Search results for "homology"

showing 10 items of 770 documents

Lineage diversification and recombination in type-4 human astroviruses.

2013

Abstract Human astroviruses (HAstVs) are important enteric pathogens and can be classified genetically and antigenically into eight types. During surveillance of HAstVs in Italy, type-4 HAstVs were detected only sporadically and found to cluster into two distinct genetic groups. Upon sequence analysis of the 3′ end of the polymerase gene (ORF1b) and of the full-length ORF2, the 2008 type-4 HAstV strains were characterised as a novel ORF2 genetic lineage, designated as 4c. The 2008 type-4 HAstVs also shared the ORF1b gene with similar HAstV-4c strains detected globally, thus displaying a conserved ORF1b/ORF2 asset. By interrogation of the databases, this novel lineage 4c accounted for 60.8% …

Microbiology (medical)Settore MED/07 - Microbiologia E Microbiologia ClinicaLineage (genetic)Sequence analysisMolecular Sequence DataSequence alignmentBiologyMicrobiologyAstrovirusFecesOpen Reading FramesAstrovirus Epidemiology Genotyping Italy Viral gastroenteritisPhylogeneticsAstroviridae InfectionsGenetic variationGeneticsHumansAmino Acid SequenceMolecular BiologyGenotypingGeneEcology Evolution Behavior and SystematicsPhylogenyGeneticsRecombination GeneticBase SequenceSequence Homology Amino AcidSequence Analysis RNAvirus diseasesGenetic Variationbiology.organism_classificationRNA-Dependent RNA PolymeraseGastroenteritisInfectious DiseasesRNA ViralCapsid ProteinsSequence AlignmentMamastrovirusInfection, genetics and evolution : journal of molecular epidemiology and evolutionary genetics in infectious diseases
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Simultaneous identification of campylobacters and prediction of quinolone resistance by comparative sequence analysis.

1997

Comparative sequence analysis of a 30-bp segment in the quinolone resistance-determining region of campylobacters not only allows for the detection of base changes associated with resistance but also is a powerful tool for species identification based on silent mutations.

Microbiology (medical)Silent mutationDNA Bacterialmedicine.drug_classSequence analysisSequence alignmentBiologymedicine.disease_causeDNA gyrasePolymerase Chain Reactionlaw.inventionAnti-Infective AgentsSpecies SpecificitylawmedicinePolymerase chain reactionAntibacterial agentGeneticsMutation4-QuinolonesSequence Homology Amino AcidCampylobacterDrug Resistance MicrobialSequence Analysis DNAQuinoloneDNA Topoisomerases Type IIDNA GyraseSequence AlignmentResearch Article
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Mitochondrial genome of Suberites domuncula: palindromes and inverted repeats are abundant in non-coding regions.

2007

The 26,300-nucleotide sequence of the mitochondrial DNA (mtDNA) molecule of the demosponge Suberites domuncula (Olivi, 1792), the largest in size yet found in Porifera, has been determined. We describe the second hadromerid sponge mitochondrial genome that contains the same set of 41 genes as the hadromerid sponge Tethya actinia, including trnMe(cau), trnI2(cau), trnR2(ucu), and atp9, all of which are transcribed in the same direction. Furthermore, rRNA genes for the small and large ribosomal subunit are very long, rns is indeed the longest among Metazoa (1833 bp). Intergenic regions (IGR) comprise about 25% of S. domuncula mtDNA and include numerous direct and inverted repeats, as well as …

Mitochondrial DNAInverted repeatMolecular Sequence DataSuberites ficusDNA MitochondrialIntergenic regionRNA TransferSpecies SpecificityLarge ribosomal subunitSequence Homology Nucleic AcidGeneticsAnimalsGenePhylogenyRepetitive Sequences Nucleic AcidGeneticsPorifera ; Hadromerida ; mtDNA ; mitochondrial evolution ; polymorphismsBase CompositionbiologyBase SequenceGenetic VariationGeneral MedicineRibosomal RNAbiology.organism_classificationSuberites domunculaGenome MitochondrialDNA IntergenicSuberitesGene
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Characterization of the length polymorphism in the A + T-rich region of the Drosophila obscura group species

1993

In the twelve Drosophila obscura group species studied, belonging to the affinis, obscura, and pseudoobscura subgroups, the mitochondrial DNA length ranges from 15.8 to 17.2 kb. This length polymorphism is mainly due to insertions/deletions in the variable region of the A + T-rich region. In addition, one species (D. tristis) possess a tandem duplication of a 470-bp fragment that contains the replication origin. The same duplication has occurred at least twice in the Drosophila evolutionary history due to the fact that the repetition is analogous to repetitions found in the four species of the D. melanogaster complex. By comparing the nucleotide sequence of the conserved region in D. ambigu…

Mitochondrial DNAMolecular Sequence DataRestriction MappingDNA RecombinantDNA MitochondrialConserved sequenceSpecies SpecificityMolecular evolutionDrosophilidaeSequence Homology Nucleic AcidGene duplicationGeneticsAnimalsMolecular BiologyEcology Evolution Behavior and SystematicsGeneticsPolymorphism GeneticbiologyBase SequenceAdenineNucleic acid sequencebiology.organism_classificationNucleic Acid ConformationDrosophilaTandem exon duplicationDrosophila obscuraSequence AlignmentPlasmidsThymidine
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Mitochondrial simple sequenze repeats and 12s – rRNA gene reveal two distinct lineages of Crocidura russula (Mammalia, Sorcidae)

2004

A short segment (135 bp) of the control region and a partial sequence (394 bp) of the 12S-rRNA gene in the mitochondrial DNA of Crocidura russula were analyzed in order to test a previous hypothesis regarding the presence of a gene flow disruption in northern Africa. This breakpoint would have separated northeast-African C. russula populations from the European (plus the northwest-African) populations. The analysis was carried out on specimens from Tunisia (C. r. cf agilis), Sardinia (C. r. ichnusae), and Pantelleria (C. r. cossyrensis), and on C. r. russula from Spain and Belgium. Two C. russula lineages were identified; they both shared R2 tandem repeated motifs of the same length (12 bp)…

Mitochondrial DNARange (biology)Lineage (evolution)Crocidura russulaMolecular Sequence DataMtDNASettore BIO/05 - ZoologiaDNA MitochondrialMonophylyAfrica NorthernPhylogeneticsSequence Homology Nucleic AcidGeneticsAnimals12S-rRNA; Crocidura russula; MtDNA; North Africa; SSRs; ZoogeographyGenetics (clinical)PhylogenybiologyBase SequenceEcology12S-rRNAShrewsGenes rRNAbiology.organism_classificationNorth AfricaCrocidura russulaSSRRussulaMitochondriaEuropeGenetics PopulationSister groupEvolutionary biologyRNA RibosomalZoogeographySequence AlignmentSequence AnalysisMicrosatellite Repeats
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Statistical Validation of the Identification of Tuna Species:  Bootstrap Analysis of Mitochondrial DNA Sequences

2002

Sequencing of the mitochondrial cytochrome b gene has been used to differentiate three tuna species: Thunnus albacares (yellowfin tuna), Thunnus obesus (bigeye tuna), and Katsuwonus pelamis (skipjack). A PCR amplified 528 bp fragment from 30 frozen samples and a 171 bp fragment from 26 canned samples of the three species were analyzed to determine the intraspecific variation and the positions with diagnostic value. Polymorphic sites between the species that did not present intraspecific variation were given a diagnostic value. The genetic distance between the sequences was calculated, and a phylogenetic tree was constructed, showing that the sequences belonging to the same species clustered…

Mitochondrial DNAYellowfin tunaMeatMolecular Sequence DataZoologyBigeye tunaDNA MitochondrialSpecies SpecificityAnimalsPhylogenyPolymorphism GeneticBase SequenceSequence Homology Amino AcidPhylogenetic treebiologyTunaCytochrome bReproducibility of ResultsGeneral Chemistrybiology.organism_classificationGenetic distanceEvolutionary biologyGeneral Agricultural and Biological SciencesTunaSequence Alignmenthuman activitiesThunnusJournal of Agricultural and Food Chemistry
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Maintenance of a Protein Structure in the Dynamic Evolution of TIMPs over 600 Million Years

2016

Deciphering the events leading to protein evolution represents a challenge, especially for protein families showing complex evolutionary history. Among them, TIMPs represent an ancient eukaryotic protein family widely distributed in the animal kingdom. They are known to control the turnover of the extracellular matrix and are considered to arise early during metazoan evolution, arguably tuning essential features of tissue and epithelial organization. To probe the structure and molecular evolution of TIMPs within metazoans, we report the mining and structural characterization of a large data set of TIMPs over approximately 600 Myr. The TIMPs repertoire was explored starting from the Cnidaria…

Models Molecular0301 basic medicineTIMPsProtein familyProtein Conformationhomology modelingSettore BIO/11 - Biologia MolecolareSequence alignmentBiologytranscriptome wide analysisConserved sequencecnidariansEvolution MolecularCnidaria03 medical and health sciences0302 clinical medicineProtein structurePhylogeneticsMolecular evolutionGeneticsAnimalsTIMPAmino Acid SequenceHomology modelingcnidarianConserved SequencePhylogenyEcology Evolution Behavior and SystematicsGeneticsmyrTissue Inhibitor of Metalloproteinases030104 developmental biologyEvolutionary biologyTIMPs; cnidarians; homology modeling; transcriptome wide analysisSequence Alignment030217 neurology & neurosurgeryResearch Article
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Structure of Rhodococcus erythropolis limonene-1,2-epoxide hydrolase reveals a novel active site

2003

Epoxide hydrolases are essential for the processing of epoxide-containing compounds in detoxification or metabolism. The classic epoxide hydrolases have an alpha/beta hydrolase fold and act via a two-step reaction mechanism including an enzyme-substrate intermediate. We report here the structure of the limonene-1,2-epoxide hydrolase from Rhodococcus erythropolis, solved using single-wavelength anomalous dispersion from a selenomethionine-substituted protein and refined at 1.2 A resolution. This enzyme represents a completely different structure and a novel one-step mechanism. The fold features a highly curved six-stranded mixed beta-sheet, with four alpha-helices packed onto it to create a …

Models MolecularAFSG Stafafdelingen (WUATV)10050 Institute of Pharmacology and Toxicologydrug protein bindingEnantioselectivityEpoxide hydrolaseCrystallography X-Rayuncultured actinomyceteCatalytic Domain2400 General Immunology and Microbiologyalpha helixRhodococcuscholesterol epoxide hydrolasenaphthalene 12-dioxygenasedcl14limonene 12 epoxide hydrolaseEpoxide hydrolaseBacteria (microorganisms)delta(5)-3-ketosteroid isomeraseEpoxide HydrolasesLimonene-12-epoxide hydrolaseGeneral Neurosciencearticle2800 General NeuroscienceActinobacteria (class)Articlesagrobacterium-radiobacterEnzyme structureRecombinant Proteinsunclassified drugenzyme structurereaction analysisBiochemistrypriority journalenzyme active siteMechanism2-dioxygenaseDimerizationBiotechnologychemical reactioncrystal structureaspergillus-nigermacromolecular structuresStereochemistrybeta sheetvalpromideMolecular Sequence Data610 Medicine & healthGenetics and Molecular BiologyBiologyGeneral Biochemistry Genetics and Molecular BiologyBacterial Proteinssite directed mutagenesis1300 General Biochemistry Genetics and Molecular BiologyHydrolase1312 Molecular BiologyAmino Acid SequencedetoxificationRhodococcus erythropolisBiologyMonoterpene degradationMolecular Biologyprotein data-bankenzyme substrate complexEnzyme substrate complexnonhumancatalysisSequence Homology Amino AcidGeneral Immunology and Microbiologybacterial enzymeActive sitecrystal-structureAFSG Staff Departments (WUATV)enzyme metabolismProtein SubunitsenzymeEpoxide HydrolasesGeneral Biochemistrybiology.proteinMutagenesis Site-Directed570 Life sciences; biologyselenomethioninenaphthalene 1Alpha helix
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Design and construction of highly stable, protease-resistant chimeric avidins.

2005

The chicken avidin gene family consists of avidin and seven separate avidin-related genes (AVRs) 1-7. Avidin protein is a widely used biochemical tool, whereas the other family members have only recently been produced as recombinant proteins and characterized. In our previous study, AVR4 was found to be the most stable biotin binding protein thus far characterized (T(m) = 106.4 degrees C). In this study, we studied further the biotin-binding properties of AVR4. A decrease in the energy barrier between the biotin-bound and unbound state of AVR4 was observed when compared with that of avidin. The high resolution structure of AVR4 facilitated comparison of the structural details of avidin and …

Models MolecularBiotin bindingInsectaProtein familyProtein subunitRecombinant Fusion ProteinsMolecular Sequence DataBiotinBiosensing TechniquesBiologyProtein EngineeringBiochemistryProtein Structure SecondaryProtein structureAnimalsAmino Acid SequenceMolecular BiologyThermostabilityCalorimetry Differential ScanningSequence Homology Amino AcidTemperatureCell BiologyProtein engineeringAvidinRecombinant ProteinsProtein Structure TertiaryKineticsBiochemistryMicroscopy FluorescenceMutagenesisBiotinylationMutationbiology.proteinChromatography GelThermodynamicsElectrophoresis Polyacrylamide GelEndopeptidase KBaculoviridaeChickensAvidinChromatography LiquidPeptide HydrolasesProtein BindingThe Journal of biological chemistry
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Cytotoxicity of Novel Sulfanilamides Towards Sensitive and Multidrugresistant Leukemia Cells

2014

Novel sulfa Schiff bases were synthesized and characterized by a reaction between aromatic sulfonamides and aromatic aldehydes or heterocyclic ketones in equimolar ratios. Their cytotoxicity was evaluated by the resazurin assay towards human sensitive CCRF-CEM and multidrug-resistant CEM/ADR5000 leukemia cells. Three of the tested compounds viz., 4-(anthracen-9-ylmethyleneamino)-N-(pyrimidin-2-yl)benzenesulfonamide (4), 4-(anthracen-9- ylmethyleneamino)benzenesulfonamide, (5) and 4-((3-phenylallylidene)amino)benzene-sulfonamide, (6) were cytotoxic (IC 50 values: 5.38-19.96 µM). CEM/ADR5000 cells were not cross-resistant to these compounds, indicating activity against otherwise drug-resistan…

Models MolecularCell SurvivalStereochemistryBiochemistrychemistry.chemical_compoundSulfanilamideCell Line TumorSulfanilamidesDrug DiscoverymedicineHumansCytotoxic T cellDoxorubicinATP Binding Cassette Transporter Subfamily B Member 1Homology modelingCytotoxicityPharmacologyLeukemiaChemistryOrganic ChemistryResazurinSulfanilamidemedicine.diseaseProtein Structure TertiaryLeukemiaDoxorubicinDrug Resistance NeoplasmMolecular MedicineVerapamilmedicine.drugCurrent Medicinal Chemistry
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