Data from: Stepwise evolution of resistance to toxic cardenolides via genetic substitutions in the Na+/K+-ATPase of milkweed butterflies (Lepidopte

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关键词：

molecular evolutionary physiology monarch butterfly plant-herbivore interactions target site insensitivity Adaptation

DOI：

doi:10.5061/dryad.v7cj8

摘要：

(Na+/K+-ATPase), has evolved amino acid substitutions which reduce cardenolide binding (so-called target site insensitivity, TSI). Since many, but not all, species

Data from: Substitutions in the cardenolide binding site and interaction of subunits affect kinetics besides cardenolide sensitivity of inse

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关键词：

NA;Drosophila;Oncopeltus fasciatus;K-ATPase;enzyme kinetics;drosophila melanogaster;Amino acid substitutions;Subunit interaction;Cardenolide resistance

DOI：

doi:10.5061/dryad.031sf

摘要：

Substitutions within the cardenolide target site of several insects' Na,K-ATPase ?-subunits may confer resistance against toxic cardenolides. Howeve

Data from: Convergently evolved toxic secondary metabolites in plants drive the parallel molecular evolution of insect resistance

负责人：

Dobler, Susanne

关键词：

DOI：

doi:10.5061/dryad.20191

摘要：

nce of the Na,K-ATPase. Our results demonstrate that target site insensitivity of Na,K-ATPase is a common response to dietary cardiac glycosides leading to highly