Agrotis segetum midgut putative receptor of Bacillus thuringiensis vegetative insecticidal protein Vip3Aa16 differs from that of Cry1Ac toxin.
about
Annual Migration of Agrotis segetum (Lepidoptera: Noctuidae): Observed on a Small Isolated Island in Northern China.Transcriptional profiling analysis of Spodoptera litura larvae challenged with Vip3Aa toxin and possible involvement of trypsin in the toxin activationCharacterization of the resistance to Vip3Aa in Helicoverpa armigera from Australia and the role of midgut processing and receptor bindingBacterial Vegetative Insecticidal Proteins (Vip) from Entomopathogenic Bacteria.Cry1Ac and Vip3Aa proteins from Bacillus thuringiensis targeting Cry toxin resistance in Diatraea flavipennella and Elasmopalpus lignosellus from sugarcaneFunctional characterization of Vip3Ab1 and Vip3Bc1: Two novel insecticidal proteins with differential activity against lepidopteran pests.The Vip3Ag4 Insecticidal Protoxin from Bacillus thuringiensis Adopts A Tetrameric Configuration That Is Maintained on ProteolysisEffects of Site-Mutations Within the 22 kDa No-Core Fragment of the Vip3Aa11 Insecticidal Toxin of Bacillus thuringiensis.Quantification of Bacillus thuringiensis Vip3Aa16 Entomopathogenic Toxin Using Its Hemolytic Activity.Toxicity, activation process, and histopathological effect of Bacillus thuringiensis vegetative insecticidal protein Vip3Aa16 on Tuta absoluta.Insights into the Structure of the Vip3Aa Insecticidal Protein by Protease Digestion Analysis.Improvement of Vip3Aa16 Toxin Production and Efficiency Through Nitrous Acid and UV Mutagenesis of Bacillus thuringiensis (Bacillales: Bacillaceae).Transgenic cotton co-expressing chimeric Vip3AcAa and Cry1Ac confers effective protection against Cry1Ac-resistant cotton bollworm.Production of polyclonal and monoclonal antibodies against the Bacillus thuringiensis vegetative insecticidal protein Vip3Aa16.Critical amino acids for the insecticidal activity of Vip3Af from Bacillus thuringiensis: Inference on structural aspects.Scavenger receptor-C acts as a receptor for Bacillus thuringiensis vegetative insecticidal protein Vip3Aa and mediates the internalization of Vip3Aa via endocytosisRelação entre toxicidade de proteínas Vip3Aa e sua capacidade de ligação a receptores intestinais de lepidópteros-pragaEffects of Vip3AcAa+Cry1Ac Cotton on Midgut Tissue in Helicoverpa armigera (Lepidoptera: Noctuidae)
P2860
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P2860
Agrotis segetum midgut putative receptor of Bacillus thuringiensis vegetative insecticidal protein Vip3Aa16 differs from that of Cry1Ac toxin.
description
2013 nî lūn-bûn
@nan
2013年の論文
@ja
2013年学术文章
@wuu
2013年学术文章
@zh-cn
2013年学术文章
@zh-hans
2013年学术文章
@zh-my
2013年学术文章
@zh-sg
2013年學術文章
@yue
2013年學術文章
@zh
2013年學術文章
@zh-hant
name
Agrotis segetum midgut putativ ...... ers from that of Cry1Ac toxin.
@en
Agrotis segetum midgut putativ ...... ers from that of Cry1Ac toxin.
@nl
type
label
Agrotis segetum midgut putativ ...... ers from that of Cry1Ac toxin.
@en
Agrotis segetum midgut putativ ...... ers from that of Cry1Ac toxin.
@nl
prefLabel
Agrotis segetum midgut putativ ...... ers from that of Cry1Ac toxin.
@en
Agrotis segetum midgut putativ ...... ers from that of Cry1Ac toxin.
@nl
P2093
P1476
Agrotis segetum midgut putativ ...... ers from that of Cry1Ac toxin.
@en
P2093
Dorra Ben Hamadou-Charfi
Hanen Boukedi
Lobna Abdelkefi-Mesrati
Samir Jaoua
Slim Tounsi
P304
P356
10.1016/J.JIP.2013.07.003
P577
2013-07-20T00:00:00Z