Molecular characterisation of resistance to ACCase-inhibiting herbicides in wild oat in the northern grain-growing region of Australia.
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- Type
- article
- Published
- 2004-01-01
- Cited by
- 0
- References
- 8
- OpenAlex
- https://openalex.org/W1490242329
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:82666135
Keywords
Agronomy, Resistance (ecology), Biology, Glyphosate, Geography
References
- A reagent for the single-step simultaneous isolation of RNA, DNA and proteins from cell and tissue samples.
- Germinal transpositions of the maize element Dissociation from T-DNA loci in tomato.
- An isoleucine to leucine substitution in the ACCase of Alopecurus myosuroides (black-grass) is associated with resistance to the herbicide sethoxydim
- An Isoleucine Residue within the Carboxyl-Transferase Domain of Multidomain Acetyl-Coenzyme A Carboxylase Is a Major Determinant of Sensitivity to Aryloxyphenoxypropionate But Not to Cyclohexanedione Inhibitors1
- An isoleucine/leucine residue in the carboxyltransferase domain of acetyl-CoA carboxylase is critical for interaction with aryloxyphenoxypropionate and cyclohexanedione inhibitors
- Altered target sites as a mechanism of herbicide resistance
- An isoleucine to leucine mutation in acetyl-CoA carboxylase confers herbicide resistance in wild oat.
- Herbicide sensitivity determinant of wheat plastid acetyl-CoA carboxylase is located in a 400-amino acid fragment of the carboxyltransferase domain.
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