Search results for "PEPTIDES"

showing 7 items of 2897 documents

Internalization of novel non-viral vector TAT-streptavidin into human cells

2007

BMC Biotechnology, 7 (1)

virusesEndocytic cyclePROTEINS + POLYPEPTIDES (BIOCHEMISTRY)02 engineering and technologyei-virusperäinen vektoriProtein EngineeringgeeniterapiaPost Transductionchemistry.chemical_compoundTHERAPIES + THERAPEUTICS (MEDICINE)Drug Delivery SystemsLääketieteen bioteknologia - Medical biotechnologyInternalizationmedia_commoninfo:eu-repo/classification/ddc/5700303 health sciencesPinocytosisNocodazoleVEKTOREN (GENETISCHE TECHNIKEN)021001 nanoscience & nanotechnologyLife sciencesCell biologyEndosomal EscapeBiotinylationGene Products tatVirusesVECTORS (GENETIC TECHNIQUES)VEKTOREN (GENETISCHE TECHNIKEN); THERAPIEN + THERAPEUTIK (MEDIZIN); PROTEINE + POLYPEPTIDE (BIOCHEMIE); VECTORS (GENETIC TECHNIQUES); THERAPIES + THERAPEUTICS (MEDICINE); PROTEINS + POLYPEPTIDES (BIOCHEMISTRY)0210 nano-technologyTHERAPIEN + THERAPEUTIK (MEDIZIN)BiotechnologyResearch ArticleStreptavidinEndosomeImmunoelectron microscopymedia_common.quotation_subjectRecombinant Fusion Proteinslcsh:BiotechnologyGenetic VectorsBiologyEndocytosis03 medical and health sciencesstreptavidiiniddc:570lcsh:TP248.13-248.65HumansEndosomal Marker030304 developmental biologyMolecular biologyEndocytic VesiclechemistryStreptavidinTATPROTEINE + POLYPEPTIDE (BIOCHEMIE)HeLa CellsBMC Biotechnology
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Nuclear localization but not PML protein is required for incorporation of the papillomavirus minor capsid protein L2 into virus-like particles.

2004

ABSTRACT Recent reports suggest that nuclear domain(s) 10 (ND10) is the site of papillomavirus morphogenesis. The viral genome replicates in or close to ND10. In addition, the minor capsid protein, L2, accumulates in these subnuclear structures and recruits the major capsid protein, L1. We have now used cell lines deficient for promyelocytic leukemia (PML) protein, the main structural component of ND10, to study the role of this nuclear protein for L2 incorporation into virus-like particles (VLPs). L2 expressed in PML protein knockout (PML −/− ) cells accumulated in nuclear dots, which resemble L2 aggregates forming at ND10 in PML protein-containing cells. These L2 assemblies also attracted…

virusesImmunologyActive Transport Cell NucleusNuclear dotsBiologyPromyelocytic Leukemia ProteinMicrobiologyCell LinePromyelocytic leukemia proteinMiceDeath-associated protein 6Virus-like particleVirologymedicineAnimalsHumansNuclear proteinPapillomaviridaeAdaptor Proteins Signal TransducingCell NucleusTumor Suppressor ProteinsStructure and AssemblyIntracellular Signaling Peptides and ProteinsVirionvirus diseasesNuclear ProteinsOncogene Proteins Viralbiochemical phenomena metabolism and nutritionMolecular biologyCell biologyNeoplasm ProteinsCell nucleusMicroscopy Electronmedicine.anatomical_structureInsect ScienceMutationbiology.proteinCapsid ProteinsNuclear transportCarrier ProteinsCo-Repressor ProteinsNuclear localization sequenceMolecular ChaperonesTranscription FactorsJournal of virology
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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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Human Papillomavirus Type 16 E7 Peptide-Directed CD8+ T Cells from Patients with Cervical Cancer Are Cross-Reactive with the Coronavirus NS2 Protein

2003

ABSTRACTHuman papillomavirus type 16 (HPV16) E6 and E7 oncoproteins are required for cellular transformation and represent candidate targets for HPV-specific and major histocompatibility complex class I-restricted CD8+-T-cell responses in patients with cervical cancer. Recent evidence suggests that cross-reactivity represents the inherent nature of the T-cell repertoire. We identified HLA-A2 binding HPV16 E7 variant peptides from human, bacterial, or viral origin which are able to drive CD8+-T-cell responses directed against wild-type HPV16 E7 amino acid 11 to 19/20 (E711-19/20) epitope YMLDLQPET(T) in vitro. CD8+T cells reacting to the HLA-A2-presented peptide from HPV16 E711-19(20)recogni…

virusesPapillomavirus E7 ProteinsImmunologyMolecular Sequence DataPriming (immunology)Epitopes T-LymphocyteUterine Cervical NeoplasmsCD8-Positive T-LymphocytesCross ReactionsViral Nonstructural Proteinsmedicine.disease_causeMajor histocompatibility complexLymphocyte ActivationMicrobiologyEpitopeImmune systemVirologyHLA-A2 AntigenmedicineCytotoxic T cellHumansHuman coronavirus OC43Amino Acid SequencePapillomaviridaeCoronavirusbiologyPapillomavirus Infectionsvirus diseasesOncogene Proteins Viralbiology.organism_classificationVirologyMolecular biologyCoronavirusTumor Virus InfectionsInsect Sciencebiology.proteinPathogenesis and ImmunityFemalePeptidesCD8Journal of Virology
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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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Characterization and antimicrobial activity of the volatile components of the flowers of Magydaris tomentosa (Desf.) DC. collected in Sicily and Alge…

2014

The essential oils of the flowers of Magydaris tomentosa (Desf.) DC. (Apiaceae) collected in Sicily (MSi) and Algeria (MAl), respectively, were obtained by hydrodistillation, and their compositions were analysed. The analyses allowed the identification and quantification of 23 components in MSi and 60 compounds in MAl, respectively, showing a very different profile in the composition of the two populations. The main components of MSi were cembrene (28.2%), α-springene (17.5%) and β-springene (14.8%), also present in MAl but in lesser amount (0.4%, 1.8% and 0.9%, respectively), whereas the principal constituents of MAl were (E)-nerolidol (35.4%), α-costol (13.3%) and β-costol (6.8%). Both MS…

β-springeneFlowersMicrobial Sensitivity TestsPlant ScienceBiochemistryMagydaris tomentosaGas Chromatography-Mass Spectrometryessential oilAnalytical ChemistryAnti-Infective Agentsα\-springeneStaphylococcus epidermidisparasitic diseasesOils VolatileMagydarisSicilyApiaceaeantimicrobial activitybiologyTraditional medicineOrganic ChemistrySettore CHIM/06 - Chimica Organicabiology.organism_classificationAntimicrobialαspringeneAnti-Bacterial AgentsPlant LeavesChemotaxonomyAlgerialipids (amino acids peptides and proteins)Composition (visual arts)DiterpenesAntibacterial activitySesquiterpenesApiaceae
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