3 when tested for cytotoxicity against two colorectal human cancer cells showed activity against the HCT 116 (IC50 4.2 microM for 1 and 2.7 microM for 3) and HT-29 (IC50 6.7 microM for 1 and 7.9 microM for 3) cell lines.

SaponinPharmaceutical ScienceAlbizziaPharmacognosyPlant RootsAnalytical ChemistryTriterpeneCoriariaDrug DiscoveryBotanyHumansCameroonOleanolic AcidMedicinal plantsNuclear Magnetic Resonance BiomolecularPharmacologychemistry.chemical_classificationPlants MedicinalMolecular StructurebiologyOrganic ChemistryGlycosideSaponinsHCT116 Cellsbiology.organism_classificationAlbiziaAntineoplastic Agents PhytogenicTriterpenesTerpenoidComplementary and alternative medicinechemistryMolecular MedicineDrug Screening Assays AntitumorHT29 CellsJournal of Natural Products
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Arboreasides A−E, Triterpene Saponins from the Bark of Cussonia arborea

2009

Five new triterpene saponins, arboreasides A-E (1-5), and two known saponins, ciwujianoside C(3) and 23-hydroxyursolic acid 28-O-alpha-L-rhamnopyranosyl-(1--4)-beta-D-glucopyranosyl-(1--6)-beta-D-glucopyranosyl ester, were isolated from the bark of Cussonia arborea. The structures were established using extensive 1D and 2D NMR spectroscopic analyses and mass spectrometry.

SaponinPharmaceutical SciencePharmacognosyAnalytical ChemistryTriterpeneDrug DiscoveryBotanyCameroonAraliaceaeNuclear Magnetic Resonance BiomolecularPharmacologychemistry.chemical_classificationMolecular StructurebiologyOrganic ChemistryGlycosideSaponinsbiology.organism_classificationTriterpenesTerpenoidComplementary and alternative medicinechemistryvisual_artPlant Barkvisual_art.visual_art_mediumMolecular MedicineAraliaceaeBarkCussonia arboreaJournal of Natural Products
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New Acylated Triterpene Saponins from Silene fortunei that Modulate Lymphocyte Proliferation

2002

Three new acylated triterpene saponins 1-3, with a quillaic acid as aglycon, were isolated from the roots of Silene fortunei together with a known phytoecdysteroid (20-hydroxyecdysone). The compounds were characterized mainly by a combination of 2D NMR techniques, mass spectrometry, and chemical methods. Saponins 1-3, jenisseensosides C and D (4, 5), and 6 (deacylated form of 2/3 and 4/5) were found to stimulate the proliferation of the Jurkat tumor cell lines at low concentration. At high concentration, 2/3 and 4/5 inhibited the proliferation of the cells and suggested the induction of apoptosis.

SaponinPhytoecdysteroidPharmaceutical ScienceApoptosisLymphocyte proliferationPharmacognosyLymphocyte ActivationPlant RootsJurkat cellsAnalytical ChemistryJurkat CellsTriterpeneDrug DiscoveryHumansSileneNuclear Magnetic Resonance BiomolecularPharmacologychemistry.chemical_classificationSilenePlants MedicinalMolecular StructurebiologyHydrolysisOrganic ChemistryGlycosideAcetylationStereoisomerismSaponinsbiology.organism_classificationTriterpenesComplementary and alternative medicinechemistryBiochemistryMolecular MedicineJournal of Natural Products
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The role of the silicatein-alpha interactor silintaphin-1 in biomimetic biomineralization.

2008

Biosilicification in sponges is initiated by formation of proteinaceous filaments, predominantly consisting of silicateins. Silicateins enzymatically catalyze condensation of silica nanospheres, resulting in symmetric skeletal elements (spicules). In order to create tailored biosilica structures in biomimetic approaches it is mandatory to elucidate proteins that are fundamental for the assembly of filaments. Silintaphin-1 is a core component of modularized filaments and also part of a spicule-enfolding layer. It bears no resemblance to other proteins, except for the presence of an interaction domain that is fundamental for its function as scaffold/template. In the presence of silicatein sil…

ScaffoldMaterials scienceDNA ComplementaryMolecular Sequence DataSilicic AcidBiophysicsNanoparticleBioengineeringNanotechnologyPlasma protein bindingFerric CompoundsAntibodiesBiomaterialsSponge spiculeCalcification PhysiologicBiomimetic MaterialsTwo-Hybrid System TechniquesAnimalsRegenerationInteractorAmino Acid SequencebiologyCore componentProteinsbiology.organism_classificationEnzymes ImmobilizedCathepsinsRecombinant ProteinsProtein TransportMechanics of MaterialsCeramics and CompositesSuberitesSuberitesBiomineralizationProtein BindingBiomaterials
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The nucleotide and partial amino acid sequences of rat fetuin. Identity with the natural tyrosine kinase inhibitor of the rat insulin receptor.

1992

Fetuins are among the major plasma proteins, yet their biological role has remained elusive. Here we report the molecular cloning of rat fetuin and the sequence analysis of a full-length clone, RF619 of 1456 bp with an open reading frame of 1056 bp encoding 352 amino acid residues. The coding part of RF619 was identical with the cDNA sequence of the natural inhibitor of the insulin receptor tyrosine kinase from rat (pp63) except for four substitutions and a single base insertion causing divergence of the predicted protein sequences. Partial amino acid sequences of rat plasma fetuin were in agreement with the predictions based on the RF619 cDNA. Purified rat fetuin inhibited the insulin rece…

Sequence analysisMolecular Sequence DataBiochemistryTropomyosin receptor kinase CReceptor tyrosine kinaseSubstrate SpecificityComplementary DNASequence Homology Nucleic AcidAnimalsAmino Acid SequencePhosphorylationchemistry.chemical_classificationbiologyBase SequenceDNAProtein-Tyrosine KinasesFetuinMolecular biologyReceptor InsulinAmino acidRatsInsulin receptorBiochemistrychemistryROR1biology.proteinalpha-FetoproteinsEuropean journal of biochemistry
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Isolation, sequence analysis and characterization of cDNA clones coding for the C chain of mouse C1q. Sequence similarity of complement subcomponent …

1992

A mouse macrophage lambda gt11 cDNA library was screened using a genomic DNA clone coding for the C-chain gene of human C1q. Approximately 600,000 recombinant phage plaques were hybridized with peroxidase-labeled human C-chain probe and detected by enhanced chemiluminescence. Five positive clones were obtained. The size of the full-length cDNA is 1019 bp. The sequence identity of the nucleotide sequence with human C1q C chain is 79%, the identity of the deduced amino acid sequences is 73%. The mouse C1q C chain exhibits the same structural features as the human C chain, e.g. conservation of the cysteine residues. Like the mouse A chain, the mouse C chain has an RGD sequence that may be reco…

Sequence analysisMolecular Sequence DataNerve Tissue ProteinsSequence alignmentBiologyBiochemistrylaw.inventionMicelawComplementary DNAAnimalsHumansTissue DistributionAmino Acid SequenceRNA MessengerProtein PrecursorsGeneComplement C1qConserved SequenceBase SequenceSequence Homology Amino AcidcDNA libraryComplement C1qMacrophagesNucleic acid sequenceNucleic Acid HybridizationDNABlotting NorthernMolecular biologyRecombinant DNACollagenEuropean Journal of Biochemistry
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The microsomal epoxide hydrolase has a single membrane signal anchor sequence which is dispensable for the catalytic activity of this protein

1994

The microsomal epoxide hydrolase (mEH) catalyses the hydrolysis of reactive epoxides which are formed by the action of cytochromes P-450 from xenobiotics. In addition it has been suggested that mEH might mediate the transport of bile acids. For the mEH it has been shown that it is co-translationally inserted into the endoplasmic reticulum. Here we demonstrate that the N-terminal 20 amino acid residues of this protein serve as its single membrane anchor signal sequence and that the function of this sequence can also be supplied by a cytochrome P-450 (CYP2B1) anchor signal sequence. The evidence supporting this conclusion is as follows: (i) the rat mEH and a CYP2B1-mEH fusion protein, in whic…

Signal peptideDNA ComplementaryCytochromeMolecular Sequence DataProtein Sorting SignalsBiochemistryCatalysisDogsMicrosomesAnimalsAmino Acid SequenceEpoxide hydrolasePancreasMolecular BiologyEpoxide HydrolasesBase SequenceCell-Free SystembiologyChemistryEndoplasmic reticulumCell MembraneTemplates GeneticCell BiologyFusion proteinRatsMembraneBiochemistryProtein BiosynthesisMicrosomal epoxide hydrolaseMicrosomebiology.proteinResearch ArticleBiochemical Journal
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dfh is a Drosophila homolog of the Friedreich's ataxia disease gene

2000

Abstract A putative Drosophila homolog of the Friedreich's ataxia disease gene (FRDA) has been cloned and characterized; it has been named Drosophila frataxin homolog (dfh). It is located at 8C/D position on X chromosome and is spread over 1 kb, a much smaller genomic region than the human gene. Its genomic organization is simple, with a single intron dividing the coding region into two exons. The predicted encoded product has 190 amino acids, being considered a frataxin-like protein on the basis of the sequence and secondary structure conservation when compared with human frataxin and related proteins from other eukaryotes. The closest match between the Drosophila and the human proteins in…

Signal peptideDNA ComplementaryEmbryo NonmammalianMolecular Sequence DataMutantEmbryonic DevelopmentGenes InsectExonIron-Binding ProteinsGeneticsAnimalsDrosophila ProteinsCoding regionAmino Acid SequenceRNA MessengerCloning MolecularGeneIn Situ HybridizationGenomic organizationGeneticsSequence Homology Amino AcidbiologyIntronGene Expression Regulation DevelopmentalDNAExonsSequence Analysis DNAGeneral MedicineBlotting NorthernIntronsPhosphotransferases (Alcohol Group Acceptor)Drosophila melanogasterFriedreich AtaxiaFrataxinbiology.proteinDrosophilaSequence AlignmentGene
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Sequence of the M28 dsRNA: Preprotoxin Is Processed to an α/β Heterodimeric Protein Toxin

1995

The killer and immunity phenotypes of K28 killer strains of Saccharomyces cerevisiae are determined by the 1.75-kb M28 dsRNA virus. In the plus strand, M28p, the K28 preprotoxin gene, comprises bases 13-1047 and is followed, after an additional 85 bases, by a 63-bp poly(A) sequence and a 553-base 3'-sequence. This 3'-sequence contains two potential stem-loop structures predicted to bind the L-A encoded cap-pol protein, initiating encapsidation; high-level expression results in curing of M1 dsRNA. Expression of M28p confers the complete K28 killer and immunity phenotype on a cell lacking M28 dsRNA. K28 toxin is a disulfide-bonded heterodimer of alpha (10.5 kDa) and beta (11 kDa) components w…

Signal peptideDNA ComplementaryGlycosylationSaccharomyces cerevisiae ProteinsGlycosylationMolecular Sequence DataMutantCarboxypeptidasesSaccharomyces cerevisiaeBiologymedicine.disease_causeCleavage (embryo)Fungal Proteinschemistry.chemical_compoundGene Expression Regulation FungalVirologyEndopeptidasesmedicineSecretionAmino Acid SequenceSubtilisinsGeneDNA PrimersRNA Double-StrandedBase SequenceToxinSerine EndopeptidasesMembrane ProteinsRNA FungalMycotoxinsMolecular biologyKiller Factors YeastRNA silencingchemistryProprotein ConvertasesProtein Processing Post-TranslationalVirology
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Structure, organization and expression of two clustered cuticle protein genes during the metamorphosis of an insect, Tenebrio molitor.

1998

A 4-kb DNA segment of Tenebrio molitor (Insecta, Coleoptera) genomic DNA containing two larval-pupal cuticular genes has been cloned and sequenced. These genes, transcribed in opposite directions, are related in DNA sequence and the proteins encoded are very similar. Each of them contains a single intron located inside the sequence encoding the signal peptide, and a conserved sequence at -200 bp from the mRNA start position. These similarities in sequence suggest that these genes have evolved by duplication followed by diversification and that they are members of a family of genes with a common ancestry. They are the first example of clustered genes in Tenebrio molitor.

Signal peptideDNA ComplementaryMolecular Sequence DataGenes InsectBiologyBiochemistryDNA sequencingConserved sequenceEvolution MolecularGene duplicationAnimalsAmino Acid SequenceTenebrioPeptide sequenceGeneIn Situ HybridizationGeneticsBase SequenceSequence Homology Amino AcidfungiIntronMetamorphosis BiologicalGene Expression Regulation DevelopmentalIntronsgenomic DNAMultigene FamilyInsect ProteinsEuropean journal of biochemistry
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