Bacillus thuringiensisCry1A toxins are versatile proteins with multiple modes of action: two distinct pre-pores are involved in toxicity
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Title
Bacillus thuringiensisCry1A toxins are versatile proteins with multiple modes of action: two distinct pre-pores are involved in toxicity
Authors
Keywords
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Journal
BIOCHEMICAL JOURNAL
Volume 459, Issue 2, Pages 383-396
Publisher
Portland Press Ltd.
Online
2014-01-24
DOI
10.1042/bj20131408
References
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Related references
Note: Only part of the references are listed.- Differential Role of Manduca sexta Aminopeptidase-N and Alkaline Phosphatase in the Mode of Action of Cry1Aa, Cry1Ab, and Cry1Ac Toxins from Bacillus thuringiensis
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- (2012) Haonan Zhang et al. PLoS One
- Efficacy of genetically modified Bt toxins against insects with different genetic mechanisms of resistance
- (2011) Bruce E Tabashnik et al. NATURE BIOTECHNOLOGY
- Dual Chaperone Role of the C-Terminal Propeptide in Folding and Oligomerization of the Pore-Forming Toxin Aerolysin
- (2011) Ioan Iacovache et al. PLoS Pathogens
- Role of Alkaline Phosphatase fromManduca sextain the Mechanism of Action ofBacillus thuringiensisCry1Ab Toxin
- (2010) Iván Arenas et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Cadherin Fragments from Anopheles gambiae Synergize Bacillus thuringiensis Cry4Ba's Toxicity against Aedes aegypti Larvae
- (2009) Y. Park et al. APPLIED AND ENVIRONMENTAL MICROBIOLOGY
- Enhancement of Bacillus thuringiensis Cry3Aa and Cry3Bb Toxicities to Coleopteran Larvae by a Toxin-Binding Fragment of an Insect Cadherin
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- Characterization of the mechanism of action of the genetically modified Cry1AbMod toxin that is active against Cry1Ab-resistant insects
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- Domain II Loop 3 ofBacillus thuringiensisCry1Ab Toxin Is Involved in a “Ping Pong” Binding Mechanism with Manduca sexta Aminopeptidase-N and Cadherin Receptors
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- N546 in β18–β19 loop is important for binding and toxicity of the Bacillus thuringiensis Cry1Ac toxin
- (2009) Wang Fa Xiang et al. JOURNAL OF INVERTEBRATE PATHOLOGY
- Manduca sexta(Lepidoptera: Sphingidae) cadherin fragments function as synergists for Cry1A and Cry1CBacillus thuringiensistoxins against noctuid mothsHelicoverpa zea, Agrotis ipsilonandSpodoptera exigua
- (2009) Mohd Amir F Abdullah et al. PEST MANAGEMENT SCIENCE
- Dominant Negative Mutants of Bacillus thuringiensis Cry1Ab Toxin Function as Anti-Toxins: Demonstration of the Role of Oligomerization in Toxicity
- (2009) Claudia Rodríguez-Almazán et al. PLoS One
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- (2008) Manoj S. Nair et al. BIOCHEMISTRY
- Study of the irreversible binding of Bacillus thuringiensis Cry1Aa to brush border membrane vesicles from Bombyx mori midgut
- (2008) Hideshi Ihara et al. JOURNAL OF INVERTEBRATE PATHOLOGY
- Enhancement of insecticidal activity of Bacillus thuringiensis Cry1A toxins by fragments of a toxin-binding cadherin correlates with oligomer formation
- (2008) Sabino Pacheco et al. PEPTIDES
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