Herpes simplex virus type 1 (HSV-1) uracil-DNA glycosylase: functional expression in Escherichia coli, biochemical characterization, and selective inhibition by 6-(p-n-octylanilino)uracil. (Articolo in rivista)

Type

• Prodotto della ricerca (Classe)
• Articolo in rivista (Classe)

Label

• Herpes simplex virus type 1 (HSV-1) uracil-DNA glycosylase: functional expression in Escherichia coli, biochemical characterization, and selective inhibition by 6-(p-n-octylanilino)uracil. (Articolo in rivista) (literal)

Anno

• 1995-01-01T00:00:00+01:00 (literal)

Alternative label

• Argnani R, Focher F, Zucchini S, Verri A, Wright GE, Spadari S, Manservigi R. (1995)
  Herpes simplex virus type 1 (HSV-1) uracil-DNA glycosylase: functional expression in Escherichia coli, biochemical characterization, and selective inhibition by 6-(p-n-octylanilino)uracil.
  in Virology (N.Y.N.Y., Print)
  (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

• Argnani R, Focher F, Zucchini S, Verri A, Wright GE, Spadari S, Manservigi R. (literal)

Pagina inizio

• 307 (literal)

Pagina fine

• 311 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

• 211 (literal)

Rivista

• Virology (Rivista)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo

• 1 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni

• Institute of Microbiology, University of Ferrara, Italy. Isituto di Genetica Molecolare, CNR Pavia (literal)

Titolo

• Herpes simplex virus type 1 (HSV-1) uracil-DNA glycosylase: functional expression in Escherichia coli, biochemical characterization, and selective inhibition by 6-(p-n-octylanilino)uracil. (literal)

Abstract

• The Herpes simplex virus type 1 (HSV-1) uracil-DNA glycosylase (UDG) is encoded by the UL2 gene. The translation from the first putative start codon of UL2 predicts a polypeptide of 334 residues, while the translation from the second start codon predicts a polypeptide of 244 residues. We have cloned and expressed the two forms of UDG, by means of the prokaryotic expression vector pMAL-c2, and both of them were enzymatically active. Furthermore, the enzymatic properties of the recombinant UDGs and of the enzyme purified from HSV-1-infected cells were similar. The two UDG polypeptides have molecular weights of 27 and 37 kDa, respectively. The 37-kDa form of recombinant UDG is consistent with the reported molecular mass of 37 kDa for the enzyme purified from HSV-1-infected cells. Both recombinant UDGs were as sensitive as UDG purified from HSV-1-infected cells to 6-(p-n-octylanilino)uracil, the most potent of a series of uracil analogs that inhibit the viral enzyme. (literal)

Prodotto di

• Institute of molecular genetics (IGM) (Istituto)

Autore CNR

• SILVIO SPADARI (Unità di personale interno)
• FEDERICO FOCHER (Unità di personale interno)

Incoming links:

Prodotto

• Institute of molecular genetics (IGM) (Istituto)

Autore CNR di

• FEDERICO FOCHER (Unità di personale interno)
• SILVIO SPADARI (Unità di personale interno)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi

• Virology (Rivista)