@article {Rausch:January 2007:1570-162X:11,
	author = "Rausch, Jason W.",
	author = "J Le Grice, Stuart F.",
	title = "Exploiting Structurally Diverse Nucleoside Analogs as Probes of Reverse Transcription Complexes",
	journal = "Current HIV Research",
	volume = "5",
	year = "January 2007",
	abstract = "The emergence of drug-resistant HIV-1 strains presents a challenge for the design of new drugs. Targeting host cell factors involved in the regulation of HIV-1 replication might be one way to overcome the resistance of HIV-1 to anti-viral agents. Our recent studies identified protein phosphatase-1 (PP1) as an important regulator of HIV-1 transcription. Transcription of HIV-1 genes is activated by HIV-1 Tat protein that induces phosphorylation of the Cterminal domain of RNA polymerase-II by CDK9/cyclin T1. We have shown that HIV-1 Tat binds PP1 in vitro; targets PP1 to the nucleus; and that Tat interaction with PP1 is important for HIV-1 transcription. In this review, we discuss two potential targets of PP1 in Tat-induced HIV-1 transcription: the C-terminal domain of RNA polymerase-II and CDK9. We also present a computer model of Tat-PP1 complex that might be useful for future drug design in anti-HIV- 1 therapeutics. <P></P> <P></P> <P></P>",
	pages = "11-22(12)",
	url = "http://www.ingentaconnect.com/content/ben/chr/2007/00000005/00000001/art00003"
	doi = "doi:10.2174/157016207779316332"
}