Single amino acid mutations in the cadherin receptor from Heliothis virescens affect its toxin binding ability to Cry1A toxins.
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Mode of action of Bacillus thuringiensis Cry and Cyt toxins and their potential for insect controlRole of receptors in Bacillus thuringiensis crystal toxin activityDown regulation of a gene for cadherin, but not alkaline phosphatase, associated with Cry1Ab resistance in the sugarcane borer Diatraea saccharalis.Affinity maturation of Cry1Aa toxin to the Bombyx mori cadherin-like receptor by directed evolution.Cry11Aa toxin from Bacillus thuringiensis binds its receptor in Aedes aegypti mosquito larvae through loop alpha-8 of domain II.Specific epitopes of domains II and III of Bacillus thuringiensis Cry1Ab toxin involved in the sequential interaction with cadherin and aminopeptidase-N receptors in Manduca sexta.Employing phage display to study the mode of action of Bacillus thuringiensis Cry toxins.Investigating the properties of Bacillus thuringiensis Cry proteins with novel loop replacements created using combinatorial molecular biology.Bacillus thuringiensis: a genomics and proteomics perspectiveDownregulation and mutation of a Cadherin gene associated with Cry1Ac resistance in the Asian Corn Borer, Ostrinia furnacalis (Guenée).Structural insights into Bacillus thuringiensis Cry, Cyt and parasporin toxinsResistance of Trichoplusia ni to Bacillus thuringiensis toxin Cry1Ac is independent of alteration of the cadherin-like receptor for Cry toxinsGene expression patterns and sequence polymorphisms associated with mosquito resistance to Bacillus thuringiensis israelensis toxinsA toxin-binding alkaline phosphatase fragment synergizes Bt toxin Cry1Ac against susceptible and resistant Helicoverpa armigeraGeneration of a Transcriptome in a Model Lepidopteran Pest, Heliothis virescens, Using Multiple Sequencing Strategies for Profiling Midgut Gene Expression.Synergism of Bacillus thuringiensis toxins by a fragment of a toxin-binding cadherin.Diverse genetic basis of field-evolved resistance to Bt cotton in cotton bollworm from China.Continuous evolution of Bacillus thuringiensis toxins overcomes insect resistance.The secondary cell wall polysaccharide of Bacillus anthracis provides the specific binding ligand for the C-terminal cell wall-binding domain of two phage endolysins, PlyL and PlyG.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.Anopheles gambiae cadherin AgCad1 binds the Cry4Ba toxin of Bacillus thuringiensis israelensis and a fragment of AgCad1 synergizes toxicity.Dominant negative mutants of Bacillus thuringiensis Cry1Ab toxin function as anti-toxins: demonstration of the role of oligomerization in toxicity.Strategies to improve the insecticidal activity of Cry toxins from Bacillus thuringiensis.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.Domain II loop 3 of Bacillus thuringiensis Cry1Ab toxin is involved in a "ping pong" binding mechanism with Manduca sexta aminopeptidase-N and cadherin receptors.Bacillus thuringiensis: A story of a successful bioinsecticide.Molecular recognition theory and sense-antisense interaction: therapeutic applications in autoimmunityEffects and mechanisms of Bacillus thuringiensis crystal toxins for mosquito larvae.Analysis of the region for receptor binding and triggering of oligomerization on Bacillus thuringiensis Cry1Aa toxin.Cry1Aa binding to the cadherin receptor does not require conserved amino acid sequences in the domain II loops.Affinity maturation of Cry1Aa toxin to the Bombyx mori cadherin-like receptor by directed evolution based on phage display and biopanning selections of domain II loop 2 mutant toxinsA cadherin-like protein from the beet armyworm Spodoptera exigua (Lepidoptera: Noctuidae) is a putative Cry1Ac receptor.A cadherin-like protein influences Bacillus thuringiensis Cry1Ab toxicity in the oriental armyworm, Mythimna separata.A single major QTL controls expression of larval Cry1F resistance trait in Ostrinia nubilalis (Lepidoptera: Crambidae) and is independent of midgut receptor genes.Bacillus thuringiensis Cry toxins bound specifically to various proteins via domain III, which had a galactose-binding domain-like fold.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 cadherin
P2860
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P2860
Single amino acid mutations in the cadherin receptor from Heliothis virescens affect its toxin binding ability to Cry1A toxins.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
2004年论文
@zh
2004年论文
@zh-cn
name
Single amino acid mutations in ...... nding ability to Cry1A toxins.
@en
Single amino acid mutations in ...... nding ability to Cry1A toxins.
@nl
type
label
Single amino acid mutations in ...... nding ability to Cry1A toxins.
@en
Single amino acid mutations in ...... nding ability to Cry1A toxins.
@nl
prefLabel
Single amino acid mutations in ...... nding ability to Cry1A toxins.
@en
Single amino acid mutations in ...... nding ability to Cry1A toxins.
@nl
P2093
P2860
P356
P1476
Single amino acid mutations in ...... nding ability to Cry1A toxins.
@en
P2093
Alejandra Bravo
Daniela I Oltean
Isabel Gomez
Linda S Ross
Mario Soberon
Meibao Zhuang
Sarjeet S Gill
P2860
P304
P356
10.1074/JBC.M408403200
P407
P577
2004-11-30T00:00:00Z