Mechanism of action of the 1,2,4‐triazolo[1,5‐a] pyrimidines

doi:10.1002/PS.2780290310

Paper

Mechanism of action of the 1,2,4‐triazolo[1,5‐a] pyrimidines

Published 1990 · B. Gerwick, M. Subramanian, Vivian I. Loney-Gallant

Pesticide Science

UNKNOWN SJR score

118

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3

Influential Citations

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Abstract

The substituted 1,2,4-triazolo[1,5-a]pyrimidines are a new class of highly active herbicides. Protection of Arabidopsis thaliana seedlings from triazolopyrimidine-induced injury by the branched-chain amino acids was observed. Acetolactate synthase (EC 4.1.3.18) was isolated and found to be quite sensitive to inhibition. I50 values for inhibition of the enzyme from a number of plant sources show little variation and no correlation to whole-plant response, suggesting uptake, translocation and metabolism play key roles in modulating herbicidal activity. Further studies indicate that these chemicals are slow, tight-binding inhibitors that are readily dissociated by gel filtration. Some correlations between in-vitro activity and in-vivo activity were observed for ortho-substituted analogs on selected broadleaf species.

Highly Cited

Study Snapshot

The 1,2,4-triazolo[1,5-a]pyrimidines are a new class of highly active herbicides, with uptake, translocation, and metabolism playing key roles in modulating their herbicidal activity.

PopulationOlder adults (50-71 years)

Sample size24

MethodsObservational

OutcomesBody Mass Index projections

ResultsSocial networks mitigate obesity in older groups.

Paper

Mechanism of action of the 1,2,4‐triazolo[1,5‐a] pyrimidines

References

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Citations

A New Pro-197-Ile Mutation in Amaranthus palmeri Associated with Acetolactate Synthase-Inhibiting Herbicide Resistance

Pro-197-Ile mutation in Amaranthus palmeri plants in China provides high resistance to imazethapyr, making it the first case of an imazethapyr-resistant biotype in China.

The Catalysis of Bacillus subtilis Acetolactate Synthase Is Fundamentally Underestimated

Bacillus subtilis acetolactate synthase has a significantly underestimated catalytic potential, offering potential for asymmetric synthesis of diverse chiral -hydroxyketones and arylhydroxamic acids.

Target-site mutation and enhanced metabolism endow resistance to nicosulfuron in a Digitaria sanguinalis population.

A Digitaria sanguinalis population in Hebei Province, China, exhibits 6.9-fold resistance to nicosulfuron due to a mutation in the ALS gene and enhanced metabolism, with a moderate cross-resistance to other ALS inhibitors.

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