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R V Srinivas

Researcher at St. Jude Children's Research Hospital

Publications -  45
Citations -  2545

R V Srinivas is an academic researcher from St. Jude Children's Research Hospital. The author has contributed to research in topics: Glycoprotein & Virus. The author has an hindex of 23, co-authored 45 publications receiving 2489 citations. Previous affiliations of R V Srinivas include National Institutes of Health & University of Alabama at Birmingham.

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MRP4: A previously unidentified factor in resistance to nucleoside-based antiviral drugs.

TL;DR: In the study of alternative or additional mechanisms of resistance operating during antiviral therapy, overexpression and amplification of the MRP4 gene correlated with ATP-dependent efflux of PMEA and azidothymidine monophosphate from cells and, thus, with resistance to these drugs.
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Anti-Human Immunodeficiency Virus Activity and Cellular Metabolism of a Potential Prodrug of the Acyclic Nucleoside Phosphonate 9-R-(2-Phosphonomethoxypropyl)adenine (PMPA), Bis(isopropyloxymethylcarbonyl)PMPA

TL;DR: Long persistence of PMPApp, particularly in resting lymphocytes, may be unique to the nucleoside phosphonate analogs and indicates that effective levels of the active metabolite can be achieved and maintained with relatively infrequent administration of the parent drug.
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Human immunodeficiency virus protease inhibitors serve as substrates for multidrug transporter proteins MDR1 and MRP1 but retain antiviral efficacy in cell lines expressing these transporters.

TL;DR: In conclusion, overexpression of MDR1 or MRP1 by T lymphocytes is not likely to limit the antiviral efficacy of HIV PI therapy, and the 90% inhibitory concentration for a given compound was comparable between the different cell types.
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Metabolism and in vitro antiretroviral activities of bis(pivaloyloxymethyl) prodrugs of acyclic nucleoside phosphonates.

TL;DR: The bis(pom) derivatives were chemically unstable and highly susceptible to serum-mediated hydrolysis, factors which limit their potential utility for intracellular drug delivery.
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Apolipoprotein A-I and its amphipathic helix peptide analogues inhibit human immunodeficiency virus-induced syncytium formation.

TL;DR: Apolipoprotein A-I, the major protein component of high density lipoprotein, and its amphipathic peptide analogue were found to inhibit cell fusion, both in HIV-1-infected T cells and in recombinant vaccinia-virus-infecting CD4+ HeLa cells expressing HIV envelope protein on their surfaces.