Search results for "Binding."

showing 10 items of 3621 documents

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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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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The Extracellular δ-Domain is Essential for the Formation of CD81 Tetraspanin Webs

2014

AbstractCD81 is a ubiquitously expressed member of the tetraspanin family. It forms large molecular platforms, so-called tetraspanin webs that play physiological roles in a variety of cellular functions and are involved in viral and parasite infections. We have investigated which part of the CD81 molecule is required for the formation of domains in the cell membranes of T-cells and hepatocytes. Surprisingly, we find that large CD81 platforms assemble via the short extracellular δ-domain, independent from a strong primary partner binding and from weak interactions mediated by palmitoylation. The δ-domain is also essential for the platforms to function during viral entry. We propose that, ins…

virusesLipoylationBiophysicschemical and pharmacologic phenomenaPlasma protein bindingBiologyTetraspanin 28Jurkat CellsProtein structurePalmitoylationTetraspaninViral entryExtracellularHumansComputingMilieux_MISCELLANEOUS[PHYS]Physics [physics]MembranesHep G2 Cellsbiochemical phenomena metabolism and nutritionCell biologyProtein Structure TertiaryProtein MultimerizationProtein Processing Post-TranslationalFunction (biology)CD81Protein Binding
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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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Characterization of the autoantigen La (SS-B) as a dsRNA unwinding enzyme

1997

During the analysis of the La (SS-B) autoantigen for catalytic activities an ATP-dependent double-stranded RNA unwinding activity was detected. Both native and recombinant La proteins from different species displayed this activity, which could be inhibited by monospecific anti-La antibodies. La protein was able to melt dsRNA substrates with either two 3'-overhangs or a single 3'- and a 5'-overhang. Double-stranded RNAs with two 5'-overhangs were not unwound, indicating that at least one 3'-overhang is required for unwinding. Sequence elements of the La protein that might be involved in dsRNA unwinding, such as an evolutionarily conserved putative ATP-binding motif and an element that is hom…

virusesgenetic processesGene ExpressionRNA-binding proteinBiologyAutoantigensAntibodiesSubstrate SpecificitySingle-stranded binding proteinlaw.inventionMiceAdenosine TriphosphatelawGene expressionEscherichia coliGeneticsAnimalsHumansGeneralLiterature_REFERENCE(e.g.dictionariesencyclopediasglossaries)Cells CulturedRNA Double-StrandedRibonucleoproteinRNARNA NucleotidyltransferasesProtein kinase RMolecular biologyRecombinant ProteinsRatsenzymes and coenzymes (carbohydrates)RNA silencingLiverRibonucleoproteinsbiology.proteinRecombinant DNAElectrophoresis Polyacrylamide GelRNA HelicasesResearch Article
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Tumor targeting of baculovirus displaying a lymphatic homing peptide.

2008

Background Tumor-associated cells and vasculature express attractive molecular markers for site-specific vector targeting. To attain tumor-selective tropism, we recently developed a baculovirus vector displaying the lymphatic homing peptide LyP-1, originally identified by ex vivo/in vivo screening of phage display libraries, on the viral envelope by fusion to the transmembrane anchor of vesicular stomatitis virus G-protein. Methods In the present study, we explored the specificity and kinetics of viral binding and internalization as well as in vivo tumor homing of the LyP-1 displaying virus to elucidate the applicability of baculovirus for targeted therapies. Results We demonstrated that th…

virusesmedia_common.quotation_subjectGenetic VectorsMice NudeBiologyPeptides CyclicVirus03 medical and health sciencesTransduction (genetics)Mice0302 clinical medicineViral envelopeViral Envelope ProteinsIn vivoTransduction GeneticCell Line TumorNeoplasmsDrug DiscoveryGeneticsAnimalsHumansTransgenesInternalizationMolecular BiologyGenetics (clinical)030304 developmental biologymedia_commonLymphatic Vessels0303 health sciencesBinding SitesMembrane GlycoproteinsGene Transfer TechniquesGenetic Therapybiology.organism_classificationMolecular biology3. Good healthCell biologyVesicular stomatitis virus030220 oncology & carcinogenesisMolecular MedicineBaculoviridaeEx vivoHoming (hematopoietic)The journal of gene medicine
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Highly sensitive olfactory biosensors for the detection of volatile organic compounds by surface plasmon resonance imaging

2018

International audience; Nowadays, monitoring of volatile organic compounds (VOCs) is very important in various domains. In this work, we aimed to develop sensitive olfactory biosensors using odorant binding proteins (OBPs) as sensing materials. Three rat OBP3 derivatives with customized binding properties were designed and immobilized on the same chip for the detection of VOCs in solution by surface plasmon resonance imaging (SPRi). We demonstrated that the proteins kept their binding properties after the immobilization under optimized conditions. The obtained olfactory biosensors exhibited very low limits of detection in both concentration (200pM of beta-ionone) and in molecular weight of …

volatile organic compoundConformational change[SDV.BIO]Life Sciences [q-bio]/BiotechnologyOdorant bindingBiomedical EngineeringBiophysicsBiosensing Techniques02 engineering and technologyReceptors Odorant01 natural sciencesHexanal[SPI]Engineering Sciences [physics]chemistry.chemical_compoundElectrochemistryAnimalsVolatile organic compoundComputingMilieux_MISCELLANEOUSDetection limitchemistry.chemical_classificationVolatile Organic CompoundsChromatographyChemistry010401 analytical chemistryGeneral MedicineRepeatabilitySurface Plasmon Resonance021001 nanoscience & nanotechnologyRats0104 chemical sciencesSmellsurface plasmon resonance imagingofactory biosensor0210 nano-technologySelectivityBiosensorodorant binding proteinsBiotechnologyBiosensors and Bioelectronics
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Conservation of the positions of metazoan introns from sponges to humans

2002

Abstract Sponges (phylum Porifera) are the phylogenetic oldest Metazoa still extant. They can be considered as reference animals (Urmetazoa) for the understanding of the evolutionary processes resulting in the creation of Metazoa in general and also for the metazoan gene organization in particular. In the marine sponge Suberites domuncula , genes encoding p38 and JNK kinases contain nine and twelve introns, respectively. Eight introns in both genes share the same positions and the identical phases. One p38 intron slipped for six bases and the JNK gene has three more introns. However, the sequences of the introns are not conserved and the introns in JNK gene are generally much longer. Intron…

xMolecular Sequence Datap38 Mitogen-Activated Protein KinasesExonGene duplicationGeneticsAnimalsHumansCoding regionGroup I catalytic intronAmino Acid SequenceGeneConserved SequencePhylogenyCaenorhabditis elegansGeneticsBase SequenceSequence Homology Amino AcidbiologyCalcium-Binding ProteinsMicrofilament ProteinsJNK Mitogen-Activated Protein KinasesIntronDNASequence Analysis DNAGeneral MedicineGroup II intronbiology.organism_classificationIntronsPoriferaDNA-Binding ProteinsMitogen-Activated Protein KinasesSequence AlignmentGene
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XPS structural data and correlation with Mossbauer spectra for Tin-organic compounds: adducts of RnSnCl4-n with 1,2-bis(diphenylphosphino)ethane

1982

Abstract Core level X-ray photoelectron spectra of 1:1 adducts of SnCl4 and RSnCl3 with DPE {[RnSnCl4−n} · DPE (n = 1, R = Me, Bun, Octn, Phn; n = 2, R = Ph; DPE = 1,2-bis(diphenylphosphino)ethane], have been measured in solid phase. The Sn3d 5 2 binding energies, corrected for the Madelung potential at the metal atom, are well correlated with both partial atomic charge on tin, accounting for relaxation upon ionization, and 119Sn Mossbauer isomer shifts. The results are discussed in terms of these molecular parameters.

xpBinding energyAnalytical chemistrychemistry.chemical_elementAdductInorganic ChemistryMossbauerchemistry.chemical_compound12-Bis(diphenylphosphino)ethanechemistryX-ray photoelectron spectroscopyIonizationcorrelationAtomMössbauer spectroscopyMaterials ChemistryPhysical chemistryPhysical and Theoretical ChemistryTin
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Rücktitelbild: Water Structure Recovery in Chaotropic Anion Recognition: High-Affinity Binding of Dodecaborate Clusters to γ-Cyclodextrin (Angew. Che…

2015

γ cyclodextrinChaotropic agentHigh affinity bindingChemistryDodecaboratePolymer chemistryGeneral MedicineIonAngewandte Chemie
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