Tryptophan spectroscopy studies and black lipid bilayer analysis indicate that the oligomeric structure of Cry1Ab toxin from Bacillus thuringiensis is the membrane-insertion intermediate.
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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 activitySpecific 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.Assessment of cry1 gene contents of Bacillus thuringiensis strains by use of DNA microarrays.Peptide-lipid interactions: insights and perspectives.Cadherin binding is not a limiting step for Bacillus thuringiensis subsp. israelensis Cry4Ba toxicity to Aedes aegypti larvae.The pre-pore from Bacillus thuringiensis Cry1Ab toxin is necessary to induce insect death in Manduca sextaCase study and application of process analytical technology (PAT) towards bioprocessing: Use of tryptophan fluorescence as at-line tool for making pooling decisions for process chromatography.Bacillus thuringiensis Cry1A toxins are versatile proteins with multiple modes of action: two distinct pre-pores are involved in toxicity.Bacillus thuringiensis insecticidal three-domain Cry toxins: mode of action, insect resistance and consequences for crop protection.An overview of the safety and biological effects of Bacillus thuringiensis Cry toxins in mammals.Effects and mechanisms of Bacillus thuringiensis crystal toxins for mosquito larvae.Functional characterizations of residues Arg-158 and Tyr-170 of the mosquito-larvicidal Bacillus thuringiensis Cry4Ba.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)Role of tryptophan residues in toxicity of Cry1Ab toxin from Bacillus thuringiensis.Preliminary comparing the toxicities of the hybrid cry1Acs fused with different heterogenous genes provided guidance for the fusion expression of Cry proteins.Domains II and III of Bacillus thuringiensis Cry1Ab toxin remain exposed to the solvent after insertion of part of domain I into the membrane.Bacillus thuringiensis Cry1Ab mutants affecting oligomer formation are non-toxic to Manduca sexta larvae.Permeability changes of Manduca sexta midgut brush border membranes induced by oligomeric structures of different cry toxins.Single amino acid mutations in the cadherin receptor from Heliothis virescens affect its toxin binding ability to Cry1A toxins.Unfolding events in the water-soluble monomeric Cry1Ab toxin during transition to oligomeric pre-pore and membrane-inserted pore channel.Composition of the Putative Prepore Complex of Bacillus thuringiensis Cry1Ab Toxin.Mitochondria permeabilization by a novel polycation peptide BTM-P1.
P2860
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P2860
Tryptophan spectroscopy studies and black lipid bilayer analysis indicate that the oligomeric structure of Cry1Ab toxin from Bacillus thuringiensis is the membrane-insertion intermediate.
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
Tryptophan spectroscopy studie ...... mbrane-insertion intermediate.
@en
Tryptophan spectroscopy studie ...... mbrane-insertion intermediate.
@nl
type
label
Tryptophan spectroscopy studie ...... mbrane-insertion intermediate.
@en
Tryptophan spectroscopy studie ...... mbrane-insertion intermediate.
@nl
prefLabel
Tryptophan spectroscopy studie ...... mbrane-insertion intermediate.
@en
Tryptophan spectroscopy studie ...... mbrane-insertion intermediate.
@nl
P2093
P356
P1433
P1476
Tryptophan spectroscopy studie ...... mbrane-insertion intermediate.
@en
P2093
Alejandra Bravo
Carlos Muñoz-Garay
Carolina Rausell
Enrique Rudiño-Piñera
Isabel Gómez
Mario Soberón
Raúl Miranda-CassoLuengo
P304
P356
10.1021/BI035527D
P407
P577
2004-01-01T00:00:00Z