@prefix prodottidellaricerca: . @prefix istituto: . @prefix prodotto: . istituto:CDS040 prodottidellaricerca:prodotto prodotto:ID27448 . @prefix pubblicazioni: . @prefix unitaDiPersonaleInterno: . unitaDiPersonaleInterno:MATRICOLA8735 pubblicazioni:autoreCNRDi prodotto:ID27448 . @prefix unitaDiPersonaleEsterno: . unitaDiPersonaleEsterno:ID4502 pubblicazioni:autoreCNRDi prodotto:ID27448 . @prefix modulo: . modulo:ID2691 prodottidellaricerca:prodotto prodotto:ID27448 . @prefix rdf: . @prefix retescientifica: . prodotto:ID27448 rdf:type retescientifica:ProdottoDellaRicerca , prodotto:TIPO1101 . @prefix rdfs: . prodotto:ID27448 rdfs:label "The balance between the rates of incorporation and pyrophosphorolytic removal influences the HIV-1 reverse transcriptase bypass of an abasic site with deoxy-, dideoxy-, and ribonucleotides. (Articolo in rivista)"@en . @prefix xsd: . prodotto:ID27448 pubblicazioni:anno "2008-01-01T00:00:00+01:00"^^xsd:gYear . @prefix skos: . prodotto:ID27448 skos:altLabel "
Sharma B, Crespan E, Villani G, Maga G. (2008)
The balance between the rates of incorporation and pyrophosphorolytic removal influences the HIV-1 reverse transcriptase bypass of an abasic site with deoxy-, dideoxy-, and ribonucleotides.
in Proteins (Print)
"^^rdf:HTML ; pubblicazioni:autori "Sharma B, Crespan E, Villani G, Maga G."^^xsd:string ; pubblicazioni:paginaInizio "715"^^xsd:string ; pubblicazioni:paginaFine "727"^^xsd:string ; pubblicazioni:numeroVolume "71"^^xsd:string . @prefix ns12: . prodotto:ID27448 pubblicazioni:rivista ns12:ID477130 ; skos:note "ISI Web of Science (WOS)"^^xsd:string ; pubblicazioni:affiliazioni "Crespan E, Maga G: IGM-CNR; Sharma B: University of Allahabad, Allahabad, India; Villani G: IPBS-CNRS, Toulouse, France."^^xsd:string ; pubblicazioni:titolo "The balance between the rates of incorporation and pyrophosphorolytic removal influences the HIV-1 reverse transcriptase bypass of an abasic site with deoxy-, dideoxy-, and ribonucleotides."^^xsd:string ; prodottidellaricerca:abstract "Abasic (AP) sites pose a potential danger to HIV-1 replication. HIV-1 RT has been shown to preferentially incorporate purines opposite an AP site, and subsequently extend from the lesion. While it is clear that AP sites are bypassed inefficiently and are major sites of RT pausing, detailed kinetic analysis of the relative contributions of both the incorporation and the pyrophosphorolytic reactions in translesion synthesis by HIV-RT is still lacking. Investigation of the molecular basis of these processes is important, in light of the fact that HIV-1 RT is the major target for anti-HIV chemotherapy, and its low fidelity is an essential determinant of the extraordinary genetic variability of HIV-1, which is important for the appearance of mutant viruses resistant to chemotherapy. Here, we analyzed the effects of the presence of an AP site on the template strand on the catalytic properties of the DNA-dependent polymerization reaction as well as on the phosphorolytic activity of HIV-1 RT, in the presence of deoxy-, dideoxy,- and ribonucleotides. We find that AP sites can substantially influence the substrate specificity of HIV-1 RT and that pyrophosphorolysis plays a significant role in determining the ability of HIV-1 RT to (mis)incorporate nucleotides." ; prodottidellaricerca:prodottoDi istituto:CDS040 , modulo:ID2691 ; pubblicazioni:autoreCNR unitaDiPersonaleEsterno:ID4502 , unitaDiPersonaleInterno:MATRICOLA8735 . @prefix parolechiave: . prodotto:ID27448 parolechiave:insiemeDiParoleChiave . ns12:ID477130 pubblicazioni:rivistaDi prodotto:ID27448 . parolechiave:insiemeDiParoleChiaveDi prodotto:ID27448 .