ArticleProceedings of the National Academy of Sciences of the United States of America2004
Molecular basis for the inhibition of the carboxyltransferase domain of acetyl-coenzyme-A carboxylase by haloxyfop and diclofop.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
42 citing papers in PubMed, 164 citations in OpenAlex.
- Shared Plant-human Biology: Herbicide Effects and New Biomarkers Perspectives.Current environmental health reports · 2026Review
- Efficacy of Haloxyfop-R-Methyl on Allium cepa: Cyto-Genotoxic and In Silico Docking Studies on the Mechanism of Action.Microscopy research and technique · 2025Article
- Structure of the endogenous insect acetyl-coA carboxylase carboxyltransferase domain.The Journal of biological chemistry · 2024Article
- Target-site mutations Ile1781Leu and Ile2041Asn in thePlant direct · 2024Article
- Mining Fatty Acid Biosynthesis for New Antimicrobials.Annual review of microbiology · 2022Review
- Biochemical and structural characterization of quizalofop-resistant wheat acetyl-CoA carboxylase.Scientific reports · 2022Article
- Sequence and structural similarities of ACCase protein ofFrontiers in plant science · 2022Article
- Diverse mechanisms associated with cyhalofop-butyl resistance in Chinese sprangletop (Frontiers in plant science · 2022Article
- Article
- Proving the Mode of Action of Phytotoxic Phytochemicals.Plants (Basel, Switzerland) · 2020Review
- Comparative Transcriptome Analysis Revealing the Different Germination Process in Aryloxyphenoxypropionate-Resistant and APP-Susceptible Asia Minor Bluegrass (Plants (Basel, Switzerland) · 2020Article
- Targeted, random mutagenesis of plant genes with dual cytosine and adenine base editors.Nature biotechnology · 2020Article
- Molecular characteristics of the first case of haloxyfop-resistant Poa annua.Scientific reports · 2020Article
- Fitness of Herbicide-Resistant Weeds: Current Knowledge and Implications for Management.Plants (Basel, Switzerland) · 2019Review
- Target-Site Mutations Conferring Herbicide Resistance.Plants (Basel, Switzerland) · 2019Review
- Design, Synthesis and Evaluation of Novel Trichloromethyl Dichlorophenyl Triazole Derivatives as Potential Safener.Biomolecules · 2019Article
- Resistance determination of the ACCase-inhibiting herbicide of clodinafop propargyl in Avena ludoviciana (Durieu), and study of their interaction using molecular docking and simulation.Molecular biology reports · 2019Article
- Analysis of Arabidopsis Accessions Hypersensitive to a Loss of Chloroplast Translation.Plant physiology · 2016Article
- Mechanism of metamifop inhibition of the carboxyltransferase domain of acetyl-coenzyme A carboxylase in Echinochloa crus-galli.Scientific reports · 2016Article
- Acetyl-CoA carboxylase inhibition by ND-630 reduces hepatic steatosis, improves insulin sensitivity, and modulates dyslipidemia in rats.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Acetyl-CoA carboxylases (ACCs) are crucial for the metabolism of fatty acids, making these enzymes important targets for the development of therapeutics against obesity, diabetes, and other diseases. The carboxyltransferase (CT) domain of ACC is the site of action of commercial herbicides, such as haloxyfop, diclofop, and sethoxydim. We have determined the crystal structures at up to 2.5-A resolution of the CT domain of yeast ACC in complex with the herbicide haloxyfop or diclofop. The inhibitors are bound in the active site, at the interface of the dimer of the CT domain. Unexpectedly, inhibitor binding requires large conformational changes for several residues in this interface, which create a highly conserved hydrophobic pocket that extends deeply into the core of the dimer. Two residues that affect herbicide sensitivity are located in this binding site, and mutation of these residues disrupts the structure of the domain. Other residues in the binding site are strictly conserved among the CT domains.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.