Resistance to Bacillus thuringiensis CryIA delta-endotoxins in a laboratory-selected Heliothis virescens strain is related to receptor alteration.
about
Bacillus thuringiensis and its pesticidal crystal proteinsAlanine scanning analyses of the three major loops in domain II of Bacillus thuringiensis mosquitocidal toxin Cry4AaExpressed sequence tags from larval gut of the European corn borer (Ostrinia nubilalis): Exploring candidate genes potentially involved in Bacillus thuringiensis toxicity and resistanceAn ABC transporter mutation is correlated with insect resistance to Bacillus thuringiensis Cry1Ac toxinInheritance patterns, dominance and cross-resistance of Cry1Ab- and Cry1Ac-selected Ostrinia furnacalis (Guenée)Binding site alteration is responsible for field-isolated resistance to Bacillus thuringiensis Cry2A insecticidal proteins in two Helicoverpa speciesPhage display of a biologically active Bacillus thuringiensis toxin.Investigating the properties of Bacillus thuringiensis Cry proteins with novel loop replacements created using combinatorial molecular biology.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 toxicityDevelopment and characterization of diamondback moth resistance to transgenic broccoli expressing high levels of Cry1CImportance of Cry1 delta-endotoxin domain II loops for binding specificity in Heliothis virescens (L.).Binding analyses of Bacillus thuringiensis Cry delta-endotoxins using brush border membrane vesicles of Ostrinia nubilalisA 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 Toxin Cry2Ab in Trichoplusia ni Is Conferred by a Novel Genetic Mechanism.Shared midgut binding sites for Cry1A.105, Cry1Aa, Cry1Ab, Cry1Ac and Cry1Fa proteins from Bacillus thuringiensis in two important corn pests, Ostrinia nubilalis and Spodoptera frugiperdaAnalyses of Cry1Ab binding in resistant and susceptible strains of the European corn borer, Ostrinia nubilalis (Hubner) (Lepidoptera: Crambidae)Aminopeptidase N purified from gypsy moth brush border membrane vesicles is a specific receptor for Bacillus thuringiensis CryIAc toxin.Genetic mapping of resistance to Bacillus thuringiensis toxins in diamondback moth using biphasic linkage analysisOne gene in diamondback moth confers resistance to four Bacillus thuringiensis toxinsDual resistance to Bacillus thuringiensis Cry1Ac and Cry2Aa toxins in Heliothis virescens suggests multiple mechanisms of resistanceInitial frequency of alleles for resistance to Bacillus thuringiensis toxins in field populations of Heliothis virescensSeeking the root of insect resistance to transgenic plants.Membrane insertion of the Bacillus thuringiensis Cry1Ab toxin: single mutation in domain II block partitioning of the toxin into the brush border membrane.Production and characterization of Bacillus thuringiensis Cry1Ac-resistant cotton bollworm Helicoverpa zea (Boddie).Cadherin fragments from Anopheles gambiae synergize Bacillus thuringiensis Cry4Ba's toxicity against Aedes aegypti larvae.Toxicity, binding, and permeability analyses of four Bacillus thuringiensis Cry1 delta-endotoxins using brush border membrane vesicles of Spodoptera exigua and Spodoptera frugiperdaPartial purification and characterization of Bacillus thuringiensis Cry1A toxin receptor A from Heliothis virescens and cloning of the corresponding cDNA.Shared binding sites in Lepidoptera for Bacillus thuringiensis Cry1Ja and Cry1A toxins.Role of Bacillus thuringiensis Cry1 delta endotoxin binding in determining potency during lepidopteran larval developmentExtent of variation of the Bacillus thuringiensis toxin reservoir: the case of the geranium bronze, Cacyreus marshalli butler (Lepidoptera: Lycaenidae).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.Different domains of Bacillus thuringiensis delta-endotoxins can bind to insect midgut membrane proteins on ligand blotsCross-resistance of the diamondback moth indicates altered interactions with domain II of Bacillus thuringiensis toxinsAltered 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 isolatesInteraction of Bacillus thuringiensis toxins with larval midgut binding sites of Helicoverpa armigera (Lepidoptera: Noctuidae).Molecular and insecticidal characterization of a Cry1I protein toxic to insects of the families Noctuidae, Tortricidae, Plutellidae, and Chrysomelidae.Mutations in the Bacillus thuringiensis Cry1Ca toxin demonstrate the role of domains II and III in specificity towards Spodoptera exigua larvae.Bacillus thuringiensis Cry1Ac toxin-binding and pore-forming activity in brush border membrane vesicles prepared from anterior and posterior midgut regions of lepidopteran larvae.Toxicity and mode of action of Bacillus thuringiensis Cry proteins in the Mediterranean corn borer, Sesamia nonagrioides (Lefebvre).
P2860
Q24548585-1B9BF2A9-7FBE-4362-A861-32AC4972B0CFQ24655827-97AE0F01-5B7E-414B-8C68-F9C4E0612E57Q27489028-1C476688-7503-49FA-BBD7-180F6AA3CD2DQ28476551-D50760DD-0FCB-45FE-82CD-90880647C946Q28655266-08C27A87-FF97-4E2F-A36C-CB4ED9A13572Q28748216-A08F2F7F-7C34-4EDA-9C40-7FFC0032CA01Q32047606-8D9880B0-F805-4009-959E-01C23DC955B1Q33327924-6EF9A0F6-0BE8-4742-8886-0647C7687EF0Q33984554-15333E13-BF0D-4966-9F9F-550C9D9FC1C4Q33985781-A2E155EA-A9F3-4FB5-96F4-7DBAE9D1C860Q33987570-F2E238DB-F153-4435-9954-BAD7CAF21DC9Q33988664-9E2A6DC7-5F77-41D8-8A51-226CF813396BQ33988936-E5A23EF3-098E-474E-910C-1E6BA59114ECQ34424115-D316EF5C-6253-416F-9B5E-FBC9FE9CC77BQ34670060-F049DA72-E072-45CD-A710-1EB08ECF2618Q34827000-99E2E708-3006-4ADF-8494-369A90EF55ECQ34973951-CA446308-C86B-4B2D-B5CA-792426452C20Q35192496-3A6D210E-F783-4E79-A653-A3E17F71EA49Q35547008-B0B82A94-E8D3-4349-8C4A-7F2E09A455E1Q36018416-EED794CD-9841-4B75-9EF3-90CA597FD8A5Q36049775-B9B0A7FD-C2DF-405D-A7A7-D69FC5AA324DQ36100935-67847E0F-D2B4-4F1A-A436-264EAFC790E9Q36153395-39EEA5F8-7263-4EB2-A941-AF4B4861B1E2Q36326957-83748416-B637-43FE-AD82-8DFF521A9007Q36420937-12760D0C-2EE5-4118-99E7-AE0BFEEB9C8AQ37451313-B8F21451-96BC-4BE6-8AE8-9DE6ACDC03EFQ39480261-0E566207-F0AA-48E6-B589-50FB0328AB25Q39483638-29F8DAB5-C597-450B-9CC3-EF5059109CC3Q39493579-E226C762-3ACE-473E-809E-C3A03DF44433Q39639703-BE8C3A73-19F7-4F38-9600-0D06761CC81DQ39640250-777D3B0B-07CD-47FB-865E-4FAB5BA41DF0Q39661703-0CE5D24D-9CC4-4300-A2BE-AB5BE4FA782FQ39800238-3EB564AB-BFA9-4C02-8A88-33F9F6B79C57Q39800287-C9A5CD05-1A40-46D1-BB31-B2B1C76AC879Q39801046-F0527DFB-3900-49C8-9881-A17FBA0B58D7Q40673201-D9F6F9BC-8019-4715-9758-288890637BD2Q41485137-F9015642-7B06-4203-B272-84DC024553A8Q41883699-8CF6CBC9-02E2-44DC-A42F-1094DE4D30CFQ41900192-CC71F8A4-2F60-4CDE-830C-CD30B0A71F62Q42037852-63C87698-BAA8-43B1-B277-B31241579BCC
P2860
Resistance to Bacillus thuringiensis CryIA delta-endotoxins in a laboratory-selected Heliothis virescens strain is related to receptor alteration.
description
1995 nî lūn-bûn
@nan
1995 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
Resistance to Bacillus thuring ...... elated to receptor alteration.
@ast
Resistance to Bacillus thuring ...... elated to receptor alteration.
@en
type
label
Resistance to Bacillus thuring ...... elated to receptor alteration.
@ast
Resistance to Bacillus thuring ...... elated to receptor alteration.
@en
prefLabel
Resistance to Bacillus thuring ...... elated to receptor alteration.
@ast
Resistance to Bacillus thuring ...... elated to receptor alteration.
@en
P2093
P2860
P1476
Resistance to Bacillus thuring ...... elated to receptor alteration.
@en
P2093
P2860
P304
P407
P577
1995-11-01T00:00:00Z