Search results for "Sequence analysi"

showing 10 items of 1351 documents

A multifunctional bicupin serves as precursor for a chromosomal protein of Pisum sativum seeds.

2005

The fact that the psp54 gene codes for p16, a seed chromatin protein of Pisum sativum, has been described previously. In the present paper it is shown that p54, the p16 precursor, also exists as a free polypeptide in pea and that it also yields p38, a second polypeptide from the N-terminal region of p54, which is co-localized at a subcellular level with p16. By using antibodies against pea p16 and p38, it was found that these proteins are present in the members of the tribe Viciae examined. Sequence analysis and 3D modelling indicates that p54 proteins belong to the cupin superfamily, and that they are related to sucrose binding proteins and, to a lesser extent, to vicilin-type seed storage…

Models MolecularPhysiologySequence analysisChromosomal Proteins Non-HistoneMolecular Sequence DataPlant ScienceResponse ElementsDNA-binding proteinPisumSativumGene Expression Regulation PlantSequence Analysis ProteinGene expressionStorage proteinAmino Acid SequenceRNA MessengerProtein PrecursorsPromoter Regions GeneticGenePlant Proteinschemistry.chemical_classificationMessenger RNAbiologyPeasfood and beveragesbiology.organism_classificationBiochemistrychemistryMultigene FamilyProtein BiosynthesisSeedsProtein Processing Post-TranslationalSequence AlignmentAbscisic AcidJournal of experimental botany
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Pharmacogenomics of cantharidin in tumor cells.

2014

Cantharis vesicatoria (blister beetle) is used in Chinese medicine and has been categorized as highly toxic in the Chinese pharmacopeia. In Europe, Cantharis patches have been used since ages to treat various skin-related diseases. We investigated the cytotoxicity of the Cantharis ingredient, cantharidin, in 41 tumor cell lines (Oncotest panel) and compared the results with those of 60 cell lines of the National Cancer Institute, USA. We found profound activity at low micromolar concentrations (log ₁₀IC₅₀ values between -6.980 and 5.009 M). Cantharidin bound to protein phosphatase 2A (PP2A) with higher affinity (-8.12 kcal/mol) than to PP1 (-6.25 kcal/mol) in molecular docking analyses. Usi…

Models MolecularProtein ConformationBlister beetleBiologyCantharisBiochemistryFas ligandGene Expression Regulation Enzymologicchemistry.chemical_compoundCell Line TumorGene expressionAnimalsHumansRNA MessengerCytotoxicityOligonucleotide Array Sequence AnalysisPharmacologyCantharidinBinding SitesMolecular Structurebiology.organism_classificationMolecular biologyReceptors Neuropeptide YchemistryCell cultureApoptosisPharmacogeneticsImmunologyCantharidinBiochemical pharmacology
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Cockroach allergens Per a 3 are oligomers

2009

Allergens from cockroaches cause major asthma-related health problems worldwide. Among them Per a 3 belongs to the most potent allergens. Although the sequences of some members of the Per a 3-family are known, their biochemical and biophysical properties have not been investigated. Here we present for the first time a thorough structural characterization of these allergens, which have recently been tested to induce an increase of allergy specific indicators in blood of Europeans. We isolated two Per a 3 isoforms, which occur freely dissolved in the hemolymph as hexamers with molecular masses of 465+/-25kDa (P II) and 512+/-25kDa (P I). Their sedimentation coefficients (S(20,W)) were determi…

Models MolecularSequence analysismedicine.medical_treatmentProtein subunitMolecular Sequence DataImmunologySequence alignmentRandom hexamermedicine.disease_causeMass SpectrometryAllergenmedicineAnimalsPeriplanetaProtein IsoformsAmino Acid SequencePeptide sequenceBase SequencebiologyCircular DichroismHemocyaninSequence Analysis DNAAllergensbiology.organism_classificationMicroscopy ElectronMicroscopy FluorescenceBiochemistryImmunologyInsect ProteinsElectrophoresis Polyacrylamide GelAmerican cockroachSequence AlignmentUltracentrifugationDevelopmental BiologyDevelopmental & Comparative Immunology
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Cloning, tissue distribution, pharmacology and three-dimensional modelling of melanocortin receptors 4 and 5 in rainbow trout suggest close evolution…

2004

The rainbow trout (Oncorhynchus mykiss) is one of the most widely used fish species in aquaculture and physiological research. In the present paper, we report the first cloning, 3D (three-dimensional) modelling, pharmacological characterization and tissue distribution of two melanocortin (MC) receptors in rainbow trout. Phylogenetic analysis indicates that these receptors are orthologues of the human MC4 and MC5 receptors. We created 3D molecular models of these rainbow trout receptors and their human counterparts. These models suggest greater divergence between the two human receptors than between their rainbow trout counterparts. The pharmacological analyses demonstrated that ACTH (adreno…

Models Molecularendocrine systemmedicine.medical_specialtyanimal structuresanimal diseasesMolecular Sequence DataAdrenocorticotropic hormoneBiologyKidneyBinding Competitivedigestive systemBiochemistryCell LineEvolution MolecularInternal medicinemedicineAnimalsHumansAmino Acid SequenceCloning MolecularBinding siteReceptorMolecular BiologyPhylogenyPharmacologyCloningBinding Sitesurogenital systemReceptors MelanocortinSequence Analysis DNACell BiologyCell biologyZincEndocrinologyReceptors CorticotropinOrgan SpecificityHypothalamusHormone receptorOncorhynchus mykissReceptor Melanocortin Type 4Rainbow troutMelanocortinSequence AlignmentResearch ArticleBiochemical Journal
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Subunit organization of the abalone Haliotis tuberculata hemocyanin type 2 (HtH2), and the cDNA sequence encoding its functional units d, e, f, g and…

1999

We have developed a HPLC procedure to isolate the two different hemocyanin types (HtH1 and HtH2) of the European abalone Haliotis tuberculata. On the basis of limited proteolytic cleavage, two-dimensional immunoelectrophoresis, PAGE, N-terminal protein sequencing and cDNA sequencing, we have identified eight different 40-60-kDa functional units (FUs) in HtH2, termed HtH2-a to HtH2-h, and determined their linear arrangement within the elongated 400-kDa subunit. From a Haliotis cDNA library, we have isolated and sequenced a cDNA clone which encodes the five C-terminal FUs d, e, f, g and h of HtH2. As shown by multiple sequence alignments, defg of HtH2 correspond structurally to defg from Octo…

Models Molecularfood.ingredientDNA ComplementarySequence analysismedicine.medical_treatmentMolecular Sequence DataOctopodiformesMegathura crenulataBiochemistryEvolution MolecularfoodSequence Analysis ProteinComplementary DNAmedicineAnimalsHaliotisAmino Acid SequenceCloning MolecularProtein Structure QuaternaryPeptide sequenceImmunoelectrophoresisbiologySequence Homology Amino AcidcDNA libraryHelix SnailsProtein primary structureHemocyaninAnatomySequence Analysis DNAbiology.organism_classificationPeptide FragmentsBiochemistryMolluscaHemocyaninsEuropean journal of biochemistry
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The cold shock response of the psychrotrophic bacterium Pseudomonas fragi involves four low-molecular-mass nucleic acid-binding proteins

1997

The psychrotrophic bacterium Pseudomonas fragi was subjected to cold shocks from 30 or 20 to 5 degrees C. The downshifts were followed by a lag phase before growth resumed at a characteristic 5 degrees C growth rate. The analysis of protein patterns by two-dimentional gel electrophoresis revealed overexpression of 25 or 17 proteins and underexpression of 12 proteins following the 30- or 20-to-5 degrees C shift, respectively. The two downshifts shared similar variations of synthesis of 20 proteins. The kinetic analysis distinguished the induced proteins into cold shock proteins (Csps), which were rapidly but transiently overexpressed, and cold acclimation proteins (Caps), which were more or …

Molecular Sequence DataAdaptation BiologicalBiologyMicrobiologyPolymerase Chain Reaction03 medical and health sciencesHeat acclimationBacterial ProteinsPseudomonas fragiHeat shock proteinNucleic AcidsPseudomonasCold acclimationElectrophoresis Gel Two-DimensionalAmino Acid SequenceCloning MolecularMolecular BiologyPeptide sequence[SDV.MP] Life Sciences [q-bio]/Microbiology and ParasitologyHeat-Shock ProteinsComputingMilieux_MISCELLANEOUS030304 developmental biologyGel electrophoresis0303 health sciencesBase SequenceSequence Homology Amino Acid030306 microbiologySequence Analysis DNACold-shock domainbiology.organism_classificationMolecular biologyCold shock responseCold TemperatureDNA-Binding Proteins[SDV.MP]Life Sciences [q-bio]/Microbiology and ParasitologyBiochemistryGenes BacterialCarrier ProteinsSequence AnalysisGenome BacterialResearch ArticleProtein Binding
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Identification of five novel tectiviruses in Bacillus strains: analysis of a highly variable region generating genetic diversity

2013

Our biosphere is abundant with unique and small genes for which no homologs are known. These genes, often referred to as orphans or ORFans, are commonly found in bacteriophage genomes but their origins remain unclear. We discovered five novel tectivirus-like genetic elements by screening more than five-hundred Bacillus strains. A highly variable region (HVR) of these viruses was shown to harbor ORFans in most of these otherwise well-conserved bacteriophages. Previous studies demonstrated that mutations close to this region dramatically alter bacteriophage gene regulation, suggesting that the acquisition of those ORFans may provide a source of genetic diversity that is then subject to geneti…

Molecular Sequence DataBacillusBacillus PhagesMicrobiologyGenomeBacteriophageMicroscopy Electron TransmissionLysogenic cycleGenetic variationAmino Acid SequenceGenetic variabilityMolecular BiologyGeneGeneticsGenetic diversitybiologyVirionta1182Genetic VariationSequence Analysis DNAGeneral Medicinebiology.organism_classificationBacillus PhageDNA ViralSequence AlignmentTectiviridaeResearch in Microbiology
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A multidomain xylanase from a Bacillus sp. with a region homologous to thermostabilizing domains of thermophilic enzymes

1999

The gene xynC encoding xylanase C from Bacillus sp. BP-23 was cloned and expressed in Escherichia coli. The nucleotide sequence of a 3538 bp DNA fragment containing xynC gene was determined, revealing an open reading frame of 3258 bp that encodes a protein of 120,567 Da. A comparison of the deduced amino acid sequence of xylanase C with known beta-glycanase sequences showed that the encoded enzyme is a modular protein containing three different domains. The central region of the enzyme is the catalytic domain, which shows high homology to family 10 xylanases. A domain homologous to family IX cellulose-binding domains is located in the C-terminal region of xylanase C, whilst the N-terminal r…

Molecular Sequence DataBacillusBiologymedicine.disease_causeMicrobiologyHomology (biology)Substrate Specificitychemistry.chemical_compoundCatalytic DomainEnzyme StabilityEscherichia colimedicineXylobioseAmino Acid SequenceCloning MolecularEscherichia coliPeptide sequencechemistry.chemical_classificationEndo-14-beta XylanasesSequence Homology Amino AcidThermophileTemperatureNucleic acid sequenceSequence Analysis DNAXylosidasesEnzymeBiochemistrychemistryGenes BacterialXylanaseSequence AlignmentMicrobiology
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The nuclear autoantigen La/SS-associated antigen B: One gene, three functional mRNAs

1997

Transcription of the gene encoding for the nuclear autoantigen La resulted in three mRNA forms. A promoter switching combined with an alternative splicing pathway replaced exon 1 with either exon 1´ or exon 1´´. The exon 1´´ donor splice site was located 4 nts downstream of the exon 1´ donor splice site. All three La mRNA forms were expressed in all the tissues analysed including peripheral blood lymphocytes, liver, fetal spleen, cultured primary endothelial cells, and mouse LTA cell lines permanently transfected with the human La gene. Both the exons 1´ and 1´´ had unusual structures. They contained GC-rich regions and an oligo(U)-tail of 23 uridine residues. Moreover, they encoded for thr…

Molecular Sequence DataBiologyAutoantigensPolymerase Chain ReactionBiochemistryMiceExonExon trappingAnimalsHumansAmino Acid SequenceRNA MessengerMolecular BiologyGeneRibonucleoproteinAdenosine TriphosphatasesMessenger RNASplice site mutationBase SequenceAlternative splicingExonsSequence Analysis DNACell BiologyMolecular biologyOpen reading frameGenetic TechniquesRibonucleoproteinsResearch ArticleTranscription Factors
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Isolation and characterisation of an isoproturon-mineralisingMethylopilasp. TES from French agricultural soil

2004

Using enrichment culture three isoproturon (IPU) mineralising bacterial isolates were isolated from a French agricultural soil mineralising up to 50% of the initially added 14C-ring labelled IPU within only eight days. These isolates showed similar metabolic (BIOLOG GN) and amplified rDNA restriction (ARDRA) profiles. Partial 16S rDNA sequencing revealed that they were identical and identified as Methylopila sp TES. This strain harbours a large plasmid (220 kb) putatively bearing essential IPU-degrading genes as demonstrated by a curing experiment. Methylopila sp. TES transformed IPU and its known metabolites to CO2 and biomass but did not degrade chlorotoluron, monolinuron, diuron and linu…

Molecular Sequence DataBiologyDNA RibosomalMicrobiologyEnrichment cultureMicrobiologychemistry.chemical_compoundPlasmidRNA Ribosomal 16SMethylopila sp. TESBotanyGeneticsMolecular BiologySoil MicrobiologyStrain (chemistry)HerbicidesPhenylurea CompoundsAgricultureSequence Analysis DNAMonolinuronBiodegradation16S ribosomal RNAIsolation (microbiology)Bacterial Typing TechniquesCulture MediaBiodegradation EnvironmentalchemistryFranceMethylocystaceaeFEMS Microbiology Letters
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