0000000000190676

AUTHOR

L. Valero

showing 5 related works from this author

iTRAQ and DIGE in the ecophysiological characterization of zebra mussel populations (Dreissena polymorpha) invading the Ebro and the Júcar hydrograph…

2012

Poster presentado en el 9th Iberian and 6th Iberoamerican Congress on Environmental Contamination and Toxicology "The environmental research: essential for sustainability" celebrado en Valencia del 1 al 3 de julio de 2013

animal structuresGeographybiologyPhysiologyEcologyZebra musselEnvironmental researchbiology.organism_classificationHydrographyMolecular BiologyBiochemistryDreissenaComparative Biochemistry and Physiology Part A: Molecular & Integrative Physiology
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An insight into the proteome of the saliva of the argasid tick Ornithodoros moubata reveals important differences in saliva protein composition betwe…

2013

26 páginas, 3 tablas, 6 figuras. -- The definitive version is available at http://www.elsevier.com

MaleProteomicsSalivaProteomeBiophysicsTickExosomesBiochemistryMicrobiologyTranscriptomeSex Factorsstomatognathic systemLC–MS/MSTandem Mass SpectrometryOrnithodoros moubataAnimalsSecretionOrnithodorosSalivaExpressed Sequence TagsbiologyProtein equalizationComputational Biologybiology.organism_classificationBlood mealActinsRecombinant ProteinsOrnithodoros moubataSialomePhosphopyruvate HydrataseSialomeImmunologyProteomeElectrophoresis Polyacrylamide GelFemaleChromatography Liquid
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Evolutionary Changes after Translational Challenges Imposed by Horizontal Gene Transfer

2019

International audience; Genes acquired by horizontal gene transfer (HGT) may provide the recipient organism with potentially new functions, but proper expression level and integration of the transferred genes in the novel environment are not granted. Notably, transferred genes can differ from the receiving genome in codon usage preferences, leading to impaired translation and reduced functionality. Here, we characterize the genomic and proteomic changes undergone during experimental evolution of Escherichia coli after HGT of three synonymous versions, presenting very different codon usage preference, of an antibiotic resistance gene. The experimental evolution was conducted with and without…

0106 biological sciencesantibiotic resistanceGene Transfer HorizontalProteome[SDV]Life Sciences [q-bio]Bacterial genome sizeBiology010603 evolutionary biology01 natural sciencesGenomeEvolution Molecular03 medical and health sciences[SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry Molecular Biology/Genomics [q-bio.GN]Drug Resistance BacterialEscherichia coliGeneticsexperimental evolutionGeneEcology Evolution Behavior and Systematics030304 developmental biologyGenetics0303 health sciencesExperimental evolution[SDV.BID.EVO]Life Sciences [q-bio]/Biodiversity/Populations and Evolution [q-bio.PE]compensatory evolutionGenomicsPhenotype[SDV.BIBS]Life Sciences [q-bio]/Quantitative Methods [q-bio.QM][SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriologycodon usage preferencesGenòmicaGenesCodon usage biasHorizontal gene transferProteomehorizontal gene transferResearch ArticleGens
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Proteomic analysis of the somatic and surface compartments from Dirofilaria immitis adult worms.

2014

31 páginas, 1 tabla, 4 figuras.-- The definitive version is available at http://www.elsevier.com

MaleProteomicsPathologymedicine.medical_specialtyProteomeSomatic cellDirofilaria immitisDirofilaria immitisProteomicsGenomeMicrobiologyTranscriptomeImmune systemmedicineParasite hostingAnimalsSomaticCATSGeneral VeterinarybiologyGeneral MedicineHelminth Proteinsbiology.organism_classificationSurfaceProtein TransportGene Expression RegulationAntigens SurfaceParasitologyFemaleVeterinary parasitology
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Identification of antigenic proteins from Echinostoma caproni (Trematoda) recognized by mouse immunoglobulins M, A and G using an immunoproteomic app…

2008

Antigenic proteins of Echinostoma caproni (Trematoda) against mouse IgM, IgA, IgG, IgG1 and IgG2a were investigated by immunoproteomics. Excretory/secretory products (ESP) of E. caproni separated by two-dimensional (2D) gel electrophoresis were transferred to nitrocellulose membranes and probed with the different mouse immunoglobulin classes. A total of four proteins (enolase, 70 kDa heat-shock protein (HSP-70), actin and aldolase) were accurately identified. Enolase was recognized in eight different spots of which seven of them were detected in the expected molecular weight and were recognized by IgA, IgG or IgG and IgG1. Another spot identified as enolase at 72 kDa was only recognized by …

MaleProteomicsImmunologyEnolaseBlotting WesternImmunoglobulinsEchinostoma caproniImmunoproteomicsaldolaseMiceexcretory/secretory productsAntigenHeat shock proteinEchinostomaFructose-Bisphosphate AldolaseAnimalsSecretionElectrophoresis Gel Two-DimensionalHSP70 Heat-Shock ProteinsGel electrophoresisEchinostomiasisMice Inbred ICRbiologyAldolase Aheat-shock proteinMolecular biologyActinsenolaseBiochemistryAntigens HelminthPhosphopyruvate HydrataseSpectrometry Mass Matrix-Assisted Laser Desorption-IonizationImmunologybiology.proteinParasitologyAntibodyactinParasite immunology
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