Opere di Francesco Berni.

Reprint of the 1864 ed. published by G. Daelli, Milan, which was issued as v. 44-45 of Biblioteca rara.

Francesco Berni,

Mode of access: Internet.

Ariosto, Berni, satirici e burleschi del secolo XVI.

Edited by Andrea Rubbi.

Il mondo cavalleresco in Boiardo, Ariosto, Berni.

"Bibliografia": p. [vii]-viii.

Orlando innamorato di Matteo M. Bojardo,

Mode of access: Internet.

Orlando innamorato /

"Vita di Francesco Berni tratta dagli scrittori d'italia delconte Giammaria Mazzuchelli": v.1, p. v-xxxvi.

Ventisei lettere famigliari.

Mode of access: Internet.

Ancora le poesie latine di Francesco Berni.

Author's autograph presentation copy.

Orlando innamorato di Matteo Ma. Bojardo rifatto da Francesco Berni : tomo I.

Mode of access: Internet.

Orlando innamorato di Matteo Ma. Bojardo rifatto da Francesco Berni : tomo II.

Mode of access: Internet.

Orlando innamorato di Matteo Ma. Bojardo rifatto da Francesco Berni : tomo III.

Mode of access: Internet.

Orlando innamorato di Matteo Ma. Bojardo rifatto da Francesco Berni : tomo IV.

Mode of access: Internet.

Orlando innamorato di Matteo Ma. Bojardo rifatto da Francesco Berni : tomo V.

Mode of access: Internet.

Targeted deletion of alkylpurine-DNA-N-glycosylase in mice eliminates repair of 1,N6-ethenoadenine and hypoxanthine but not of 3,N4-ethenocytosine or 8-oxoguanine

It has previously been reported that 1,N6-ethenoadenine (ɛA), deaminated adenine (hypoxanthine, Hx), and 7,8-dihydro-8-oxoguanine (8-oxoG), but not 3,N4-ethenocytosine (ɛC), are released from DNA in vitro by the DNA repair enzyme alkylpurine-DNA-N-glycosylase (APNG). To assess the potential contribution of APNG to the repair of each of these mutagenic lesions in vivo, we have used cell-free extracts of tissues from APNG-null mutant mice and wild-type controls. The ability of these extracts to cleave defined oligomers containing a single modified base was determined. The results showed that both testes and liver cells of these knockout mice completely lacked activity toward oligonucleotides containing ɛA and Hx, but retained wild-type levels of activity for ɛC and 8-oxoG. These findings indicate that (i) the previously identified ɛA-DNA glycosylase and Hx-DNA glycosylase activities are functions of APNG; (ii) the two structurally closely related mutagenic adducts ɛA and ɛC are repaired by separate gene products; and (iii) APNG does not contribute detectably to the repair of 8-oxoG.