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-Reference-Cited by-同舟云学术

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

Published:2013-10-10 Issue:7 Volume:16 Page:2253-2266
ISSN:1462-2912
Container-title:Environmental Microbiology
language:en
Short-container-title:Environ Microbiol

Author:

Lalève Anaïs¹,Gamet Stéphanie²,Walker Anne-Sophie¹,Debieu Danièle¹,Toquin Valérie²,Fillinger Sabine¹

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.

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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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