Anopheles gambiae cadherin AgCad1 binds the Cry4Ba toxin of Bacillus thuringiensis israelensis and a fragment of AgCad1 synergizes toxicity.
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Dominant negative phenotype of Bacillus thuringiensis Cry1Ab, Cry11Aa and Cry4Ba mutants suggest hetero-oligomer formation among different Cry toxinsCytotoxicity of the Bacillus thuringiensis Cry4B toxin is mediated by the cadherin receptor BT-R₃ of Anopheles gambiae.A 106-kDa aminopeptidase is a putative receptor for Bacillus thuringiensis Cry11Ba toxin in the mosquito Anopheles gambiaeABCC transporters mediate insect resistance to multiple Bt toxins revealed by bulk segregant analysis.Knockdown of two Cadherin genes confers resistance to Cry2A and Cry1C in Chilo suppressalisBacillus thuringiensis: a genomics and proteomics perspectiveDownregulation and mutation of a Cadherin gene associated with Cry1Ac resistance in the Asian Corn Borer, Ostrinia furnacalis (Guenée).Larval midgut modifications associated with Bti resistance in the yellow fever mosquito using proteomic and transcriptomic approaches.Binding of Bacillus thuringiensis subsp. israelensis Cry4Ba to Cyt1Aa has an important role in synergism.Gene expression patterns and sequence polymorphisms associated with mosquito resistance to Bacillus thuringiensis israelensis toxinsCadherin, alkaline phosphatase, and aminopeptidase N as receptors of Cry11Ba toxin from Bacillus thuringiensis subsp. jegathesan in Aedes aegyptiResistance to Bacillus thuringiensis Toxin Cry2Ab in Trichoplusia ni Is Conferred by a Novel Genetic Mechanism.Aedes cadherin mediates the in vivo toxicity of the Cry11Aa toxin to Aedes aegypti.A toxin-binding alkaline phosphatase fragment synergizes Bt toxin Cry1Ac against susceptible and resistant Helicoverpa armigeraThe Anopheles-midgut APN1 structure reveals a new malaria transmission-blocking vaccine epitopeAedes aegypti alkaline phosphatase ALP1 is a functional receptor of Bacillus thuringiensis Cry4Ba and Cry11Aa toxins.Multiple receptors as targets of Cry toxins in mosquitoesAedes aegypti cadherin serves as a putative receptor of the Cry11Aa toxin from Bacillus thuringiensis subsp. israelensisCloning and epitope mapping of Cry11Aa-binding sites in the Cry11Aa-receptor alkaline phosphatase from Aedes aegypti.A Spodoptera exigua cadherin serves as a putative receptor for Bacillus thuringiensis Cry1Ca toxin and shows differential enhancement of Cry1Ca and Cry1Ac toxicity.Loop residues of the receptor binding domain of Bacillus thuringiensis Cry11Ba toxin are important for mosquitocidal activity.Identification and characterization of Aedes aegypti aminopeptidase N as a putative receptor of Bacillus thuringiensis Cry11A toxin.Cadherin fragments from Anopheles gambiae synergize Bacillus thuringiensis Cry4Ba's toxicity against Aedes aegypti larvae.Bacillus thuringiensis: A story of a successful bioinsecticide.Bacillus thuringiensis insecticidal three-domain Cry toxins: mode of action, insect resistance and consequences for crop protection.Receptors of garlic (Allium sativum) lectins and their role in insecticidal action.Effects and mechanisms of Bacillus thuringiensis crystal toxins for mosquito larvae.Differential protection of Cry1Fa toxin against Spodoptera frugiperda larval gut proteases by cadherin orthologs correlates with increased synergism.An alpha-amylase is a novel receptor for Bacillus thuringiensis ssp. israelensis Cry4Ba and Cry11Aa toxins in the malaria vector mosquito Anopheles albimanus (Diptera: Culicidae)A cadherin-like protein from the beet armyworm Spodoptera exigua (Lepidoptera: Noctuidae) is a putative Cry1Ac receptor.Increased toxicity of Bacillus thuringiensis Cry3Aa against Crioceris quatuordecimpunctata, Phaedon brassicae and Colaphellus bowringi by a Tenebrio molitor cadherin fragment.A novel Tenebrio molitor cadherin is a functional receptor for Bacillus thuringiensis Cry3Aa toxin.Enhancement of Bacillus thuringiensis Cry3Aa and Cry3Bb toxicities to coleopteran larvae by a toxin-binding fragment of an insect cadherinThe Cry4B toxin of Bacillus thuringiensis subsp. israelensis kills Permethrin-resistant Anopheles gambiae, the principal vector of malaria.
P2860
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P2860
Anopheles gambiae cadherin AgCad1 binds the Cry4Ba toxin of Bacillus thuringiensis israelensis and a fragment of AgCad1 synergizes 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
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bilimsel makale
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scientific article published on 12 April 2008
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Anopheles gambiae cadherin AgC ...... of AgCad1 synergizes toxicity.
@en
Anopheles gambiae cadherin AgC ...... of AgCad1 synergizes toxicity.
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type
label
Anopheles gambiae cadherin AgC ...... of AgCad1 synergizes toxicity.
@en
Anopheles gambiae cadherin AgC ...... of AgCad1 synergizes toxicity.
@nl
prefLabel
Anopheles gambiae cadherin AgC ...... of AgCad1 synergizes toxicity.
@en
Anopheles gambiae cadherin AgC ...... of AgCad1 synergizes toxicity.
@nl
P2093
P2860
P356
P1433
P1476
Anopheles gambiae cadherin AgC ...... of AgCad1 synergizes toxicity.
@en
P2093
Michael J Adang
Mohd Amir F Abdullah
P2860
P304
P356
10.1021/BI7023578
P407
P577
2008-04-12T00:00:00Z