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A High Throughput MHC II Binding Assay for Quantitative Analysis of Peptide Epitopes
Published on: March 25, 2014
Molecular Modeling Indicates that Two Chemically Distinct Classes of Anti-Mitotic Herbicide Bind to the Same Receptor
J. R. Ellis1, R. Taylor, P. J. Hussey
1Zeneca Seeds and Agrochemicals, Jealott's Hill Research Station, Bracknell, Berkshire RG12 6EY, United Kingdom (J.R.E., R.T.).
Abstract:
Dinitroaniline and phosphorothioamidate herbicides disrupt microtubule assembly from tubulin protein dimers and thereby halt microtubule-based processes such as mitosis in plant cells. Despite the contrasting chemical properties of dinitroaniline and phosphorothioamidate herbicides, a three-dimensional molecular analysis revealed remarkable electrostatic similarity between these two classes of herbicide. From these data it is proposed that dinitroaniline and phosphorothioamidate herbicides share common binding site(s) in the plant cell.
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