Helix 4 mutants of the Bacillus thuringiensis insecticidal toxin Cry1Aa display altered pore-forming abilities.
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Molecular approaches to improve the insecticidal activity of Bacillus thuringiensis Cry toxins.Helix alpha 4 of the Bacillus thuringiensis Cry1Aa toxin plays a critical role in the postbinding steps of pore formation.A mechanism of cell death involving an adenylyl cyclase/PKA signaling pathway is induced by the Cry1Ab toxin of Bacillus thuringiensis.Investigating the properties of Bacillus thuringiensis Cry proteins with novel loop replacements created using combinatorial molecular biology.Bacillus thuringiensis: a genomics and proteomics perspectiveStructural insights into Bacillus thuringiensis Cry, Cyt and parasporin toxinsCysteine scanning mutagenesis of alpha4, a putative pore-lining helix of the Bacillus thuringiensis insecticidal toxin Cry1Aa.Two conformational states of the membrane-associated Bacillus thuringiensis Cry4Ba delta-endotoxin complex revealed by electron crystallography: implications for toxin-pore formation.Dominant negative mutants of Bacillus thuringiensis Cry1Ab toxin function as anti-toxins: demonstration of the role of oligomerization in toxicity.Mutations in domain I interhelical loops affect the rate of pore formation by the Bacillus thuringiensis Cry1Aa toxin in insect midgut brush border membrane vesiclesBacillus thuringiensis insecticidal three-domain Cry toxins: mode of action, insect resistance and consequences for crop protection.A mechanical force contributes to the "osmotic swelling" of brush-border membrane vesicles.Aedes aegypti Mos20 cells internalizes cry toxins by endocytosis, and actin has a role in the defense against Cry11Aa toxin.Functional characterizations of residues Arg-158 and Tyr-170 of the mosquito-larvicidal Bacillus thuringiensis Cry4Ba.Isolation and characterization of a new Bacillus thuringiensis strain Lip harboring a new cry1Aa gene highly toxic to Ephestia kuehniella (Lepidoptera: Pyralidae) larvae.Domains II and III of Bacillus thuringiensis Cry1Ab toxin remain exposed to the solvent after insertion of part of domain I into the membrane.Cytotoxicity of Bacillus thuringiensis Cry1Ab toxin depends on specific binding of the toxin to the cadherin receptor BT-R1 expressed in insect cells.Rapid topology probing using fluorescence spectroscopy in planar lipid bilayer: the pore-forming mechanism of the toxin Cry1Aa of Bacillus thuringiensis.
P2860
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P2860
Helix 4 mutants of the Bacillus thuringiensis insecticidal toxin Cry1Aa display altered pore-forming abilities.
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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 October 2004
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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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Helix 4 mutants of the Bacillu ...... ltered pore-forming abilities.
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Helix 4 mutants of the Bacillu ...... ltered pore-forming abilities.
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Helix 4 mutants of the Bacillu ...... ltered pore-forming abilities.
@en
Helix 4 mutants of the Bacillu ...... ltered pore-forming abilities.
@nl
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Helix 4 mutants of the Bacillu ...... ltered pore-forming abilities.
@en
Helix 4 mutants of the Bacillu ...... ltered pore-forming abilities.
@nl
P2093
P2860
P1476
Helix 4 mutants of the Bacillu ...... ltered pore-forming abilities.
@en
P2093
Cécile Rang
Florence Coux
Gabrielle Préfontaine
Jean-Louis Schwartz
Luke Masson
Marc Juteau
Raynald Laprade
Roger Frutos
Roland Brousseau
Vincent Vachon
P2860
P304
P356
10.1128/AEM.70.10.6123-6130.2004
P407
P577
2004-10-01T00:00:00Z