Engineering modified Bt toxins to counter insect resistance.
about
Bt toxin modification for enhanced efficacyAn ABC transporter mutation is correlated with insect resistance to Bacillus thuringiensis Cry1Ac toxinMolecular approaches to improve the insecticidal activity of Bacillus thuringiensis Cry toxins.Affinity maturation of Cry1Aa toxin to the Bombyx mori cadherin-like receptor by directed evolution.Contributions of gut bacteria to Bacillus thuringiensis-induced mortality vary across a range of Lepidoptera.Interactions between Bacillus anthracis and plants may promote anthrax transmission.ABCC2 is associated with Bacillus thuringiensis Cry1Ac toxin oligomerization and membrane insertion in diamondback mothRole of alkaline phosphatase from Manduca sexta in the mechanism of action of Bacillus thuringiensis Cry1Ab toxinBacillus thuringiensis Cry3Aa fused to a cellulase-binding peptide shows increased toxicity against the longhorned beetle.Identification of a novel aminopeptidase P-like gene (OnAPP) possibly involved in Bt toxicity and resistance in a major corn pest (Ostrinia nubilalis)Improving Cry8Ka toxin activity towards the cotton boll weevil (Anthonomus grandis)Plant science. Communal benefits of transgenic corn.Structural insights into Bacillus thuringiensis Cry, Cyt and parasporin toxinsResistance of Trichoplusia ni to Bacillus thuringiensis toxin Cry1Ac is independent of alteration of the cadherin-like receptor for Cry toxinsEvidence of field-evolved resistance of Spodoptera frugiperda to Bt corn expressing Cry1F in Brazil that is still sensitive to modified Bt toxins.Parallel evolution of Bacillus thuringiensis toxin resistance in lepidoptera.Identification of a New cry1I-Type Gene as a Candidate for Gene Pyramiding in Corn To Control Ostrinia Species Larvae.Binding and Oligomerization of Modified and Native Bt Toxins in Resistant and Susceptible Pink Bollworm.Evolutionary ecology of insect adaptation to Bt crops.Association of Cry1Ac toxin resistance in Helicoverpa zea (Boddie) with increased alkaline phosphatase levels in the midgut lumenDual mode of action of Bt proteins: protoxin efficacy against resistant insectsRetargeting of the Bacillus thuringiensis toxin Cyt2Aa against hemipteran insect pestsSodium solute symporter and cadherin proteins act as Bacillus thuringiensis Cry3Ba toxin functional receptors in Tribolium castaneumAedes aegypti cadherin serves as a putative receptor of the Cry11Aa toxin from Bacillus thuringiensis subsp. israelensisDifferential role of Manduca sexta aminopeptidase-N and alkaline phosphatase in the mode of action of Cry1Aa, Cry1Ab, and Cry1Ac toxins from Bacillus thuringiensis.Delaying insect resistance to transgenic crops.Biotechnological prospects for engineering insect-resistant plants.A Spodoptera exigua cadherin serves as a putative receptor for Bacillus thuringiensis Cry1Ca toxin and shows differential enhancement of Cry1Ca and Cry1Ac toxicity.The outlook for protein engineering in crop improvement.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 vesiclesAsymmetrical cross-resistance between Bacillus thuringiensis toxins Cry1Ac and Cry2Ab in pink bollworm.Strategies to improve the insecticidal activity of Cry toxins from Bacillus thuringiensis.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.Cadherin fragments from Anopheles gambiae synergize Bacillus thuringiensis Cry4Ba's toxicity against Aedes aegypti larvae.Novel giant siphovirus from Bacillus anthracis features unusual genome characteristics.Risk assessment of toxins derived from Bacillus thuringiensis-synergism, efficacy, and selectivityResponses of the cutworm Spodoptera litura (Lepidoptera: Noctuidae) to two Bt corn hybrids expressing Cry1AbBacillus thuringiensis Cry1A toxins are versatile proteins with multiple modes of action: two distinct pre-pores are involved in toxicity.Bacillus thuringiensis: A story of a successful bioinsecticide.
P2860
Q26824423-68A19264-8B65-4CC1-AE48-86FEDBE029B7Q28476551-655DF21E-BB79-4D04-AB18-43D9F04311D4Q30365704-A1A59226-2E9E-4FA6-BBCC-4D668843D431Q31109314-7C072F04-4A86-4522-9B35-C6C497E78557Q33414857-66C6D977-2612-474A-98EB-39F7FE6BCF18Q33716614-C32AC532-B44C-4B16-9A91-075B34E974B6Q33725872-532D01EE-478D-4F8B-949B-EB475B27E31BQ33800279-FDDC8F0F-D7B1-460C-B459-0F06519C7BDBQ33993000-E078A0F7-8CB4-452D-AAF8-63DC4894B0FCQ34009751-C9B4DBCE-A39E-4E74-9C5C-AEF38B1CA026Q34015232-1C258B3D-DE04-4A18-AD45-2C88468973A5Q34142266-236D3C23-D2D6-48B2-8B66-184C8A69EF0FQ34263404-F85A65F4-B4C0-420C-AB8B-2F8CDA47B0A0Q34273507-E12A740F-0398-4C31-BAF6-7B003CF21923Q35241989-F88AB482-68A2-45A8-9A6A-205A88098827Q35298029-0E4D8EEB-96C8-408C-BF6E-34AFBACF9CB5Q35573432-582F9FDB-7BDD-4801-BE89-DE1E6F5C71ADQ35860164-C0E494CA-E6A7-48A5-AFCD-913FC2F0AFC0Q35961110-1E8AA348-F2FB-4C7D-81E7-CFABC93A3C8DQ36120281-88AA4F5E-D1B0-4FED-9CCF-467E5429364BQ36146639-7F69E6A3-2F05-4F80-999E-3B12ADA5C747Q36883934-1F2558DA-C530-4705-9437-829819904AB5Q36947721-0A9D5BCF-941C-4101-BA0A-F5E776B3459BQ36985457-7734E2A1-C2A4-48B1-8AA6-793218F29B26Q37035889-6FE89248-AA97-48F6-91B4-98F947F8FB6AQ37039363-572A163A-D90C-4824-AA07-4320F0D46AB4Q37100658-E599F6FB-70EA-45C1-8E63-C9F8725B0C68Q37123645-B649CC5A-B174-454C-AA35-CEDEB5D0A579Q37149684-50223BFF-32DA-4867-8B41-547877D717B6Q37182468-AD5B4573-52E8-4B21-B4B2-18C3408076C3Q37232467-AAA2A1E4-B1F1-4299-AAEE-0E6FEA4D891FQ37251701-F5EB9869-5E5D-40C8-8E9D-EE781413F4D3Q37261642-62E0C444-D75A-4B6F-A8F1-EA9E447DCA20Q37432113-78B365C8-579F-4EDE-A420-200EF631E827Q37451313-37C6E585-D252-4C41-919D-6DBDB6D8AD8EQ37520648-562D7429-73A2-4566-88AB-345B2F105DBDQ37532086-5F6368C9-E29D-4366-BE8D-52F710B9A272Q37635007-5E19EEB0-5B4D-49D0-8287-C8B9409BA4E3Q37671417-F21F9ABE-24F6-458D-8580-6438FFE37679Q37849891-01AD104B-2DDD-4303-AC0B-4B9821764DA5
P2860
Engineering modified Bt toxins to counter insect resistance.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
2007年论文
@zh
2007年论文
@zh-cn
name
Engineering modified Bt toxins to counter insect resistance.
@en
Engineering modified Bt toxins to counter insect resistance.
@nl
type
label
Engineering modified Bt toxins to counter insect resistance.
@en
Engineering modified Bt toxins to counter insect resistance.
@nl
prefLabel
Engineering modified Bt toxins to counter insect resistance.
@en
Engineering modified Bt toxins to counter insect resistance.
@nl
P2093
P2860
P50
P356
P1433
P1476
Engineering modified Bt toxins to counter insect resistance
@en
P2093
Idalia López
Isabel Gómez
Mario Soberón
P2860
P304
P356
10.1126/SCIENCE.1146453
P407
P577
2007-11-01T00:00:00Z