0000000000409674

AUTHOR

Roberto Bruzzone

showing 2 related works from this author

Antiviral Properties of Chemical Inhibitors of Cellular Anti-Apoptotic Bcl-2 Proteins

2017

Viral diseases remain serious threats to public health because of the shortage of effective means of control. To combat the surge of viral diseases, new treatments are urgently needed. Here we show that small-molecules, which inhibit cellular anti-apoptotic Bcl-2 proteins (Bcl-2i), induced the premature death of cells infected with different RNA or DNA viruses, whereas, at the same concentrations, no toxicity was observed in mock-infected cells. Moreover, these compounds limited viral replication and spread. Surprisingly, Bcl-2i also induced the premature apoptosis of cells transfected with viral RNA or plasmid DNA but not of mock-transfected cells. These results suggest that Bcl-2i sensiti…

0301 basic medicinevirusesFAMILY INHIBITORSlcsh:QR1-502Virus Replicationlcsh:Microbiologychemistry.chemical_compoundTranscription (biology)SALIPHENYLHALAMIDEhost responseTRANSCRIPTIONprogrammed cell deathinnate immunity1183 Plant biology microbiology virologySulfonamidesAniline CompoundsapoptosisTransfection3. Good healthInfectious DiseasesProto-Oncogene Proteins c-bcl-2X-L INHIBITORVirus DiseasesvirustauditVirusesRNA ViralBiologyTransfectionta3111Antiviral AgentsArticleCell LineMicrobiology in the medical areaantiviral agent03 medical and health sciencesohjelmoitunut solukuolemaVirologyMikrobiologi inom det medicinska områdetHumansMetabolomicsBenzothiazolesInnate immune systemapoptosis; antiviral agent; innate immunity; host responseZIKA VIRUS-INFECTIONCHRONIC LYMPHOCYTIC-LEUKEMIAPOTENTta1183INFLUENZA-Ata1182RNAIsoquinolinesVirology030104 developmental biologyViral replicationchemistryCell cultureApoptosisCELLSREPLICATIONDNA Viral3111 BiomedicineDNA
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Identification and functional expression of HCx31.9, a novel gap junction gene

2002

By combining in silico and bench molecular biology methods we have identified a novel human gap junction gene that encodes a protein designated HCx31.9. We have determined its human chromosomal location and gene structure, and we have identified a putative mouse ortholog, mCx30.2. We have observed the presence of HCx31.9 in human cerebral cortex, liver, heart, spleen, lung, and kidney and the presence of mCx30.2 in mouse cerebral cortex, liver and lung. Moreover, preliminary data on the electrophysiological properties of HCx31.9 have been obtained by functional expression in paired Xenopus oocytes and in transfected N2A cells.

Patch-Clamp TechniquesIn silicoMolecular Sequence DataClinical BiochemistryXenopuscloningGene ExpressionConnexinConnexinsCell Linegap junctionMiceXenopus laevisGene expressionmedicineAnimalsHumansTissue DistributionAmino Acid SequenceCloning MolecularGenePhylogenybiologycloning; CNS; gap junctionGap junctionGap JunctionsCell BiologyGeneral MedicineTransfectionbiology.organism_classificationMolecular biologymedicine.anatomical_structureCerebral cortexOocytesCNSSequence Alignment
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