Search results for "Sequence alignment"

showing 10 items of 447 documents

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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Current bioinformatics tools in genomic biomedical research (Review).

2006

On the advent of a completely assembled human genome, modern biology and molecular medicine stepped into an era of increasingly rich sequence database information and high-throughput genomic analysis. However, as sequence entries in the major genomic databases currently rise exponentially, the gap between available, deposited sequence data and analysis by means of conventional molecular biology is rapidly widening, making new approaches of high-throughput genomic analysis necessary. At present, the only effective way to keep abreast of the dramatic increase in sequence and related information is to apply biocomputational approaches. Thus, over recent years, the field of bioinformatics has r…

Sequence databaseGenome HumanGene predictionGene Expression ProfilingComputational BiologyGenomicsSequence alignmentGeneral MedicineGenomicsOncogenomicsBiologyBioinformaticsGenomePolymorphism Single NucleotideComputingMethodologies_PATTERNRECOGNITIONDatabases GeneticHuman Genome ProjectGeneticsHumansHuman genomePromoter Regions GeneticSequence AlignmentSoftwareSequence (medicine)International journal of molecular medicine
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A comparative analysis of the products of GROEL-1 gene fromChlamydia trachomatisserovar D and the HSP60 var1 transcript fromHomo sapienssuggests a po…

2009

Summary Chlamydia trachomatis serovar D produces large quantities of HSP60-1 during infections, which accumulate inside the host cell inducing autoimmunity. We compare the aminoacid sequences of the human HSP60 with the bacterial counterpart to better elucidate how CTHSP60 may simulate HSP60 from human origin during infection and may induce an autoimmune response. As a result of the comparison we suggest several possible epitopes of the CTHSP60, which may induce autoimmunity.

Serotypeanimal structuresTranscription GeneticMolecular Sequence DataImmunologyAutoimmunityChlamydia trachomatischemical and pharmacologic phenomenaBiologymedicine.disease_causecomplex mixturesEpitopeAutoimmunityGeneticsmedicineHumansAmino Acid SequenceMolecular BiologyGeneGenetics (clinical)GeneticsBase SequencefungiChaperonin 60General MedicineChlamydia InfectionsHsp60 Chlamydia trachomatisGroELHomo sapiensHSP60Chlamydia trachomatisSequence AlignmentInternational Journal of Immunogenetics
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Evolution and functional differentiation of recently diverged phytochelatin synthase genes from Arundo donax L.

2019

Plant phytochelatin synthases undergo evolutionarily rapid functional differentiation after duplication, allowing fast and precise adjustment of metal detoxification capacity by modulation of both transcription and enzymatic activity.

Settore BIO/01 - BOTANICA GENERALE0106 biological sciences0301 basic medicineGene duplicationPhysiologyArabidopsisSaccharomyces cerevisiaePlant SciencePoaceae01 natural sciencesGenomeDivergenceEvolution Molecular03 medical and health sciencesGene Expression Regulation Plantcadmium; divergence; gene duplication; giant reed; phytochelatin synthase; phytochelatins; subfunctionalizationSubfunctionalizationPhytochelatinsArabidopsis thalianaAmino Acid SequenceGenePhylogenyPlant ProteinsGeneticsNatural selectionGiant reedbiologyArundo donaxAminoacyltransferasesPlants Genetically Modifiedbiology.organism_classificationResearch PapersPhenotype030104 developmental biologyPlant—Environment InteractionsSubfunctionalizationPhytochelatinMicroorganisms Genetically-ModifiedPhytochelatin synthaseSequence AlignmentCadmium010606 plant biology & botanyJournal of Experimental Botany
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Epidemiological dynamics of norovirus GII.4 variant New Orleans 2009.

2015

Norovirus (NoV) is one of the major causes of diarrhoeal disease with epidemic, outbreak and sporadic patterns in humans of all ages worldwide. NoVs of genotype GII.4 cause nearly 80–90 % of all NoV infections in humans. Periodically, some GII.4 strains become predominant, generating major pandemic variants. Retrospective analysis of the GII.4 NoV strains detected in Italy between 2007 and 2013 indicated that the pandemic variant New Orleans 2009 emerged in Italy in the late 2009, became predominant in 2010–2011 and continued to circulate in a sporadic fashion until April 2013. Upon phylogenetic analysis based on the small diagnostic regions A and C, the late New Orleans 2009 NoVs circulati…

Settore MED/07 - Microbiologia E Microbiologia ClinicaGenotypeMolecular Sequence DataBiologymedicine.disease_causeGenomeFecesOpen Reading FramesPhylogeneticsVirologyPandemicGenotypemedicineHumansAmino Acid SequencePhylogenyCaliciviridae InfectionsRetrospective StudiesGeneticsnorovirus GII.4 variant New Orleans 2009 epidemiologyPhylogenetic treeNorovirusOutbreakNew OrleansVirologyGastroenteritisCaliciviridae InfectionsItalyNorovirusCapsid ProteinsSequence AlignmentThe Journal of general virology
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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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Diplopod hemocyanin sequence and the phylogenetic position of the Myriapoda

2001

Hemocyanins are copper-containing respiratory proteins of the Arthropoda that have so far been thoroughly investigated only in the Chelicerata and the Crustacea but have remained unstudied until now in the Myriapoda. Here we report the first sequence of a myriapod hemocyanin. The hemocyanin of Spirostreptus sp. (Diplopoda: Spirostreptidae) is composed of two distinct subunits that are arranged in a 6 x 6 native molecule. The cloned hemocyanin subunit cDNA codes of for a polypeptide of 653 amino acids (75.5 kDa) that includes a signal peptide of 18 amino acids. The sequence closely resembles that of the chelicerate hemocyanins. Molecular phylogenetic analyses reject with high statistical con…

Signal peptideDNA Complementarymedicine.medical_treatmentMolecular Sequence DataMyriapodachemical and pharmacologic phenomenaBiologycomplex mixturesEvolution MolecularSequence Analysis ProteinGeneticsmedicineAnimalsAmino Acid SequenceCloning MolecularMolecular BiologyArthropodsEcology Evolution Behavior and SystematicsPhylogenyPhylogenetic treeSequence Homology Amino Acidhemic and immune systemsHemocyaninAnatomySequence Analysis DNAbiology.organism_classificationSpirostreptusSister groupEvolutionary biologyHemocyaninsChelicerataSequence AlignmentSpirostreptidae
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The nucleotide and deduced amino acid structures of sheep and pig fetuin. Common structural features of the mammalian fetuin family

1992

This study was initiated to gain further insight into the structural features of the mammalian fetuin family. The cDNA structures of sheep and pig fetuin were determined. The cDNA insert encoding sheep (pig) fetuin comprised 1550 (1470) nucleotides, including 54 (46) nucleotides encoding a signal peptide of 18 (15) residues and 1038 (1041) nucleotides encoding the 346 (347) amino acids of the mature plasma protein. The predicted amino-terminal sequence of the mature pig fetuin was confirmed by the amino-terminal sequence of the purified protein. However, two alternative sheep amino-terminal sequences were found in fetuin purified from the plasma of a single sheep fetus; the minor product wa…

Signal peptideGlycosylationSwineBlotting WesternMolecular Sequence DataSequence alignmentBiologyBiochemistrySequence Homology Nucleic AcidComplementary DNAEndopeptidasesAnimalsHumansAmino Acid SequenceCloning MolecularPeptide sequenceMammalschemistry.chemical_classificationSheepBase SequenceSerine EndopeptidasesStructural geneNucleic acid sequenceMembrane ProteinsDNAMolecular biologyFetuinAmino acidBiochemistrychemistryElectrophoresis Polyacrylamide Gelalpha-FetoproteinsEuropean Journal of Biochemistry
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Isolation of a novel LPS-induced component of the ML superfamily in Ciona intestinalis

2015

ML superfamily represents a group of proteins playing important roles in lipid metabolism and innate immune response. In this study, we report the identification of the first component of the ML superfamily in the invertebrate Ciona intestinalis by means of a subtractive hybridization strategy. Sequence homology and phylogenetic analysis showed that this protein forms a specific clade with vertebrate components of the Niemann-Pick type C2 protein and, for this reason, it has been named Ci-NPC2. The putative Ci-NPC2 is a 150 amino acids long protein with a short signal peptide, seven cysteine residues, three putative lipid binding site and a three-dimensional model showing a characteristic b…

Signal peptideLipopolysaccharidesHemocytesImmunologyMolecular Sequence DataSettore BIO/05 - ZoologiaSequence alignmentBiologyBioinformaticshemic and lymphatic diseasesGene expressionAnimalsCiona intestinalisAmino Acid SequencePeptide sequenceGenePhylogenychemistry.chemical_classificationBase SequenceSequence Homology Amino Acidnutritional and metabolic diseasesbiology.organism_classificationLipid MetabolismImmunity InnateAmino acidCiona intestinalisBiochemistrychemistryLPS NPC2 Ciona intestinalisSuppression subtractive hybridizationCarrier ProteinsSequence AlignmentDevelopmental Biology
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The crystal structure of bacteriophage Qβ at 3.5 å resolution

1996

Abstract Background: The capsid protein subunits of small RNA bacteriophages form a T=3 particle upon assembly and RNA encapsidation. Dimers of the capsid protein repress translation of the replicase gene product by binding to the ribosome binding site and this interaction is believed to initiate RNA encapsidation. We have determined the crystal structure of phage Qβ with the aim of clarifying which factors are the most important for particle assembly and RNA interaction in the small phages. Results The crystal structure of bacteriophage Qβ determined at 3.5 a resolution shows that the capsid is stabilized by disulfide bonds on each side of the flexible loops that are situated around the fi…

Small RNAcrystal structureProtein ConformationvirusesMolecular Sequence DataBeta sheetMS2RNA-dependent RNA polymeraseCapsidProtein structureStructural BiologyAmino Acid SequenceBinding siteMolecular BiologyAllolevivirusBinding SitesCrystallographySequence Homology Amino AcidbiologyRNA-Binding ProteinsRNAbiology.organism_classificationProtein Structure TertiaryCrystallographyCapsidBiophysicsSequence AlignmentBacteriophage QβStructure
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