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Michael J. Currens

Researcher at Government of the United States of America

Publications -  19
Citations -  3654

Michael J. Currens is an academic researcher from Government of the United States of America. The author has contributed to research in topics: Calanolides & Reverse transcriptase. The author has an hindex of 15, co-authored 19 publications receiving 3540 citations.

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Journal Article

Evaluation of a Soluble Tetrazolium/Formazan Assay for Cell Growth and Drug Sensitivity in Culture Using Human and Other Tumor Cell Lines

TL;DR: The new XTT reagent provides for a simplified, in vitro cell growth assay with possible applicability to a variety of problems in cellular pharmacology and biology, but still shares many of the limitations and potential pitfalls of MTT or other tetrazolium-based assays.
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The calanolides, a novel HIV-inhibitory class of coumarin derivatives from the tropical rainforest tree, Calophyllum lanigerum.

TL;DR: Calanolide A was active not only against the AZT-resistant G-9106 strain of HIV-1 but also against the pyridinone-resistant A17 strain, which was of particular interest since the A17 virus is highly resistant to previously known HIV- 1 specific, non-nucleoside RT inhibitors.
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Analysis of nonnucleoside drug-resistant variants of human immunodeficiency virus type 1 reverse transcriptase

TL;DR: Analysis of mutants used to analyze calanolide A, 1H,3H-thiazolo[3,4-a]benzimidazole(4i), and the acyclic nucleoside analog 1-[(2-hydroxyethoxy)methyl]-6-(phenylthio)thymine suggest that all three drugs interact with HIV-1 RT within the previously defined common binding site for nonnucleoside inhibitors.
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Application of high-throughput, molecular-targeted screening to anticancer drug discovery.

TL;DR: The application of high-throughput screening to anti-cancer drug discovery, with special reference to approaches used at the U.S. National Cancer Institute is discussed.
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Analysis of the interaction between the HIV-inactivating protein cyanovirin-N and soluble forms of the envelope glycoproteins gp120 and gp41.

TL;DR: Circular dichroism studies additionally illuminated the binding of CV-N with both sgp120 and sgp41, providing the first direct evidence that conformational changes are a consequence ofCV-N interactions with both HIV-1 envelope glycoproteins.