Bacillus thuringiensis Cry1A toxins are versatile proteins with multiple modes of action: two distinct pre-pores are involved in toxicity.
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ABCC2 is associated with Bacillus thuringiensis Cry1Ac toxin oligomerization and membrane insertion in diamondback mothComparison of drought stress response and gene expression between a GM maize variety and a near-isogenic non-GM variety.Evidence of field-evolved resistance of Spodoptera frugiperda to Bt corn expressing Cry1F in Brazil that is still sensitive to modified Bt toxins.Comparative performance of modified full-length and truncated Bacillus thuringiensis-cry1Ac genes in transgenic tomato.Binding and Oligomerization of Modified and Native Bt Toxins in Resistant and Susceptible Pink Bollworm.Use of Redundant Exclusion PCR To Identify a Novel Bacillus thuringiensis Cry8 Toxin Gene from Pooled Genomic DNA.Activation of Bt Protoxin Cry1Ac in Resistant and Susceptible Cotton Bollworm.Dual mode of action of Bt proteins: protoxin efficacy against resistant insectsIdentification of ABCC2 as a binding protein of Cry1Ac on brush border membrane vesicles from Helicoverpa armigera by an improved pull-down assay.An Intramolecular Salt Bridge in Bacillus thuringiensis Cry4Ba Toxin Is Involved in the Stability of Helix α-3, Which Is Needed for Oligomerization and Insecticidal Activity.Interactions between Bt crops and aquatic ecosystems: A review.Possible health impacts of Bt toxins and residues from spraying with complementary herbicides in genetically engineered soybeans and risk assessment as performed by the European Food Safety Authority EFSA.Validation of ADAM10 metalloprotease as a Bacillus thuringiensis Cry3Aa toxin functional receptor in Colorado potato beetle (Leptinotarsa decemlineata).Potential Prepore Trimer Formation by the Bacillus thuringiensis Mosquito-specific Toxin: MOLECULAR INSIGHTS INTO A CRITICAL PREREQUISITE OF MEMBRANE-BOUND MONOMERS.Helix α-3 inter-molecular salt bridges and conformational changes are essential for toxicity of Bacillus thuringiensis 3D-Cry toxin family.Membrane insertion of α-xenorhabdolysin in near-atomic detail
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Bacillus thuringiensis Cry1A toxins are versatile proteins with multiple modes of action: two distinct pre-pores are involved in toxicity.
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article científic
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article scientifique
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articolo scientifico
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artigo científico
@pt
bilimsel makale
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scientific article published on April 2014
@en
vedecký článok
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vetenskaplig artikel
@sv
videnskabelig artikel
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vědecký článek
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name
Bacillus thuringiensis Cry1A t ...... ores are involved in toxicity.
@en
Bacillus thuringiensis Cry1A t ...... ores are involved in toxicity.
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type
label
Bacillus thuringiensis Cry1A t ...... ores are involved in toxicity.
@en
Bacillus thuringiensis Cry1A t ...... ores are involved in toxicity.
@nl
prefLabel
Bacillus thuringiensis Cry1A t ...... ores are involved in toxicity.
@en
Bacillus thuringiensis Cry1A t ...... ores are involved in toxicity.
@nl
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P1433
P1476
Bacillus thuringiensis Cry1A t ...... ores are involved in toxicity.
@en
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Carlos Muñoz-Garay
Isabel Gómez
Jorge Sánchez
Mario Soberón
Sarjeet S Gill
Violeta Matus
P2860
P304
P356
10.1042/BJ20131408
P407
P577
2014-04-01T00:00:00Z