Search results for "Sequence Alignment"

showing 10 items of 447 documents

Parallel and scalable short-read alignment on multi-core clusters using UPC++

2016

[Abstract]: The growth of next-generation sequencing (NGS) datasets poses a challenge to the alignment of reads to reference genomes in terms of alignment quality and execution speed. Some available aligners have been shown to obtain high quality mappings at the expense of long execution times. Finding fast yet accurate software solutions is of high importance to research, since availability and size of NGS datasets continue to increase. In this work we present an efficient parallelization approach for NGS short-read alignment on multi-core clusters. Our approach takes advantage of a distributed shared memory programming model based on the new UPC++ language. Experimental results using the …

Parallel computingInternetGenome HumanBioinformaticsPGASShort read alignmentlcsh:RComputational BiologyHigh-Throughput Nucleotide SequencingReproducibility of Resultslcsh:Medicine004 InformatikHumansProgramming Languageslcsh:QHigh performance computinglcsh:ScienceSequence AlignmentAlgorithms004 Data processingResearch Article
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Multiple Protein Sequence Alignment with MSAProbs

2013

Multiple sequence alignment (MSA) generally constitutes the foundation of many bioinformatics studies involving functional, structural, and evolutionary relationship analysis between sequences. As a result of the exponential computational complexity of the exact approach to producing optimal multiple alignments, the majority of state-of-the-art MSA algorithms are designed based on the progressive alignment heuristic. In this chapter, we outline MSAProbs, a parallelized MSA algorithm for protein sequences based on progressive alignment. To achieve high alignment accuracy, this algorithm employs a hybrid combination of a pair hidden Markov model and a partition function to calculate posterior…

Partition function (quantum field theory)Multiple sequence alignmentHeuristic (computer science)Computer scienceSequence alignmentAlgorithm
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Identification and functional expression of HCx31.9, a novel gap junction gene

2002

By combining in silico and bench molecular biology methods we have identified a novel human gap junction gene that encodes a protein designated HCx31.9. We have determined its human chromosomal location and gene structure, and we have identified a putative mouse ortholog, mCx30.2. We have observed the presence of HCx31.9 in human cerebral cortex, liver, heart, spleen, lung, and kidney and the presence of mCx30.2 in mouse cerebral cortex, liver and lung. Moreover, preliminary data on the electrophysiological properties of HCx31.9 have been obtained by functional expression in paired Xenopus oocytes and in transfected N2A cells.

Patch-Clamp TechniquesIn silicoMolecular Sequence DataClinical BiochemistryXenopuscloningGene ExpressionConnexinConnexinsCell Linegap junctionMiceXenopus laevisGene expressionmedicineAnimalsHumansTissue DistributionAmino Acid SequenceCloning MolecularGenePhylogenybiologycloning; CNS; gap junctionGap junctionGap JunctionsCell BiologyGeneral MedicineTransfectionbiology.organism_classificationMolecular biologymedicine.anatomical_structureCerebral cortexOocytesCNSSequence Alignment
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Primary structure and unusual carbohydrate moiety of functional unit 2-c of keyhole limpet hemocyanin (KLH)

1999

Abstract The complete amino acid sequence of the Megathura crenulata hemocyanin functional unit KLH2-c was determined by direct sequencing and matrix-assisted laser desorption ionization mass spectrometry of the protein, and of peptides obtained by cleavage with EndoLysC proteinase, chymotrypsin and cyanogen bromide. This is the first complete primary structure of a functional unit c from a gastropod hemocyanin. KLH2-c consists of 420 amino acid residues. Circular dichroism spectra indicated approx. 31% β-sheet and 29% α-helix contents. A multiple sequence alignment with other molluscan hemocyanin functional units revealed average identities between 41 and 49%, but 55% in case of Octopus he…

Peanut agglutininmedicine.medical_treatmentMolecular Sequence DataCarbohydratesBiophysicschemical and pharmacologic phenomenaMegathura crenulataBiochemistrychemistry.chemical_compoundStructural BiologymedicineAnimalsChymotrypsinAmino Acid SequenceRNA MessengerMolecular BiologyPeptide sequenceChromatography High Pressure LiquidbiologyMolecular massCircular DichroismProtein primary structureHemocyaninbiology.organism_classificationMolecular WeightBiochemistrychemistryMolluscaSpectrometry Mass Matrix-Assisted Laser Desorption-IonizationHemocyaninsbiology.proteinElectrophoresis Polyacrylamide GelCyanogen bromideSequence AlignmentKeyhole limpet hemocyaninBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
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Assessing divergence time of Spirulida and Sepiida (Cephalopoda) based on hemocyanin sequences

2011

Abstract The phylogenetic position of the mesopelagic decabrachian cephalopod Spirula is still a matter of debate. Since hemocyanin has successfully been used to calibrate a molecular clock for many molluscan species, a molecular clock was calculated based on this gene with special attention to the cephalopod genera Spirula and Sepia. The obtained partial sequence comprising ca., one third (3567 bp) of the complete gene is similar to that of Sepia officinalis. The molecular clock was calibrated using the splits of Gastropoda–Cephalopoda (ca. 550 ± 50 mya) and Heterobranchia–Vetigastropoda (ca. 380 ± 10 mya). The resulting hemocyanin-based molecular clock is stable, and the estimated diverge…

Phylogenetic treebiologyMesopelagic zonemedicine.medical_treatmentHemocyaninSequence Analysis DNAbiology.organism_classificationDivergenceCephalopodEvolution MolecularPaleontologyCephalopodaEvolutionary biologyHemocyaninsGeneticsmedicineAnimalsSpirulidaSepiaMolecular clockSequence AlignmentMolecular BiologyPhylogenyEcology Evolution Behavior and SystematicsMolecular Phylogenetics and Evolution
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The Arabidopsis COPT6 Transport Protein Functions in Copper Distribution Under Copper-Deficient Conditions

2013

Copper (Cu), an essential redox active cofactor, participates in fundamental biological processes, but it becomes highly cytotoxic when present in excess. Therefore, living organisms have established suitable mechanisms to balance cellular and systemic Cu levels. An important strategy to maintain Cu homeostasis consists of regulating uptake and mobilization via the conserved family of CTR/COPT Cu transport proteins. In the model plant Arabidopsis thaliana, COPT1 protein mediates root Cu acquisition, whereas COPT5 protein functions in Cu mobilization from intracellular storage organelles. The function of these transporters becomes critical when environmental Cu bioavailability diminishes. Ho…

PhysiologyMolecular Sequence DataSaccharomyces cerevisiaeMutantArabidopsisSaccharomyces cerevisiaePlant SciencePlant RootsCofactorCell membraneGene Expression Regulation PlantArabidopsisOrganellemedicineHomeostasisAmino Acid SequenceSLC31 ProteinsbiologyArabidopsis ProteinsMembrane transport proteinCell MembraneGenetic Complementation TestMembrane Transport ProteinsBiological TransportCell BiologyGeneral MedicinePlants Genetically Modifiedbiology.organism_classificationUp-RegulationTransport proteinCell biologyPlant LeavesMutagenesis Insertionalmedicine.anatomical_structureBiochemistrySeedsbiology.proteinPlant Vascular BundleSequence AlignmentCopperPlant ShootsPlant and Cell Physiology
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Similarities and singularities of three DnaK proteins from the cyanobacterium Synechocystis sp. PCC 6803.

2010

In the genome of completely sequenced mesophilic cyanobacterium Synechocystis sp. PCC 6803 three DnaK proteins are encoded, which share a high degree of sequence identity in their N-terminal ATPase region as well as in the adjacent peptide-binding domain. However, as typical for DnaK proteins, the C-termini of the three Synechocystis proteins are highly diverse. To study the functions of the three Synechocystis DnaK proteins in more detail, we have analyzed the abundance of the individual proteins in Synechocystis cells as well as dnaK expression under various stress conditions. The presented results show that all three Synechocystis DnaK proteins interact with the same GrpE nucleotide exch…

Physiologygenetic processesAmino Acid MotifsMolecular Sequence DataSequence alignmentPlant SciencePlasma protein bindingBiologymedicine.disease_causeMicrobiologyConserved sequenceNucleotide exchange factorBacterial ProteinsStress PhysiologicalmedicineHSP70 Heat-Shock ProteinsAmino Acid SequencePeptide sequenceConserved SequenceHeat-Shock ProteinsMutationSynechocystisSynechocystisCell BiologyGeneral MedicineGene Expression Regulation Bacterialbiology.organism_classificationBiochemistrybiological sciencesMutationbacteriaSequence AlignmentFunction (biology)Protein BindingPlantcell physiology
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Are elicitins cryptograms in plant-oomycete communications?

1999

Stimulation of plant natural defenses is an important challenge in phytoprotection prospects. In that context, elicitins, which are small proteins secreted by Phytophthora and Pythium species, have been shown to induce a hypersensitive-like reaction in tobacco plants. Moreover, these plants become resistant to their pathogens, and thus this interaction constitutes an excellent model to investigate the signaling pathways leading to plant resistance. However, most plants are not reactive to elicitins, although they possess the functional signaling pathways involved in tobacco responses to elicitin. The understanding of factors involved in this reactivity is needed to develop agronomic applica…

Phytophthora0106 biological sciences[SDV]Life Sciences [q-bio]Molecular Sequence DataMutagenesis (molecular biology technique)Context (language use)01 natural sciencesHost-Parasite InteractionsEvolution MolecularFungal Proteins03 medical and health sciencesCellular and Molecular NeuroscienceErgosterolGene Expression Regulation FungalTobaccoPlant defense against herbivoryAmino Acid SequenceMolecular BiologyPhylogenyComputingMilieux_MISCELLANEOUSPlant Diseases030304 developmental biologyPharmacologyOomycete0303 health sciencesBase SequencebiologyAlgal Proteinsfungifood and beveragesElicitinCell Biologybiology.organism_classification[SDV] Life Sciences [q-bio]Plants ToxicOomycetesBiochemistryMolecular MedicinePhytophthoraSequence AlignmentPlant lipid transfer proteinsFunction (biology)BiotechnologySignal Transduction010606 plant biology & botany
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Identification of a plasminogen-binding motif in PAM, a bacterial surface protein.

1995

Surface-associated plasmin(ogen) may contribute to the invasive properties of various cells. Analysis of plasmin(ogen)-binding surface proteins is therefore of interest. The N-terminal variable regions of M-like (ML) proteins from five different group A streptococcal serotypes (33, 41, 52, 53 and 56) exhibiting the plasminogen-binding phenotype were cloned and expressed in Escherichia coli. The recombinant proteins all bound plasminogen with high affinity. The binding involved the kringle domains of plasminogen and was blocked by a lysine analogue, 6-aminohexanoic acid, indicating that lysine residues in the M-like proteins participate in the interaction. Sequence analysis revealed that the…

PlasminStreptococcus pyogenesMolecular Sequence DataPlasma protein bindingBiologyMicrobiologyKringle domainBacterial ProteinsKringlesmedicineEscherichia coliAmino Acid SequenceBinding siteCloning MolecularMolecular BiologyPeptide sequenceBinding SitesBase SequenceLysinePlasminogenFusion proteinMolecular biologyRecombinant ProteinsPhenotypeBiochemistryCarrier ProteinsPlasminogen activatorSequence AlignmentBinding domainmedicine.drugProtein BindingMolecular microbiology
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TRIC: an automated alignment strategy for reproducible protein quantification in targeted proteomics

2016

Nature Methods, 13 (9)

Pluripotent Stem CellsProteomics0301 basic medicineAnalyteStreptococcus pyogenesSoftware toolQuantitative proteomicsProteomic analysisComputational biologyBiologyProteome informaticsProteomicsBioinformaticsBiochemistryArticleMass Spectrometry03 medical and health sciencesSequence Analysis ProteinProtein methodsHumansProtein PrecursorsHuman Induced Pluripotent Stem CellsMolecular BiologyElectronic Data ProcessingReproducibility of ResultsCell BiologyMass spectrometricTargeted proteomics030104 developmental biologyProteolysissense organsPeptidesSequence AlignmentAlgorithmsSoftwareBiotechnologyNature Methods
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