Retargeting of the Bacillus thuringiensis toxin Cyt2Aa against hemipteran insect pests - Wikidata - awgldk - TriplyDB

Retargeting of the Bacillus thuringiensis toxin Cyt2Aa against hemipteran insect pests

Retargeting of the Bacillus thuringiensis toxin Cyt2Aa against hemipteran insect pests

http://www.wikidata.org/entity/Q36883934

about

Enhancing Integrated Pest Management in GM Cotton Systems Using Host Plant Resistance Bt toxin modification for enhanced efficacy New Cyt-like δ-endotoxins from Dickeya dadantii: structure and aphicidal activity Improvement and efficient display of Bacillus thuringiensis toxins on M13 phages and ribosomes Modification of Cry4Aa toward Improved Toxin Processing in the Gut of the Pea Aphid, Acyrthosiphon pisum In Vitro Evidence Supports Membrane Alanyl Aminopeptidase N as a Receptor for a Plant Virus in the Pea Aphid Vector.Loop replacements with gut-binding peptides in Cry1Ab domain II enhanced toxicity against the brown planthopper, Nilaparvata lugens (Stål).The Effect of an Interspersed Refuge on Aphis glycines (Hemiptera: Aphididae), Their Natural Enemies, and Biological Control.Continuous evolution of Bacillus thuringiensis toxins overcomes insect resistance.Plant resistance to aphid feeding: behavioral, physiological, genetic and molecular cues regulate aphid host selection and feeding.Engineering plants for aphid resistance: current status and future perspectives.Membrane binding and oligomer membrane insertion are necessary but insufficient for Bacillus thuringiensis Cyt1Aa toxicity.Efficacy of genetically modified Bt toxins alone and in combinations against pink bollworm resistant to Cry1Ac and Cry2Ab.Transgenic plants expressing the AaIT/GNA fusion protein show increased resistance and toxicity to both chewing and sucking pests.Cry64Ba and Cry64Ca, two ETX/MTX2 Bacillus thuringiensis insecticidal proteins against hemipteran pests.Analysis of Homologs of Cry-toxin Receptor-Related Proteins in the Midgut of a Non-Bt Target, Nilaparvata lugens (Stål) (Hemiptera: Delphacidae).Time influence on the interaction between Cyt2Aa2 and lipid/cholesterol bilayers.Engineering Bacillus thuringiensis Cyt1Aa toxin specificity from dipteran to lepidopteran toxicity.Recent advancement on chemical arsenal of Bt toxin and its application in pest management system in agricultural field.Identification of plant virus receptor candidates in the stylets of their aphid vectors.Computational and biological characterization of fusion proteins of two insecticidal proteins for control of insect pests.Expression of hybrid fusion protein (Cry1Ac::ASAL) in transgenic rice plants imparts resistance against multiple insect pests.Classes, Databases, and Prediction Methods of Pharmaceutically and Commercially Important Cystine-Stabilized Peptides.

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P2860

Retargeting of the Bacillus thuringiensis toxin Cyt2Aa against hemipteran insect pests

http://www.wikidata.org/entity/Q36883934

description

2013 nî lūn-bûn

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2013年の論文

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2013年論文

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2013年論文

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2013年論文

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2013年論文

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2013年論文

@zh-tw

2013年论文

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2013年论文

@zh

2013年论文

@zh-cn

name

Retargeting of the Bacillus thuringiensis toxin Cyt2Aa against hemipteran insect pests

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type

label

Retargeting of the Bacillus thuringiensis toxin Cyt2Aa against hemipteran insect pests

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Retargeting of the Bacillus thuringiensis toxin Cyt2Aa against hemipteran insect pests

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P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Retargeting of the Bacillus thuringiensis toxin Cyt2Aa against hemipteran insect pests

@en

P2093

Bryony C Bonning

http://www.w3.org/2001/XMLSchema#string

Huarong Li

http://www.w3.org/2001/XMLSchema#string

Kenneth E Narva

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Lucas B Linz

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Nanasaheb P Chougule

http://www.w3.org/2001/XMLSchema#string

Sijun Liu

http://www.w3.org/2001/XMLSchema#string

Thomas Meade

http://www.w3.org/2001/XMLSchema#string

P2860

TM-align: a protein structure alignment algorithm based on the TM-score

ProCKSI: a decision support system for Protein (structure) Comparison, Knowledge, Similarity and Information

LOMETS: a local meta-threading-server for protein structure prediction

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

Structure of the mosquitocidal delta-endotoxin CytB from Bacillus thuringiensis sp. kyushuensis and implications for membrane pore formation

Site-directed mutagenesis by overlap extension using the polymerase chain reaction

DaliLite workbench for protein structure comparison

Mirid bug outbreaks in multiple crops correlated with wide-scale adoption of Bt cotton in China

Cytolytic toxin Cyt1A and its mechanism of membrane damage: data and hypotheses.

A peptide that binds the pea aphid gut impedes entry of Pea enation mosaic virus into the aphid hemocoel.

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8465-8470

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scholarly article

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10.1073/PNAS.1222144110

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21

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110

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2013-05-06T00:00:00Z

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236644045

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23650347

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Bacillus thuringiensis

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