Publication | Open Access
Molecular Modeling Indicates that Two Chemically Distinct Classes of Anti-Mitotic Herbicide Bind to the Same Receptor Site(s)
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Citations
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References
1994
Year
BotanyMolecular BiologyAnti-mitotic Herbicide BindCytoskeletonChemical BiologyChemical PropertiesPlant CytologyPlant BiologyMode Of ActionBiochemistryReceptor (Biochemistry)Mechanism Of ActionPharmacologyMolecular ModelingSame Receptor SiteNatural SciencesPesticide ResistanceHerbicides Disrupt MicrotubuleTubulin Protein DimersMedicineDrug Discovery
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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