D. L. Siehl
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
D. L. Siehl has a total of 10 co-authors. Here are the top co-authors by number of shared publications:
M. V. Subramanian
Sandoz AgroInc.975 California Ave.Palo AltoCA94304‐1104
2 shared publicationsA. G. Toschi
1 shared publicationA. S. Bengtson
Sandoz AgroInc.975 California Ave.Palo AltoCA94304‐1104
1 shared publicationE. W. Walters
1 shared publicationG. W. Kraatz
Sandoz AgroInc.5653 Monterey Rd.GilroyCA95020
1 shared publicationJ. H. Butler
Sandoz AgroInc.975 California Ave.Palo AltoCA94304‐1104
1 shared publication
Latest Publications
- 1 March 1996
- Published by Wiley in Crop Science
- Vol. 36 (2) , 274-278
Patterns of Cross‐Tolerance to Herbicides Inhibiting Acetohydroxyacid Synthase in Commercial Corn Hybrids Designed for Tolerance to Imidazolinones
- 1 March 1996
- Published by Wiley in Crop Science
- Vol. 36 (2) , 274-278
Patterns of Cross‐Tolerance to Herbicides Inhibiting Acetohydroxyacid Synthase in Commercial Corn Hybrids Designed for Tolerance to Imidazolinones
- Open Access
- 1 March 1996
- Published by Oxford University Press (OUP) in Plant Physiology
- Vol. 110 (3) , 753-758
Adenylosuccinate Synthetase: Site of Action of Hydantocidin, a Microbial Phytotoxin
The site of action of hydantocidin was probed using Arabidopsis thaliana plants growing on agar plates. Herbicidal effects were reversed when the agar medium was supplemented with AMP, but not IMP or GMP, suggesting that hydantocidin blocked the two-step conversion of IMP to AMP in the de novo purine biosynthesis pathway. Hydantocidin itself did not inhibit adenylosuccinate synthetase or adenylosuccinate lyase isolated from Zea mays. However, a phosphorylated derivative of hydantocidin, N-acetyl-5[prime]-phosphohydantocidin, was a potent inhibitor of the synthetase but not of the lyase. These results identify the site of action of hydantocidin and establish adenylosuccinate synthetase as an herbicide target of commercial potential.
- 1 March 1996
- Published by Oxford University Press (OUP) in Plant Physiology
- Vol. 110 (3) , 753-758
Open AccessAdenylosuccinate Synthetase: Site of Action of Hydantocidin, a Microbial Phytotoxin
The site of action of hydantocidin was probed using Arabidopsis thaliana plants growing on agar plates. Herbicidal effects were reversed when the agar medium was supplemented with AMP, but not IMP or GMP, suggesting that hydantocidin blocked the two-step conversion of IMP to AMP in the de novo purine biosynthesis pathway. Hydantocidin itself did not inhibit adenylosuccinate synthetase or adenylosuccinate lyase isolated from Zea mays. However, a phosphorylated derivative of hydantocidin, N-acetyl-5[prime]-phosphohydantocidin, was a potent inhibitor of the synthetase but not of the lyase. These results identify the site of action of hydantocidin and establish adenylosuccinate synthetase as an herbicide target of commercial potential.