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George L. Kenyon

Researcher at University of California, San Francisco

Publications -  165
Citations -  9145

George L. Kenyon is an academic researcher from University of California, San Francisco. The author has contributed to research in topics: Mandelate racemase & Creatine kinase. The author has an hindex of 48, co-authored 165 publications receiving 8842 citations. Previous affiliations of George L. Kenyon include University of Maryland, College Park & Massachusetts Institute of Technology.

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Structural identification of autoinducer of Photobacterium fischeri luciferase.

TL;DR: In this paper, an autoinducer excreted by Photobacterium fischeri strain MJ-1 was isolated from the cell-free medium by extraction with ethyl acetate, evaporation of solvent, workup with ethanol-water mixtures, and silica gel chromatography.
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Inhibition of the HIV-1 protease by fullerene derivatives: model building studies and experimental verification

TL;DR: The ability of C[sub 60] fullerene derivatives to interact with the active site of HIV-1 protease (HIVP) has been examined through model building and simple physical chemical analysis as discussed by the authors.
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Synthesis of a fullerene derivative for the inhibition of HIV enzymes

TL;DR: In this article, a diamido diacid diphenyl fulleroid derivative was designed specifically to inhibit an HIV enzyme and detailed synthesis and mass spectrometric analysis of the water-soluble, biologically active methanofullerene are described.
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In Vitro Antimalarial Activity of Chalcones and Their Derivatives

TL;DR: Structural relationships (SAR) of the chalcones in the context of a homology-based model structure of the malaria trophozoite cysteine protease, the most likely target enzyme, are presented, suggesting that this series will be active against chloroquine-resistant malaria.
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The Enolase Superfamily: A General Strategy for Enzyme-Catalyzed Abstraction of the α-Protons of Carboxylic Acids†

TL;DR: A superfamily of enzymes related by their ability to catalyze the abstraction of the alpha-proton of a carboxylic acid to form an enolic intermediate is discovered, and the established and deduced structure-function relationships in the superfamily allow the prediction that other apparent members of the family for which no catalytic functions have yet been assigned will also perform chemistry involving abstraction of their alpha-protons.