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John T. Gupton

Researcher at University of Richmond

Publications -  91
Citations -  1278

John T. Gupton is an academic researcher from University of Richmond. The author has contributed to research in topics: Iminium & Aryl. The author has an hindex of 22, co-authored 90 publications receiving 1221 citations. Previous affiliations of John T. Gupton include Kyoto University & University of North Carolina at Asheville.

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Application of 2-substituted vinamidinium salts to the synthesis of 2,4-disubstituted pyrroles

TL;DR: In this article, a variety of 2-substituted vinamidinium salts react with α-amino acid esters under basic conditions to produce 2-carbethoxy-4-substantituted-pyrroles in good yield.
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Autophagic cell death, polyploidy and senescence induced in breast tumor cells by the substituted pyrrole JG-03-14, a novel microtubule poison.

TL;DR: The observation that JG-03-14 promotes autophagic cell death and also retains activity in tumor cells expressing the multidrug resistance pump indicates that novel microtubule poisons of the substituted pyrroles class may hold promise in the treatment of breast cancer.
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Preparation of novel β-trifluoromethyl vinamidinium salt and its synthetic application to trifluoromethylated heterocycles

TL;DR: In this article, the β-trifluoromethylated vinamidinium salt (1) was prepared in high yield by the reaction between 3,3,3 trifluorsopropanoic acid and phosphorus oxychloride in N,N-dimethylformamide at 70 °C for 1 h.
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The application of disubstituted vinylogous iminium salts and related synthons to the regiocontrolled preparation of unsymmetrical 2,3,4-trisubstituted pyrroles

TL;DR: In this article, 2,3,4-trisubstituted pyrrole systems were studied under acidic, basic and neutral conditions, and the results of such reactions have resulted in efficient and selective methodology for the synthesis of unsymmetrical 2, 3, 4 trisubstantituted Pyrrole system.
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Docking and hydropathic scoring of polysubstituted pyrrole compounds with antitubulin activity

TL;DR: Docking calculations coupled with HINT interaction analyses are able to represent the complex structures and the binding modes of inhibitors such that calculated and measured free energies of binding correlate with an r(2) of 0.76.