Heliothis virescens and Manduca sexta lipid rafts are involved in Cry1A toxin binding to the midgut epithelium and subsequent pore formation.
about
Mode of action of Bacillus thuringiensis Cry and Cyt toxins and their potential for insect controlRole of receptors in Bacillus thuringiensis crystal toxin activityNew insight to structure-function relationship of GalNAc mediated primary interaction between insecticidal Cry1Ac toxin and HaALP receptor of Helicoverpa armigeraAn ABC transporter mutation is correlated with insect resistance to Bacillus thuringiensis Cry1Ac toxinSpecific 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.Role of alkaline phosphatase from Manduca sexta in the mechanism of action of Bacillus thuringiensis Cry1Ab toxinReduced levels of membrane-bound alkaline phosphatase are common to lepidopteran strains resistant to Cry toxins from Bacillus thuringiensis.Mitochondrial ceramide-rich macrodomains functionalize Bax upon irradiation.Analyses of Cry1Ab binding in resistant and susceptible strains of the European corn borer, Ostrinia nubilalis (Hubner) (Lepidoptera: Crambidae)Transcriptome differences between Cry1Ab resistant and susceptible strains of Asian corn borer.Ookinete-interacting proteins on the microvillar surface are partitioned into detergent resistant membranes of Anopheles gambiae midgutsIdentification of differentially expressed microRNAs between Bacillus thuringiensis Cry1Ab-resistant and -susceptible strains of Ostrinia furnacalis.The Anopheles-midgut APN1 structure reveals a new malaria transmission-blocking vaccine epitopeAssociation of Cry1Ac toxin resistance in Helicoverpa zea (Boddie) with increased alkaline phosphatase levels in the midgut lumenAedes aegypti alkaline phosphatase ALP1 is a functional receptor of Bacillus thuringiensis Cry4Ba and Cry11Aa toxins.Membrane insertion of the Bacillus thuringiensis Cry1Ab toxin: single mutation in domain II block partitioning of the toxin into the brush border membrane.Proteome analysis of Cry4Ba toxin-interacting Aedes aegypti lipid rafts using geLC-MS/MSAbout lipids and toxins.Aedes aegypti cadherin serves as a putative receptor of the Cry11Aa toxin from Bacillus thuringiensis subsp. israelensisCloning and epitope mapping of Cry11Aa-binding sites in the Cry11Aa-receptor alkaline phosphatase from Aedes aegypti.The pre-pore from Bacillus thuringiensis Cry1Ab toxin is necessary to induce insect death in Manduca sextaAnopheles gambiae cadherin AgCad1 binds the Cry4Ba toxin of Bacillus thuringiensis israelensis and a fragment of AgCad1 synergizes toxicity.Dominant negative mutants of Bacillus thuringiensis Cry1Ab toxin function as anti-toxins: demonstration of the role of oligomerization in toxicity.Identification and characterization of Aedes aegypti aminopeptidase N as a putative receptor of Bacillus thuringiensis Cry11A toxin.Effects of Periplocoside P from Periploca sepium on the Midgut Transmembrane Potential of Mythimna separata Larvae.Domain II loop 3 of Bacillus thuringiensis Cry1Ab toxin is involved in a "ping pong" binding mechanism with Manduca sexta aminopeptidase-N and cadherin receptors.Bacillus thuringiensis insecticidal three-domain Cry toxins: mode of action, insect resistance and consequences for crop protection.Bacillus thuringiensis: mechanism of action, resistance, and new applications: a review.The amphiphilic nature of saponins and their effects on artificial and biological membranes and potential consequences for red blood and cancer cells.Clostridium perfringens epsilon-toxin forms a heptameric pore within the detergent-insoluble microdomains of Madin-Darby canine kidney cells and rat synaptosomes.Cytotoxicity and binding profiles of activated Cry1Ac and Cry2Ab to three insect cell lines.Investigation of the Cry4B-prohibitin interaction in Aedes aegypti cells.Bt-R1a extracellular cadherin repeat 12 mediates Bacillus thuringiensis Cry1Ab binding and cytotoxicity.Roles of the Mevalonate Pathway and Cholesterol Trafficking in Pulmonary Host Defense.Bacillus thuringiensis ssp. israelensis Cyt1Aa enhances activity of Cry11Aa toxin by facilitating the formation of a pre-pore oligomeric structure.A GPI-anchored alkaline phosphatase is a functional midgut receptor of Cry11Aa toxin in Aedes aegypti 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.HT-SuperSAGE of the gut tissue of a Vip3Aa-resistant Heliothis virescens (Lepidoptera: Noctuidae) strain provides insights into the basis of resistance.Increased toxicity of Bacillus thuringiensis Cry3Aa against Crioceris quatuordecimpunctata, Phaedon brassicae and Colaphellus bowringi by a Tenebrio molitor cadherin fragment.Domains II and III of Bacillus thuringiensis Cry1Ab toxin remain exposed to the solvent after insertion of part of domain I into the membrane.
P2860
Q24679272-3C8181A0-2585-4F67-98C6-0C58278B9A1FQ24683647-9F9DD24F-B4BD-40BB-A920-13964DEEEC35Q27303507-152F6E86-8074-4A26-A35B-068CB78DA573Q28476551-4AEE1F7B-AE30-40BC-879B-1B121C2A6069Q33257320-0FE783E9-1817-4D64-8DE6-728BD671B287Q33800279-8E80E724-6E5B-431F-B646-AF0BF07305A7Q33842095-E3021266-C4E5-4D7D-9CAD-99499F390A1CQ33939529-D66C1794-D5FD-4C75-B2ED-1E54494EC1D9Q34973951-9738C116-95CA-448A-A98E-E4101CBC3FE4Q35521622-1CB80457-13DD-46EC-B6FE-1CA10DAA10D3Q35526306-31B540B6-35E3-4159-A726-0892C81A2F47Q35815106-472489AD-8D4D-42DA-A6E3-0E30D2C49637Q35989209-EF21040A-EF59-4DDE-8E80-8CB9BED7DE61Q36120281-05E0BE76-D04F-4841-BC1F-5561EAC99495Q36157304-0CD4DF91-991F-423C-B616-A65285CC3C5EQ36326957-281231AF-CCE2-44D3-ABED-142AE2EE3F23Q36567153-368B7609-1008-432A-B555-2EDCB04BEC8BQ36589899-CCCD1D67-BC73-4FB1-9351-CB56E17E5E19Q36985457-8877A293-B425-40DE-8BA9-82E3923F4A60Q36992398-384F416D-C304-485F-B58E-E17A9C4C4502Q37069589-57AF691A-55A0-4006-A455-F7622439E412Q37143721-0E6A8A91-2653-4303-9360-38214A19DB57Q37182468-41A2035B-455C-45AF-9B85-C2FA34CE1F6AQ37389707-8274CE7D-48E2-4139-A35D-B6AD324C7C99Q37408383-BA5435F8-FB6C-4222-A893-A1C489858521Q37432113-C9426342-4505-4661-9E56-16A9A15D3C5AQ38006022-C6ED0253-48BB-40B5-BCAB-72974DCB605EQ38255175-99E11D9D-4661-442A-8AC3-0B2FB9AF49B8Q38258125-12D1EA60-E32E-408D-87B5-E8DC7A6DF490Q38363668-B3E0A2C3-4500-4C77-9E6D-96248EA8D41AQ38714392-1439AD2B-D7C6-4333-B89C-2588F7AF879AQ39318932-1AAC7951-7D11-4467-84B5-DBF15710A1A6Q40559777-E7EA484C-B8F1-461A-9582-89BD17DEDE91Q40835741-0D08F6A3-FC32-493C-80D1-8002ADCB93EAQ41817794-A0474A3E-4CA1-46B5-9CB3-CB2AAD836919Q41866194-95C26107-EE59-4DA2-821C-E61532DE92E1Q41900192-251847D2-C217-4895-BC95-BE2E9B27A08AQ41986029-B9B15FD8-0289-4CD5-BB2A-7F2303775992Q42017602-A5E65A99-A634-4C51-B265-4DEE801A0E22Q42017688-A505B97A-B4AD-4A2D-8A11-DB4356EBE02A
P2860
Heliothis virescens and Manduca sexta lipid rafts are involved in Cry1A toxin binding to the midgut epithelium and subsequent pore formation.
description
2002 nî lūn-bûn
@nan
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
2002年论文
@zh
2002年论文
@zh-cn
name
Heliothis virescens and Manduc ...... and subsequent pore formation.
@en
Heliothis virescens and Manduc ...... and subsequent pore formation.
@nl
type
label
Heliothis virescens and Manduc ...... and subsequent pore formation.
@en
Heliothis virescens and Manduc ...... and subsequent pore formation.
@nl
prefLabel
Heliothis virescens and Manduc ...... and subsequent pore formation.
@en
Heliothis virescens and Manduc ...... and subsequent pore formation.
@nl
P2093
P2860
P356
P1476
Heliothis virescens and Manduc ...... and subsequent pore formation.
@en
P2093
Alejandra Bravo
Daniela I Oltean
Isabel Gómez
Mario Soberón
Meibao Zhuang
Sarjeet S Gill
P2860
P304
13863-13872
P356
10.1074/JBC.M110057200
P407
P577
2002-02-08T00:00:00Z