Search results for "Avian Sarcoma Viruses"

showing 3 items of 3 documents

Bleomycin: Action on growth of oncogenic RNA viruses and on cell transformation

1975

Bleomycin (BLM) inhibits cell proliferation of noninfected chick embryo fibroblasts by blocking their DNA synthesis selectively. Chick embryo fibroblasts have beentransformed by Schmidt-Ruppin D strain of Rous Sarcoma Virus. Transformation has been determined by a focus assay. Foci formation is strongly reduced by BLM. Virus replication is inhibited by BLM in growing and confluent monolayer cells. This result might be explained by the observation that this drug reduces proliferation of growing and of confluent monolayer cells very sensitively. During the first 24 hours after infection the BLM inhibitory effect is more pronounced than in the case of BLM-application during the period 24--48 h…

congenital hereditary and neonatal diseases and abnormalitiesTime Factorsanimal structuresTranscription GeneticCell divisionCellChick EmbryoBiologyVirus ReplicationVirusBleomycinTranscription (biology)VirologymedicineAnimalsRNA VirusesCells CulturedRous sarcoma virusurogenital systemCell growthnutritional and metabolic diseasesRNADNAGeneral MedicineFibroblastsbiology.organism_classificationVirologyMolecular biologyCell Transformation Neoplasticmedicine.anatomical_structureAvian Sarcoma VirusesViral replicationembryonic structuresRNARNA ViralArchives of Virology
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Roles of a conserved proline in the internal fusion peptide of Ebola glycoprotein

2004

AbstractThe structural determinants underlying the functionality of viral internal fusion peptides (IFPs) are not well understood. We have compared EBOwt (GAAIGLAWIPYFGPAAE), representing the IFP of the Ebola fusion protein GP, and EBOmut (GAAIGLAWIPYFGRAAE) derived from a non-functional mutant with conserved Pro537 substituted by Arg. P537R substitution did not abrogate peptide-membrane association, but interfered with the ability to induce bilayer destabilization. Structural determinations suggest that Pro537 is required to preserve a membrane-perturbing local conformation in apolar environments.

Circular dichroismEbola glycoproteinProtein insertion into membranesProlinePeptide conformationMutantMolecular Sequence DataBiophysicsBiochemistrySendai viruschemistry.chemical_compoundStructural BiologyGeneticsProlineAmino Acid SequenceMolecular BiologyPeptide sequencePOPCchemistry.chemical_classificationChemistryProteïnes de membranaCell BiologyEbolavirusFusion proteinPeptide FragmentsPeptide ConformationViral fusion peptideBiochemistryAvian Sarcoma VirusesLiposomesHIV-1PèptidsGlycoproteinPeptide–lipid interactionViral Fusion ProteinsFEBS Letters
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Arabinose nucleoside triphosphates are no inhibitors for DNA-dependent RNA polymerases.

1976

1-Beta-D-arabinofuranosylcytosine-5' -triphosphate and 9-beta-D-arabinofuranosyladenosine-5' -triphosphate were found to have no inhibitory potency for both mammalian DNA-dependent RNA polymerase II and E. coli DNA-dependent RNA polymerase.

RNA-dependent RNA polymeraseRNA polymerase IIOviductsCytosine NucleotidesQuailCellular and Molecular Neurosciencechemistry.chemical_compoundAdenosine TriphosphateTranscription (biology)RNA polymeraseRNA polymerase IEscherichia coliAnimalsMolecular BiologyPolymerasePharmacologybiologyChemistryMusclesCytarabineRNACell BiologyDNA-Directed RNA PolymerasesMolecular biologyKineticsAvian Sarcoma VirusesRNA editingbiology.proteinMolecular MedicineRNA Polymerase IIVidarabineExperientia
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