Search results for "ACID"

showing 10 items of 13107 documents

Protección integral de la mujer con diversidad funcional en supuestos de violencia de género

2016

"Protección integral de la mujer con diversidad funcional en supuestos de violencia de género" es la culminación de cuatro intensos años de apasionante investigación jurídica, dirigidos por la Doctora Elena Martínez García, la cual partió de una temática especialmente novedosa en el ámbito del derecho, pero que nos inducía a pensar que detrás de ella existía una realidad muchas veces silenciada. A partir de cuestiones tan concretas como igualdad, género, discapacidad o violencia machista, hemos visto como en la última fase de nuestro trabajo, el mismo ha terminado por coincidir con un legislador y unas políticas sociales mucho más abiertas e inclusivas, permitiéndonos recorrer en paralelo y…

violencia de génerodiscapacidadinterseccionalidaddiversidad funcional:CIENCIAS JURÍDICAS Y DERECHO [UNESCO]UNESCO::CIENCIAS JURÍDICAS Y DERECHOdoble discriminación
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Single-chain antibodies against a plant viral RNA-dependent RNA polymerase confer virus resistance.

2004

Crop loss due to viral diseases is still a major problem for agriculture today. We present a strategy to achieve virus resistance based on the expression of single-chain Fv fragments (scFvs) against a conserved domain in a plant viral RNA-dependent RNA polymerase (RdRp), a key enzyme in virus replication. The selected scFvs inhibited complementary RNA synthesis of different plant virus RdRps in vitro and virus replication in planta. Moreover, the scFvs also bound to the RdRp of the distantly related hepatitis C virus. T(1) and T(2) progeny of transgenic lines of Nicotiana benthamiana expressing different scFvs either in the cytosol or in the endoplasmic reticulum showed varying degrees of r…

virusesHepatitis C virusAmino Acid MotifsBiomedical EngineeringNicotiana benthamianaBioengineeringmedicine.disease_causeAntibodies ViralVirus ReplicationApplied Microbiology and BiotechnologyVirusPlant VirusesTombusviruschemistry.chemical_compoundRNA polymerasePlant virusTobaccomedicinePlant DiseasesGeneticsbiologyfungifood and beveragesbiology.organism_classificationPlants Genetically ModifiedRNA-Dependent RNA PolymeraseVirologyTombusviridaechemistryViral replicationMolecular MedicineSingle-Chain AntibodiesBiotechnologyNature biotechnology
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Modulation of Hepatitis C Virus NS5A Hyperphosphorylation by Nonstructural Proteins NS3, NS4A, and NS4B

1999

NS5A of the hepatitis C virus (HCV) is a highly phosphorylated protein involved in resistance against interferon and required most likely for replication of the viral genome. Phosphorylation of this protein is mediated by a cellular kinase(s) generating multiple proteins with different electrophoretic mobilities. In the case of the genotype 1b isolate HCV-J, in addition to the basal phosphorylated NS5A (designated pp56), a hyperphosphorylated form (pp58) was found on coexpression of NS4A (T. Kaneko, Y. Tanji, S. Satoh, M. Hijikata, S. Asabe, K. Kimura, and K. Shimotohno, Biochem. Biophys. Res. Commun. 205:320‐326, 1994). Using a comparative analysis of two full-length genomes of genotype 1b…

virusesHepatitis C virusHepacivirusMolecular Sequence DataImmunologyGene ExpressionReplicationHyperphosphorylationGenome ViralHepacivirusViral Nonstructural Proteinsmedicine.disease_causeMicrobiologyCell LineInterferonCricetinaeVirologymedicineAnimalsHumansPhosphorylationNS5ANS3Base SequencebiologyPestivirusvirus diseasesRNAbiochemical phenomena metabolism and nutritionbiology.organism_classificationVirologyMolecular biologydigestive system diseasesAmino Acid SubstitutionInsect ScienceDNA Viralmedicine.drugJournal of Virology
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Functional properties of a monoclonal antibody inhibiting the hepatitis C virus RNA-dependent RNA polymerase.

2001

The hepatitis C virus (HCV) RNA-dependent RNA polymerase (RdRp), represented by nonstructural protein 5B (NS5B), has recently emerged as a promising target for antiviral intervention. Here, we describe the isolation, functional characterization, and molecular cloning of a monoclonal antibody (mAb) inhibiting the HCV RdRp. This mAb, designated 5B-12B7, binds with high affinity to a conformational epitope in the palm subdomain of the HCV RdRp and recognizes native NS5B expressed in the context of the entire HCV polyprotein or subgenomic replicons. Complete inhibition of RdRp activity in vitro was observed at equimolar concentrations of NS5B and mAb 5B-12B7, whereas RdRp activities of classica…

virusesHepatitis C virusMolecular Sequence DataBiologyViral Nonstructural Proteinsmedicine.disease_causeBiochemistryAntiviral AgentsViruschemistry.chemical_compoundMiceRNA polymerasemedicineAnimalsAmino Acid SequenceMolecular BiologyNS5BImmunoglobulin FragmentsPolymeraseSubgenomic mRNAMice Inbred BALB CBase Sequencevirus diseasesRNAAntibodies MonoclonalCell BiologyVirologyMolecular biologydigestive system diseasesEpitope mappingchemistrybiology.proteinFemaleEpitope MappingThe Journal of biological chemistry
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Viral and cellular determinants of hepatitis C virus RNA replication in cell culture.

2003

Studies on the replication of hepatitis C virus (HCV) have been facilitated by the development of selectable subgenomic replicons replicating in the human hepatoma cell line Huh-7 at a surprisingly high level. Analysis of the replicon population in selected cells revealed the occurrence of cell culture-adaptive mutations that enhance RNA replication substantially. To gain a better understanding of HCV cell culture adaptation, we characterized conserved mutations identified by sequence analysis of 26 independent replicon cell clones for their effect on RNA replication. Mutations enhancing replication were found in nearly every nonstructural (NS) protein, and they could be subdivided into at …

virusesImmunologyCell Culture TechniquesReplicationRNA-dependent RNA polymeraseEukaryotic DNA replicationHepacivirusViral Nonstructural ProteinsBiologyVirus ReplicationOrigin of replicationMicrobiologyReplication factor CControl of chromosome duplicationVirologyTumor Cells Cultured[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular BiologyHumansRepliconVirologyAmino Acid SubstitutionViral replicationInsect ScienceRNA ViralOrigin recognition complexRepliconRibosomes
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Biochemical properties of hepatitis C virus NS5B RNA-dependent RNA polymerase and identification of amino acid sequence motifs essential for enzymati…

1997

The NS5B protein of the hepatitis C virus (HCV) is an RNA-dependent RNA polymerase (RdRp) (S.-E. Behrens, L. Tomei, and R. De Francesco, EMBO J. 15:12-22, 1996) that is assumed to be required for replication of the viral genome. To further study the biochemical and structural properties of this enzyme, an NS5B-hexahistidine fusion protein was expressed with recombinant baculoviruses in insect cells and purified to near homogeneity. The enzyme was found to have a primer-dependent RdRp activity that was able to copy a complete in vitro-transcribed HCV genome in the absence of additional viral or cellular factors. Filter binding assays and competition experiments showed that the purified enzym…

virusesImmunologyMolecular Sequence DataRNA-dependent RNA polymeraseSequence alignmentRNA-binding proteinHepacivirusViral Nonstructural ProteinsMicrobiologychemistry.chemical_compoundStructure-Activity RelationshipVirologyRNA polymeraseNS5BPeptide sequencePolymerasebiologyBase SequenceSequence Homology Amino AcidRNARNA-Binding ProteinsTemplates GeneticRNA-Dependent RNA PolymeraseMolecular biologyRecombinant ProteinschemistryAmino Acid SubstitutionInsect Sciencebiology.proteinRNA ViralSequence AlignmentResearch Article
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Impact of VP1-Specific Protein Sequence Motifs on Adeno-Associated Virus Type 2 Intracellular Trafficking and Nuclear Entry

2012

ABSTRACT Adeno-associated virus type 2 (AAV2) has gained much interest as a gene delivery vector. A hallmark of AAV2-mediated gene transfer is an intracellular conformational change of the virus capsid, leading to the exposure of infection-relevant protein domains. These protein domains, which are located on the N-terminal portion of the structural proteins VP1 and VP2, include a catalytic phospholipase A 2 domain and three clusters of basic amino acids. We have identified additional protein sequence motifs located on the VP1/2 N terminus that also proved to be obligatory for virus infectivity. These motifs include signals that are known to be involved in protein interaction, endosomal sort…

virusesImmunologyProtein domainAmino Acid MotifsMolecular Sequence DataSequence alignmentBiologyMicrobiologyVirusCell LineParvoviridae InfectionsVirologyHumansAmino Acid SequenceAdeno-Associated Virus Type 2Peptide sequenceCell NucleusDependovirusMolecular biologyTransport proteinCell biologyVirus-Cell InteractionsProtein TransportCapsidInsect ScienceCapsid ProteinsSequence motifSequence Alignment
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Lipid Binding Controls Dimerization of the Coat Protein p24 Transmembrane Helix

2019

Abstract Coat protein (COP) I and COP II complexes are involved in the transport of proteins between the endoplasmic reticulum and the Golgi apparatus in eukaryotic cells. The formation of COP I/II complexes at membrane surfaces is an early step in vesicle formation and is mastered by p24, a type I transmembrane protein. Oligomerization of p24 monomers was suggested to be mediated and/or stabilized via interactions within the transmembrane domain, and the p24 transmembrane helix appears to selectively bind a single sphingomyelin C18:0 molecule. Furthermore, a potential cholesterol-binding sequence has also been predicted in the p24 transmembrane domain. Thus, sphingomyelin and/or cholestero…

virusesLipid BilayersBiophysicsProtein Structure Secondary03 medical and health sciencessymbols.namesake0302 clinical medicineimmune system diseasesAmino Acid Sequence030304 developmental biology0303 health sciencesChemistryEndoplasmic reticulumVesicleCholesterol bindingvirus diseasesArticlesCOPIGolgi apparatusLipidsTransmembrane proteinSphingomyelinsTransmembrane domainCholesterolsymbolsBiophysicsCapsid Proteinslipids (amino acids peptides and proteins)SphingomyelinDimerization030217 neurology & neurosurgeryBiophysical Journal
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In vitro studies on the activation of the hepatitis C virus NS3 proteinase by the NS4A cofactor.

1996

AbstractProteolytic processing of the nonstructural proteins of the hepatitis C virus (HCV) is mediated by two viral proteinases: the NS2-3 proteinase cleaving at the NS2/3 junction and the NS3 serine-type proteinase responsible for processing at the NS3/4A, NS4A/B, NS4B/5A, and NS5A/B sites. Activity of the NS3 proteinase is modulated by NS4A. In the absence of this cofactor processing at the NS3-dependent sites does not occur or, in the case of the NS5A/B junction, is poor but increased when NS4A is present. Although recent studies demonstrated that proteinase activation requires direct interaction between NS3 and NS4A, the mechanism by which NS4A exerts the activation function is not kno…

virusesMolecular Sequence DataHepacivirusBiologyViral Nonstructural ProteinsCell LineEnzyme activatorProteinase 3VirologyCricetinaeMicrosomesAnimalsHumansAmino Acid SequenceBinding siteNS5APeptide sequenceSequence Deletionchemistry.chemical_classificationNS3Binding SitesBase Sequencevirus diseasesIntracellular Membranesbiochemical phenomena metabolism and nutritionMolecular biologyIn vitrodigestive system diseasesAmino acidEnzyme ActivationBiochemistrychemistryDNA ViralPeptidesHeLa CellsVirology
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Genome sequence of SeIV-1, a novel virus from the Iflaviridae family infective to Spodoptera exigua

2011

Analysis of the transcriptome of Spodoptera exigua larvae revealed the presence of several ESTs with homology to virus of the order Picornavirales and with the highest similarity to Infectious flacherie virus (Iflaviridae) that infects Bombyx mori larvae. Iflaviridae is a recently defined family of insect-infecting viruses that consist of positive single strand RNA genomes translated into a single polyprotein of around 3000 amino acids long. Using the sequence information derived from the obtained ESTs, we have completed the genomic sequence of this virus. The novel S. exigua iflavirus (SeIV-1) has a genome of 10.3 kb and codes for a 3222 aa polyprotein. Expression analysis has revealed the…

virusesMolecular Sequence DataInsect VirusesSpodopteraSpodopteraGenomeVirusRNA Virus InfectionsExiguaAnimalsRNA VirusesAmino Acid SequencePest Control BiologicalEcology Evolution Behavior and SystematicsExpressed Sequence TagsViral Structural ProteinsGeneticsInfectivityGenomebiologyfungibiology.organism_classificationVirologyIntestinesIflaviridaeNovel virusHost-Pathogen InteractionsRNA ViralPicornaviralesJournal of Invertebrate Pathology
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