Reduced Levels of Membrane-Bound Alkaline Phosphatase Are Common to Lepidopteran Strains Resistant to Cry Toxins from Bacillus thuringiensis
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Title
Reduced Levels of Membrane-Bound Alkaline Phosphatase Are Common to Lepidopteran Strains Resistant to Cry Toxins from Bacillus thuringiensis
Authors
Keywords
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Journal
PLoS One
Volume 6, Issue 3, Pages e17606
Publisher
Public Library of Science (PLoS)
Online
2011-03-02
DOI
10.1371/journal.pone.0017606
References
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Related references
Note: Only part of the references are listed.- Midgut GPI-anchored proteins with alkaline phosphatase activity from the cotton boll weevil (Anthonomus grandis) are putative receptors for the Cry1B protein of Bacillus thuringiensis
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- Signaling versus punching hole: How do Bacillus thuringiensis toxins kill insect midgut cells?
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- Cloning and characterization of the Cry1Ac-binding alkaline phosphatase (HvALP) from Heliothis virescens
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- The mitogen-activated protein kinase p38 is involved in insect defense against Cry toxins from Bacillus thuringiensis
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- Homodimeric Alkaline Phosphatase Located atHelicoverpa armigeraMidgut, a Putative Receptor of Cry1Ac Contains α-GalNAc in Terminal Glycan Structure as Interactive Epitope†
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- Using an F2screen to monitor frequency of resistance alleles to Bt cotton in field populations ofHelicoverpa armigera(Hübner) (Lepidoptera: Noctuidae)
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- Specific Binding of Bacillus thuringiensis Cry2A Insecticidal Proteins to a Common Site in the Midgut of Helicoverpa Species
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- Insect resistance to Bt crops: evidence versus theory
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