Investigation of physicochemical condition to stabilize phosphatidylcholine-liposome enclosing fluorescent calcein and its exploitation for analysis of pore formation with Cry1A toxins of Bacillus thuringiensis-Reference-Cited by-同舟云学术

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Investigation of physicochemical condition to stabilize phosphatidylcholine-liposome enclosing fluorescent calcein and its exploitation for analysis of pore formation with Cry1A toxins of Bacillus thuringiensis

Published:2010 Issue:3 Volume:45 Page:477-488
ISSN:0003-6862
Container-title:Applied Entomology and Zoology
language:en
Short-container-title:Appl. Entomol. Zool.

Author:

Haginoya Kohsuke,Thangavel Vaijayanthi,Pandian Ganesh N.,Tomimoto Kazuya,Shitomi Yasuyuki,Azuma Masaaki,Angsuthanasombat Chanan,Hori Hidetaka

Publisher

Japanese Society of Applied Entomology & Zoology

Subject

Insect Science

Reference34 articles.

1. Oligomerization triggers binding of a Bacillus thuringiensis Cry1Ab pore-forming toxin to aminopeptidase N receptor leading to insertion into membrane microdomains

2. Delta-endotoxin-induced leakage of 86Rb+-K+ and H2O from phospholipid vesicles is catalyzed by reconstituted midgut membrane

3. Kinetics of pore formation by the Bacillus thuringiensis toxin Cry1Ac

4. Insertion and Organization within Membranes of the δ-Endotoxin Pore-forming Domain, Helix 4-Loop-Helix 5, and Inhibition of Its Activity by a Mutant Helix 4 Peptide

5. Identification, Isolation, and Cloning of a Bacillus thuringiensis CryIAc Toxin-binding Protein from the Midgut of the Lepidopteran Insect Heliothis virescens

Cited by 1 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. The C-Terminal Domain of the Bacillus thuringiensis Cry4Ba Mosquito-Specific Toxin Serves as a Potential Membrane Anchor;Toxins;2019-01-23

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