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PLANT PHYSIOLOGY , Vol 105, Issue 1 15-18, Copyright © 1994 by American Society of Plant Biologists


RAPID COMMUNICATIONS

Molecular Modeling Indicates that Two Chemically Distinct Classes of Anti-Mitotic Herbicide Bind to the Same Receptor Site(s)

J. R. Ellis, R. Taylor and P. J. Hussey
Zeneca Seeds and Agrochemicals, Jealott's Hill Research Station, Bracknell, Berkshire RG12 6EY, United Kingdom (J.R.E., R.T.)

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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P. M. Chilley, S. A. Casson, P. Tarkowski, N. Hawkins, K. L.-C. Wang, P. J. Hussey, M. Beale, J. R. Ecker, G. K. Sandberg, and K. Lindsey
The POLARIS Peptide of Arabidopsis Regulates Auxin Transport and Root Growth via Effects on Ethylene Signaling
PLANT CELL, November 1, 2006; 18(11): 3058 - 3072.
[Abstract] [Full Text] [PDF]


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C. Delye, Y. Menchari, S. Michel, and H. Darmency
Molecular Bases for Sensitivity to Tubulin-Binding Herbicides in Green Foxtail
Plant Physiology, December 1, 2004; 136(4): 3920 - 3932.
[Abstract] [Full Text] [PDF]




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Copyright © 1994 by the American Society of Plant Biologists