Search results for " primary"

showing 10 items of 453 documents

CD28, a marker associated with tumoral expansion in multiple myeloma

1998

International audience; CD28 expression was thoroughly investigated on plasma cells of monoclonal gammopathy of undetermined significance, multiple myeloma (MM), and human myeloma cell lines. CD28+ plasma cells were detected in 19% of 31 monoclonal gammopathy of undetermined significance, 41% of 116 MM, and 100% of 13 human myeloma cell lines. CD28+ myeloma cells were detected in 21 of 79 (26%) MM cases at diagnosis, 13 of 22 (59%) at medullary relapse (P < 0.009), and 14 of 15 (93%) at extramedullary relapse (P = 0.05), including 10 of 10 (100%) secondary plasma cell leukemias (P = 0.05). Serial studies in individual patients confirmed the emergence of CD28+ myeloma cells with tumoral expa…

Membrane GlycoproteinsParaproteinemiasNeoplasms Second Primarychemical and pharmacologic phenomenahemic and immune systemsCD56 AntigenCell LineLeukemia Plasma CellCD28 AntigensAntigens CDBone MarrowPredictive Value of TestsRecurrence[ INFO.INFO-BI ] Computer Science [cs]/Bioinformatics [q-bio.QM]hemic and lymphatic diseasesB7-1 AntigenBiomarkers TumorDisease ProgressionTumor Cells CulturedHumansB7-2 AntigenTreatment Failure[INFO.INFO-BI]Computer Science [cs]/Bioinformatics [q-bio.QM]Multiple Myeloma[INFO.INFO-BI] Computer Science [cs]/Bioinformatics [q-bio.QM]
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Genes and derived amino acid sequences of S-layer proteins from mesophilic, thermophilic, and extremely thermophilic methanococci

2002

Cells of methanococci are covered by a single layer of protein subunits (S-layer) in hexagonal arrangement, which are directly exposed to the environment and which cannot be stabilized by cellular components. We have isolated S-layer proteins from cells of Methanococcus vannielii ( T(opt.)=37 degrees C), Methanococcus thermolithotrophicus ( T(opt.)=65 degrees C), and Methanococcus jannaschii ( T(opt.)=85 degrees C). The primary structure of the S-layer proteins was determined by sequencing the corresponding genes. According to the predicted amino acid sequence, the molecular masses of the S-layer proteins of the different methanococci are in a small range between 59,064 and 60,547 Da. Compa…

MethanococcusArchaeal ProteinsMethanococcusMolecular Sequence DataMicrobiologySpecies SpecificityMethanococcalesAmino Acid SequencePeptide sequencechemistry.chemical_classificationSequence Homology Amino AcidbiologyThermophileTemperatureProtein primary structureGeneral Medicinebiology.organism_classificationMethanococciAmino acidchemistryBiochemistryGenes BacterialMolecular MedicineSequence AlignmentS-layerBacterial Outer Membrane ProteinsExtremophiles
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The evolutionary history of symbiotic associations among bacteria and their animal hosts: a model

2009

AbstractA model to explain the evolutionary history of animal-bacteria obligatory mutualistic symbiosis is presented. Dispensability of genes and genetic isolation are key factors in the reduction process of these bacterial genomes. Major steps in such genome reductive evolution, leading towards primary endoslmblosis, and the possibility of complementation or replacement by a secondary symbiont are also indicated. Yet, we need to understand what happens at the beginning of the adaptative process towards an obligate mutualistic relationship. For this purpose, we propose to sequence the complete genome of SOPE, the primary endosymbiont of the rice weevil.

Microbiology (medical)Bacterial genome sizeBiologyreplacementBacterial Physiological PhenomenaGenomeEvolution MolecularAnimalsgenome reductionSymbiosisGeneSequence DeletionGeneticsendosymbiosisComplementationBacteriaObligateEndosymbiosisGeneral Medicinebiology.organism_classificationSOPE (Sitophilus oryzae primary endorsement)ComplementationInfectious DiseasesWeevilsGenetic isolateGene DeletionGenome BacterialBacteriaClinical Microbiology and Infection
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The Streptomyces coelicolor Small ORF trpM Stimulates Growth and Morphological Development and Exerts Opposite Effects on Actinorhodin and Calcium-De…

2020

In actinomycetes, antibiotic production is often associated with a morpho-physiological differentiation program that is regulated by complex molecular and metabolic networks. Many aspects of these regulatory circuits have been already elucidated and many others still deserve further investigations. In this regard, the possible role of many small open reading frames (smORFs) in actinomycete morpho-physiological differentiation is still elusive. In Streptomyces coelicolor, inactivation of the smORF trpM (SCO2038) – whose product modulates L-tryptophan biosynthesis – impairs production of antibiotics and morphological differentiation. Indeed, it was demonstrated that TrpM is able to interact w…

Microbiology (medical)Primary and secondary metabolismlcsh:QR1-502cytosol aminopeptidaseStreptomyces coelicoloractinorhodin productionSettore BIO/19 - Microbiologia GeneraletrpM.MicrobiologyAminopeptidaselcsh:MicrobiologyActinorhodin03 medical and health scienceschemistry.chemical_compoundBiosynthesisTRPMSmall open reading frameProtein biosynthesis030304 developmental biologychemistry.chemical_classificationsmall open reading frame0303 health sciencescalcium-dependent antibioticCalcium-dependent antibioticbiologysmall open reading frame trpM actinorhodin production Streptomyces coelicolor cytosol aminopeptidase calcium-dependent antibiotic primary and secondary metabolism030306 microbiologyActinorhodin productionStreptomyces coelicolorprimary and secondary metabolismtrpMbiology.organism_classificationAmino acidMetabolic pathwaychemistryBiochemistryCytosol aminopeptidaseFrontiers in Microbiology
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Heterogeneity at the HLA-DRB1 locus and risk for multiple sclerosis.

2006

Variation in major histocompatibility complex genes on chromosome 6p21.3, specifically the human leukocyte antigen HLA-DR2 or DRB1*1501-DQB1*0602 extended haplotype, confers risk for multiple sclerosis (MS). Previous studies of DRB1 variation and both MS susceptibility and phenotypic expression have lacked statistical power to detect modest genotypic influences, and have demonstrated conflicting results. Results derived from analyses of 1339 MS families indicate DRB1 variation influences MS susceptibility in a complex manner. DRB1*15 was strongly associated in families (P=7.8x10(-31)), and a dominant DRB1*15 dose effect was confirmed (OR=7.5, 95% CI=4.4-13.0, P<0.0001). A modest dose effect…

Models MolecularMaleSequence Homologyimmune system diseasesModelsRisk FactorsDatabases GeneticAdult Alleles Amino Acid Sequence Databases; Genetic Female Genetic Variation Genotype HLA-DR Antigens; chemistry/genetics HLA-DRB1 Chains Humans Male Middle Aged Models; Molecular Molecular Sequence Data Multiple Sclerosis; Chronic Progressive; genetics/immunology Multiple Sclerosis; genetics/immunology Phenotype Risk Factors Sequence Homology; Amino Acidskin and connective tissue diseasesHLA-DRB1Genetics (clinical)GeneticsGeneral MedicineMultiple Sclerosis Chronic ProgressiveMiddle AgedAmino AcidChronic ProgressivePhenotypeFemalemusculoskeletal diseasesAdultMultiple SclerosisGenotypeMolecular Sequence DataLocus (genetics)Human leukocyte antigenBiologyDatabases. Alleles phenotype heterogeneity human leukocyte antigens age of onset chromosomes genes genotype haplotypesmultiple sclerosis relapsing-remitting genetics disability primary progressive multiple sclerosis hla-drb1 gene illness length severity of illnessGeneticGenetic variationGeneticsmedicineHumansAmino Acid SequenceAlleleMolecular BiologyAllelesSequence Homology Amino AcidMultiple sclerosisHaplotypeGenetic VariationMolecularHLA-DR Antigensmedicine.diseasegenetics/immunologychemistry/geneticsImmunologyAge of onsetHLA-DRB1 Chains
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Nautilus pompilius Hemocyanin: 9 Å Cryo-EM Structure and Molecular Model Reveal the Subunit Pathway and the Interfaces between the 70 Functional Units

2007

Hemocyanins are giant extracellular oxygen carriers in the hemolymph of many molluscs. Nautilus pompilius (Cephalopoda) hemocyanin is a cylindrical decamer of a 350 kDa polypeptide subunit that in turn is a "pearl-chain" of seven different functional units (FU-a to FU-g). Each globular FU has a binuclear copper centre that reversibly binds one O(2) molecule, and the 70-FU decamer is a highly allosteric protein. Its primary structure and an 11 A cryo-electron microscopy (cryo-EM) structure have recently been determined, and the crystal structures of two related FU types are available in the databanks. However, in molluscan hemocyanin, the precise subunit pathway within the decamer, the inter…

Models MolecularMolecular modelProtein Conformationmedicine.medical_treatmentProtein subunitMolecular Sequence DataOctopodiformesAllosteric regulationBiologyHemocyaninTurn (biochemistry)Protein structureStructural BiologyImage Processing Computer-AssistedmedicineAnimalsAmino Acid SequenceMolecular BiologyBinding SitesSequence Homology Amino AcidCryoelectron MicroscopyProtein primary structureHemocyaninCrystallographyHemocyaninsBiophysicsNautilusProtein quaternary structureJournal of Molecular Biology
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Structure of Mega-Hemocyanin Reveals Protein Origami in Snails

2014

SummaryMega-hemocyanin is a 13.5 MDa oxygen transporter found in the hemolymph of some snails. Similar to typical gastropod hemocyanins, it is composed of 400 kDa building blocks but has additional 550 kDa subunits. Together, they form a large, completely filled cylinder. The structural basis for this highly complex protein packing is not known so far. Here, we report the electron cryomicroscopy (cryo-EM) structure of mega-hemocyanin complexes from two different snail species. The structures reveal that mega-hemocyanin is composed of flexible building blocks that differ in their conformation, but not in their primary structure. Like a protein origami, these flexible blocks are optimally pac…

Models MolecularProtein FoldingCryo-electron microscopymedicine.medical_treatmentGastropodaSnailsNanotechnologySnailBiologyMega-Cylinder (gastropod)Structural Biologybiology.animalHemolymphmedicineAnimalsProtein Structure QuaternaryMolecular BiologyCryoelectron MicroscopyProtein primary structureHemocyaninbiology.organism_classificationProtein SubunitsComplex proteinHemocyaninsBiophysicsProtein MultimerizationStructure
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The Sequence of a Gastropod Hemocyanin (HtH1 from Haliotis tuberculata)

2000

The eight functional units (FUs), a-h, of the hemocyanin isoform HtH1 from Haliotis tuberculata (Prosobranchia, Archaeogastropoda) have been sequenced via cDNA, which provides the first complete primary structure of a gastropod hemocyanin subunit. With 3404 amino acids (392 kDa) it is the largest polypeptide sequence ever obtained for a respiratory protein. The cDNA comprises 10,758 base pairs and includes the coding regions for a short signal peptide, the eight different functional units, a 3'-untranslated region of 478 base pairs, and a poly(A) tail. The predicted protein contains 13 potential sites for N-linked carbohydrates (one for HtH1-a, none for HtH1-c, and two each for the other si…

Models MolecularSignal peptideDNA ComplementaryProtein subunitmedicine.medical_treatmentMolecular Sequence DataOctopodiformesBiologyBiochemistryEvolution MolecularArchaeogastropodaComplementary DNAmedicineAnimalsProtein IsoformsComputer SimulationAmino Acid SequenceMolecular BiologyPeptide sequencePhylogenyGene LibrarySequence Homology Amino AcidProtein primary structureHemocyaninCell BiologyAnatomybiology.organism_classificationRespiratory proteinBiochemistryMolluscaHemocyaninsProtein BindingJournal of Biological Chemistry
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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 ADVANTAGES OF FLIPPED LEARNING MODEL: AN OPPORTUNITY TO INTEGRATE TECHNOLOGY IN CHILDREN'S LITERATURE

2016

Studying children’s literature involves questioning how fantasy and representations of childhood relate to cultural contexts and a specific target audience. In an age of technology and online media, this program teaches students how to encourage young people to appreciate literature's heritage. This research examines how using the flipped classroom model provides opportunities to design and deliver courses using active learning and engagement strategies to facilitate students’ teamwork, problem solving and critical thinking skills in a collegial environment. The aims of research are: to familiarise with some of the themes and ideas explored in a selection of literature for children from the…

Multimediabusiness.industrymedia_common.quotation_subjectFlipped learningElectrical engineeringFlipped model children's literature primary and pre-primary education.Artbusinesscomputer.software_genreSettore M-PED/04 - Pedagogia SperimentalecomputerSettore M-PED/03 - Didattica E Pedagogia Specialemedia_commonEDULEARN proceedings
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