Binding of Bacillus thuringiensis proteins to a laboratory-selected line of Heliothis virescens.
about
Bacillus thuringiensis and its pesticidal crystal proteinsResistance to bio-insecticides or how to enhance their sustainability: a reviewDiversity of aminopeptidases, derived from four lepidopteran gene duplications, and polycalins expressed in the midgut of Helicoverpa armigera: identification of proteins binding the delta-endotoxin, Cry1Ac of Bacillus thuringiensis.Effects of midgut-protein-preparative and ligand binding procedures on the toxin binding characteristics of BT-R1, a common high-affinity receptor in Manduca sexta for Cry1A Bacillus thuringiensis toxins.Integrative model for binding of Bacillus thuringiensis toxins in susceptible and resistant larvae of the diamondback moth (Plutella xylostella)Identification of residues in domain III of Bacillus thuringiensis Cry1Ac toxin that affect binding and toxicityCommon, but complex, mode of resistance of Plutella xylostella to Bacillus thuringiensis toxins Cry1Ab and Cry1Ac.Development of Bacillus thuringiensis CryIC Resistance by Spodoptera exigua (Hubner) (Lepidoptera: Noctuidae)A Change in a Single Midgut Receptor in the Diamondback Moth (Plutella xylostella) Is Only in Part Responsible for Field Resistance to Bacillus thuringiensis subsp. kurstaki and B. thuringiensis subsp. aizawai.Resistance to Bacillus thuringiensis CryIA delta-endotoxins in a laboratory-selected Heliothis virescens strain is related to receptor alteration.The Bacillus thuringiensis insecticidal toxin binds biotin-containing proteins.Effect of Bacillus thuringiensis toxins on the membrane potential of lepidopteran insect midgut cells.Reversal of resistance to Bacillus thuringiensis in Plutella xylostellaDomain III of Bacillus thuringiensis Cry1Ie Toxin Plays an Important Role in Binding to Peritrophic Membrane of Asian Corn BorerDual resistance to Bacillus thuringiensis Cry1Ac and Cry2Aa toxins in Heliothis virescens suggests multiple mechanisms of resistanceBroad-spectrum resistance to Bacillus thuringiensis toxins in Heliothis virescensGenetic and biochemical characterization of field-evolved resistance to Bacillus thuringiensis toxin Cry1Ac in the diamondback moth, Plutella xylostella.Mutations in domain I of Bacillus thuringiensis delta-endotoxin CryIAb reduce the irreversible binding of toxin to manduca sexta brush border membrane vesicles.An Overview of Mechanisms of Cry Toxin Resistance in Lepidopteran Insects.Altered Glycosylation of 63- and 68-kilodalton microvillar proteins in Heliothis virescens correlates with reduced Cry1 toxin binding, decreased pore formation, and increased resistance to Bacillus thuringiensis Cry1 toxins.Comparison of toxin overlay and solid-phase binding assays to identify diverse CryIA(c) toxin-binding proteins in Heliothis virescens midgut.Altered binding of the Cry1Ac toxin to larval membranes but not to the toxin-binding protein in Plodia interpunctella selected for resistance to different Bacillus thuringiensis isolatesBinding of Insecticidal Crystal Proteins of Bacillus thuringiensis to the Midgut Brush Border of the Cabbage Looper, Trichoplusia ni (Hübner) (Lepidoptera: Noctuidae), and Selection for Resistance to One of the Crystal Proteins.Developmental studies of transgenic maize expressing Cry1Ab on the African stem borer, Busseola fusca; effects on midgut cellular structure.Development and characterisation of transgenic rice expressing two Bacillus thuringiensis genes.GalNAc pretreatment inhibits trapping of Bacillus thuringiensis Cry1Ac on the peritrophic membrane of Bombyx mori.Resistance to the Cry1Ac delta-endotoxin of Bacillus thuringiensis in the cotton bollworm, Helicoverpa armigera (Lepidoptera: Noctuidae).Role of two arginine residues in domain II, loop 2 of Cry1Ab and Cry1Ac Bacillus thuringiensis delta-endotoxin in toxicity and binding to Manduca sexta and Lymantria dispar aminopeptidase N.Proteinase-mediated insect resistance to Bacillus thuringiensis toxins.Irreversible binding kinetics of Bacillus thuringiensis CryIA delta-endotoxins to gypsy moth brush border membrane vesicles is directly correlated to toxicity.The CryIA(c) receptor purified from Manduca sexta displays multiple specificities.Kinetics of Bacillus thuringiensis toxin binding with brush border membrane vesicles from susceptible and resistant larvae of Plutella xylostella.Determination of Binding of Bacillus thuringiensis (delta)-Endotoxin Receptors to Rice Stem Borer Midguts.Binding of Bacillus thuringiensis Cry1Ac Toxin to Aminopeptidase in Susceptible and Resistant Diamondback Moths (Plutella xylostella).Resistance to bacillus thuringiensis Cry1Ac toxin in three strains of heliothis virescens: proteolytic and SEM study of the larval midgutInheritance of resistance to aBacillus thuringiensistoxin in a field population of diamondback moth (Plutella xylostella)
P2860
Q24548585-1BAF326B-BF23-4451-A566-88DD91A2C02DQ28085524-78614996-31DC-4C82-920B-9BA64D203D75Q30436490-2DD04CF2-6760-4F22-85ED-07029AF04194Q33709444-B1D0D8A6-7E26-4818-BF95-B8D356969C10Q33984554-A5A29D47-5F5A-4D9E-9036-3F8F9F391938Q33985781-69F1DD4F-0638-478A-BD1C-873155FB489DQ34143345-F7FAC856-BB0E-4C43-8FCA-F01F6CA4D23DQ34422719-A63345DC-B88F-4A0D-B422-C49E3DD480EEQ34424115-6376776F-36FF-4B04-BEF3-3A3226981DA0Q35186814-6BD1B984-3915-4B9A-A594-61C6F8097304Q35192649-8827306A-0E1E-45EF-9193-5F269331F051Q35200369-739B6C0F-FD18-45E5-955B-AE923FF9EC7FQ35216679-9942054B-940F-45A5-8E77-FE0E7A23631DQ35752243-5D6F22C1-01E3-4A96-9721-317346C120F7Q36049775-A5F9C323-B40C-4715-B49A-2CF89C0EC537Q37173338-4C7A3E86-9EE5-422D-B9D8-2D3EB68B6631Q37701993-B41E828C-8317-452B-B26E-A9B010826DA2Q38297485-C0837C14-9FE0-4321-A80B-27459C613DA6Q39196030-47026ECD-6252-46E6-A207-1EC32CA9D315Q39661703-FF24B8A7-B221-4BD6-9F40-26618A8ACD15Q39798033-5AABC9BA-98C5-4AEA-B355-50C821344FBEQ39801046-942788FD-03ED-4064-9ACA-93DC6B48E307Q39916422-8FEE5890-D724-4B07-9501-929FE4B2A256Q42016236-42AF24F0-D78E-4F71-9C74-3442292C4C52Q42017972-A424DF7D-ED23-4169-AA0A-75B5733B6EF4Q42043388-4F8A0A53-B5CA-4642-80DF-702D5F5A7F6BQ42046549-BCBBC2CE-38FD-4D11-8E42-EBCCEA383971Q42055391-ED0B507E-DDCB-4FA9-87D4-F38BA957F583Q42061716-27D63FA9-A349-48D2-9566-D2DB48E65B92Q42065569-9104F3C9-26A4-4934-B050-C03EB0C210FDQ42065778-7466373E-BE82-48CD-BCFD-F5DA3E25AA48Q42066331-6A3A9BD2-49AF-4316-A2F1-3450B1C3D245Q42124524-50AA1AFC-7DD1-4A0C-B264-F3056536DDCEQ43231781-2DA31142-6D11-4E30-A31C-862F58586DBCQ54080766-7B351995-2CF5-4772-B847-38927E960C85Q58046643-AB0F197C-F913-4C8F-85F6-1A34201F92B4
P2860
Binding of Bacillus thuringiensis proteins to a laboratory-selected line of Heliothis virescens.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on October 1991
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Binding of Bacillus thuringien ...... d line of Heliothis virescens.
@en
Binding of Bacillus thuringien ...... d line of Heliothis virescens.
@nl
type
label
Binding of Bacillus thuringien ...... d line of Heliothis virescens.
@en
Binding of Bacillus thuringien ...... d line of Heliothis virescens.
@nl
prefLabel
Binding of Bacillus thuringien ...... d line of Heliothis virescens.
@en
Binding of Bacillus thuringien ...... d line of Heliothis virescens.
@nl
P2093
P2860
P356
P1476
Binding of Bacillus thuringien ...... d line of Heliothis virescens.
@en
P2093
P2860
P304
P356
10.1073/PNAS.88.20.8930
P407
P577
1991-10-01T00:00:00Z