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Globler, J.A., Stillmock, K., Hu, B., Witmer, M., Felock, P., Espeseth, A.S., Wolfe, A., Egbertson, M., Bourgeois, M., Melamed, J., Wai, J.S., Young, S., Vacca, J. and Hazuda, D.J. (2002) Diketo acid inhibitor mechanism and HIV-1 integrase? Implications for metal binding in the active site of phosphotransferase enzymes. Proceedings of the National Academy of Sciences, 99, 6661-6666. doi:10.1073/pnas.092056199

has been cited by the following article:

• TITLE: A quantum-chemical model of the inhibition mechanismof viral DNA HIV-1 replication by Iodine complexcompounds

  AUTHORS: Gulnara A. Yuldasheva, Georgii M. Zhidomirov, Aleksandr I. Ilin

  KEYWORDS: HIV; Integrase HIV; Quantum-Chemical Method Ab Initio

  JOURNAL NAME: Natural Science, Vol.3 No.7, July 27, 2011

  ABSTRACT: The interaction of molecular iodine with virus DNA nucleotide is studied by ab initio RHF/3-21G** method. Formation of the nucleoprotein complex of the HIV DNA, molecular iodine and the HIV-1 integrase co-factor is considered to cause the inhibition action of the integrase enzyme. Experimental data on the anti-HIV effect of the molecular iodine complex compounds and the results of calculations suggest that molecular iodine contained in iodine polymer complexes may be considered as a compound inhibiting the catalytic center of the integrase enzyme. Unlike the known integrase inhibitors, molecular iodine also changes the virus DNA structure and produces the N-I bond in the purine bases of adenosine and guanosine nucleotides.