prikaz prve stranice dokumenta Phosphorylation of aciclovir, ganciclovir, penciclovir and S2242 by the cytomegalovirus UL97 protein: a quantitative analysis using recombinant vaccinia virus
Pristup korisnicima matične ustanove
Znanstveni rad - Izvorni znanstveni rad
Phosphorylation of aciclovir, ganciclovir, penciclovir and S2242 by the cytomegalovirus UL97 protein: a quantitative analysis using recombinant vaccinia virus
Antiviral Research, 36 (1997), 1; 35-42. https://doi.org/10.1016/S0166-3542(97)00034-X
Zimmermann, Albert; Michel, Detlef; Pavić, Ivica; Hampl, Walter; Luske, Anke; Neyts, Johan; De Clercq, Erik; Mertens, Thomas

Citiranost:
,
Citirajte ovaj rad

Zimmermann, A., Michel, D., Pavić, I., Hampl, W., Luske, A., Neyts, J. ... Mertens, T. (1997). Phosphorylation of aciclovir, ganciclovir, penciclovir and S2242 by the cytomegalovirus UL97 protein: a quantitative analysis using recombinant vaccinia virus. Antiviral Research, 36. (1), 35-42. doi: 10.1016/S0166-3542(97)00034-X

Zimmermann, Albert, et al. "Phosphorylation of aciclovir, ganciclovir, penciclovir and S2242 by the cytomegalovirus UL97 protein: a quantitative analysis using recombinant vaccinia virus." Antiviral Research, vol. 36, br. 1, 1997, str. 35-42. https://doi.org/10.1016/S0166-3542(97)00034-X

Zimmermann, Albert, Detlef Michel, Ivica Pavić, Walter Hampl, Anke Luske, Johan Neyts, Erik De Clercq i Thomas Mertens. "Phosphorylation of aciclovir, ganciclovir, penciclovir and S2242 by the cytomegalovirus UL97 protein: a quantitative analysis using recombinant vaccinia virus." Antiviral Research 36, br. 1 (1997): 35-42. https://doi.org/10.1016/S0166-3542(97)00034-X

Zimmermann, A., et al. (1997) 'Phosphorylation of aciclovir, ganciclovir, penciclovir and S2242 by the cytomegalovirus UL97 protein: a quantitative analysis using recombinant vaccinia virus', Antiviral Research, 36(1), str. 35-42. doi: 10.1016/S0166-3542(97)00034-X

Zimmermann A, Michel D, Pavić I, Hampl W, Luske A, Neyts J, i sur.. Phosphorylation of aciclovir, ganciclovir, penciclovir and S2242 by the cytomegalovirus UL97 protein: a quantitative analysis using recombinant vaccinia virus. Antiviral Research [Internet]. 1997. [pristupljeno 04.03.2025.];36(1):35-42. doi: 10.1016/S0166-3542(97)00034-X

A. Zimmermann, et al., "Phosphorylation of aciclovir, ganciclovir, penciclovir and S2242 by the cytomegalovirus UL97 protein: a quantitative analysis using recombinant vaccinia virus", Antiviral Research, vol. 36, br. 1, str. 35-42, 1997. [Online]. Dostupno na: https://urn.nsk.hr/urn:nbn:hr:184:740874. [Citirano: 04.03.2025.]

Za citiranje koristite ovu mrežnu adresu: https://urn.nsk.hr/urn:nbn:hr:184:740874
Prijavite se u repozitorij kako biste mogli spremiti objekt u svoju listu.
Podaci o radu
Naslov (engleski)Phosphorylation of aciclovir, ganciclovir, penciclovir and S2242 by the cytomegalovirus UL97 protein: a quantitative analysis using recombinant vaccinia virus
AutorAlbert Zimmermann
AutorDetlef Michel
AutorIvica Pavić
AutorWalter Hampl
AutorAnke Luske
AutorJohan Neyts
AutorErik De Clercq
AutorThomas Mertens
Autorova ustanovaSveučilište u Rijeci
Medicinski fakultet
(Katedra za zarazne bolesti)
Znanstveno / umjetničko
područje, polje i grana		BIOMEDICINA I ZDRAVSTVO
Temeljne medicinske znanosti
Sažetak (engleski)
We used recombinant vaccinia viruses (rVV) containing the UL97 open reading frame (ORF) of the human cytomegalovirus (HCMV) to investigate the UL97-dependent phosphorylation of different nucleoside analogs. The rVV T1 expressed the wild-type UL97 protein whereas rVV A5 contained a 12 bp deletion in the UL97 which had been known to be responsible for resistance of HCMV to ganciclovir (GCV). The rVV T1opal was generated which contained a stop codon at position 1089 of the UL97 ORF and which... Više expressed a truncated UL97 protein. We quantitatively analyzed the capability of these rVVs to phosphorylate GCV, penciclovir (PCV), aciclovir (ACV) and 2-amino-7-[(1, 3-dihydroxy-2-propoxy)methyl] purine (S2242) as well as the natural nucleosides deoxycytidine and deoxythymidine. Moreover, we compared their phosphorylating capability with that of herpes simplex virus type 1 strains. In thymidine kinase (TK)-deficient 143B cells infected with rVV T1, the three compounds GCV, ACV and PCV were phosphorylated with different efficiency whereas in cells infected with the rVV A5 a markedly reduced but not completely abolished phosphorylation of these compounds was observed. In rVV T1opal-infected cells no specific phosphorylation of the compounds was detectable at all. Neither S2242 nor the natural substrates of TKs were phosphorylated by any of the vaccinia recombinants. The rVVs proved to be a suitable tool for analysis of UL97-dependent phosphorylation of nucleoside analogs and also allowed to quantitatively study the influence of UL97 mutations on drug phosphorylation. Sakrij dio sažetka
Ključne riječi (engleski)
Jezikengleski
Vrsta publikacijeZnanstveni rad - Izvorni znanstveni rad
Status objaveObjavljen
Vrsta recenzijeRecenziran - međunarodna recenzija
Verzija publikacijeObjavljena verzija rada (izdavačev PDF)
Naslov časopisaAntiviral Research
Brojčani podacivol. 36, br. 1, str. 35-42
p-ISSN0166-3542
DOIhttps://doi.org/10.1016/S0166-3542(97)00034-X
URN:NBNurn:nbn:hr:184:740874
Datum objave publikacije1997
URL dokumentahttp://bib.irb.hr/811823
Vrsta resursaTekst
Prava pristupaInstitucijski pristup
Uvjeti korištenjaIkona licence Zaštićeno autorskim pravom.
Datum i vrijeme pohrane2022-04-20 14:05:48
accessibility

closePristupačnostrefresh

Ako želite spremiti trajne postavke, kliknite Spremi, ako ne - vaše će se postavke poništiti kad zatvorite preglednik.