Site-directed mutagenesis of the P225, N230 and H272 residues of succinate dehydrogenase subunit B fromBotrytis cinereahighlights different roles in enzyme activity and inhibitor binding
Author:
Affiliation:
1. INRA; UR 1290 BIOGER-CPP; Avenue Lucien Brétignières F-78850 Thiverval-Grignon France
2. BAYER SAS; BayerCropScience; Impasse Pierre Baizet F-69009 Lyon France
Funder
Bayer CropScience
Publisher
Wiley
Subject
Ecology, Evolution, Behavior and Systematics,Microbiology
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/1462-2920.12282/fullpdf
Reference49 articles.
1. Phenotypic characterization of multifungicide resistance in botrytis cinerea isolates from strawberry fields in Florida;Amiri;Plant Dis,2013
2. Characterization of mutations in the membrane-anchored subunits AaSDHC and AaSDHD of succinate dehydrogenase from Alternaria alternata isolates conferring field resistance to the fungicide boscalid;Avenot;Plant Pathol,2009
3. Progress in understanding molecular mechanisms and evolution of resistance to succinate dehydrogenase inhibiting (SDHI) fungicides in phytopathogenic fungi;Avenot;Crop Prot,2010
4. Characterization of mutations in the iron-sulphur subunit of succinate dehydrogenase correlating with boscalid resistance in Alternaria alternata from California pistachio;Avenot;Phytopathology,2008
5. Multiple resistance of Botrytis cinerea from kiwifruit to SDHIs, QoIs and fungicides of other chemical groups;Bardas;Pest Manag Sci,2010
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