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Mechanism of interaction of novel indolylarylsulfone derivatives with K103N and Y181I mutant HIV-1 reverse transcriptase in complex with its substrates.
Antivir Chem Chemother. 2011 Nov 17;22(3):107-18. doi: 10.3851/IMP1855.
Antivir Chem Chemother. 2011.
PMID: 22095519
Free article.
Non-nucleoside HIV-1 reverse transcriptase inhibitors di-halo-indolyl aryl sulfones achieve tight binding to drug-resistant mutants by targeting the enzyme-substrate complex.
Samuele A, Kataropoulou A, Viola M, Zanoli S, La Regina G, Piscitelli F, Silvestri R, Maga G.
Samuele A, et al. Among authors: kataropoulou a.
Antiviral Res. 2009 Jan;81(1):47-55. doi: 10.1016/j.antiviral.2008.09.008. Epub 2008 Nov 5.
Antiviral Res. 2009.
PMID: 18984007
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Mutational analysis of the HIV-1 auxiliary protein Vif identifies independent domains important for the physical and functional interaction with HIV-1 reverse transcriptase.
Kataropoulou A, Bovolenta C, Belfiore A, Trabatti S, Garbelli A, Porcellini S, Lupo R, Maga G.
Kataropoulou A, et al.
Nucleic Acids Res. 2009 Jun;37(11):3660-9. doi: 10.1093/nar/gkp226. Epub 2009 Apr 15.
Nucleic Acids Res. 2009.
PMID: 19369217
Free PMC article.
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Mutational analysis of the HIV-1 auxiliary protein Vif identifies independent domains important for the physical and functional interaction with HIV-1 reverse transcriptase.
Kataropoulou A, Bovolenta C, Belfiore A, Trabatti S, Garbelli A, Porcellini S, Lupo R, Maga G.
Kataropoulou A, et al.
Nucleic Acids Res. 2014 Apr;42(6):4144. doi: 10.1093/nar/gku195. Epub 2014 Mar 13.
Nucleic Acids Res. 2014.
PMID: 24627181
Free PMC article.
No abstract available.
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