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Susan L. Morris-Natschke

Researcher at University of North Carolina at Chapel Hill

Publications -  287
Citations -  9762

Susan L. Morris-Natschke is an academic researcher from University of North Carolina at Chapel Hill. The author has contributed to research in topics: Cytotoxicity & Camptothecin. The author has an hindex of 48, co-authored 284 publications receiving 8331 citations. Previous affiliations of Susan L. Morris-Natschke include China Medical University (Taiwan) & Shandong University.

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Anti-tumor agents 255: novel glycyrrhetinic acid-dehydrozingerone conjugates as cytotoxic agents.

TL;DR: Although GA-DZ conjugates showed potent cytotoxic activity, the individual components (GA and DZ analogs) were inactive suggesting that the GA component is critical for activity.
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Synthesis of sulfur analogues of alkyl lysophospholipid and neoplastic cell growth inhibitory properties.

TL;DR: Five sulfur-containing phosphate analogues of alkyl lysophospholipid were synthesized and tested for inhibition of neoplastic cell proliferation with two human ovarian carcinoma cell lines in a clonogenic assay and with the HL-60 promyelocytic leukemia cell line.
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Plant-derived Terpenoids and Analogues as Anti-HIV Agents

TL;DR: The plant-derived terpenoids and analogues are reviewed with respect to their anti-HIV activity, structure-activity relationships, and mechanism of action.
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In vitro evaluation of phosphocholine and quaternary ammonium containing lipids as novel anti-HIV agents

TL;DR: Initial mechanistic studies have indicated that these compounds, unlike AZT, are not reverse transcriptase (RT) inhibitors, but instead appear to inhibit a late step in HIV replication involving virus assembly and infectious virus production.
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Optimization of 4-(N-Cycloamino)phenylquinazolines as a Novel Class of Tubulin-Polymerization Inhibitors Targeting the Colchicine Site

TL;DR: 7-Methoxy-4-(2-methylquinazolin-4-yl)-3,4-dihydroquinoxalin- 2(1H)-one (5f), the most potent compound, exhibited high in vitro cytotoxic activity, significant potency against tubulin assembly, and substantial inhibition of colchicine binding.