| scholarly article | Q13442814 |
| P50 | author | Takayuki Uchihashi | Q55856636 |
| Wilaiwan Sriwimol | Q88928921 | ||
| P2093 | author name string | Toshio Ando | |
| Chanan Angsuthanasombat | |||
| Chalermpol Kanchanawarin | |||
| Somsri Sakdee | |||
| Aratee Aroonkesorn | |||
| P2860 | cites work | Protease-resistant core form of Bacillus thuringiensis Cry1Ie: monomeric and oligomeric forms in solution | Q42024663 |
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| Novel preparation and characterization of the alpha4-loop-alpha5 membrane-perturbing peptide from the Bacillus thuringiensis Cry4Ba delta-endotoxin | Q42037127 | ||
| Crystal structure of the mosquito-larvicidal toxin Cry4Ba and its biological implications | Q42041533 | ||
| Oligomerization triggers binding of a Bacillus thuringiensis Cry1Ab pore-forming toxin to aminopeptidase N receptor leading to insertion into membrane microdomains. | Q42043195 | ||
| Importance of polarity of the α4-α5 loop residue-Asn(166) in the pore-forming domain of the Bacillus thuringiensis Cry4Ba toxin: implications for ion permeation and pore opening | Q42623052 | ||
| Asn183 in alpha5 is essential for oligomerisation and toxicity of the Bacillus thuringiensis Cry4Ba toxin | Q42997127 | ||
| Bacillus thuringiensis Cry4Aa insecticidal protein: functional importance of the intrinsic stability of the unique α4-α5 loop comprising the Pro-rich sequence | Q43001117 | ||
| Average protein density is a molecular-weight-dependent function. | Q43104992 | ||
| Cadherin-like receptor binding facilitates proteolytic cleavage of helix alpha-1 in domain I and oligomer pre-pore formation of Bacillus thuringiensis Cry1Ab toxin | Q43923822 | ||
| Lipid-induced conformation of helix 7 from the pore-forming domain of the Bacillus thuringiensis Cry4Ba toxin: implications for toxicity mechanism | Q44144658 | ||
| Structurally conserved aromaticity of Tyr249 and Phe264 in helix 7 is important for toxicity of the Bacillus thuringiensis Cry4Ba toxin | Q44171997 | ||
| Carbohydrate analysis by a phenol-sulfuric acid method in microplate format | Q46377666 | ||
| A conserved tetrameric interaction of cry toxin helix α3 suggests a functional role for toxin oligomerization. | Q51746740 | ||
| Lipid-induced pore formation of the Bacillus thuringiensis Cry1Aa insecticidal toxin. | Q52587999 | ||
| Structure and distribution of the Bacillus thuringiensis Cry4Ba toxin in lipid membranes. | Q52660372 | ||
| Guide to video recording of structure dynamics and dynamic processes of proteins by high-speed atomic force microscopy. | Q54508514 | ||
| A simplified procedure for lipid phosphorus analysis shows that digestion rates vary with phospholipid structure | Q70013978 | ||
| Phospholipid vesicle binding and aggregation by four novel fish annexins are differently regulated by Ca2+ | Q77910511 | ||
| Bacillus thuringiensis and its pesticidal crystal proteins | Q24548585 | ||
| CHARMM general force field: A force field for drug-like molecules compatible with the CHARMM all-atom additive biological force fields | Q24632987 | ||
| Role of receptors in Bacillus thuringiensis crystal toxin activity | Q24683647 | ||
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| Scalable molecular dynamics with NAMD | Q27860718 | ||
| EMAN: semiautomated software for high-resolution single-particle reconstructions | Q27860772 | ||
| Fourier shell correlation threshold criteria | Q28269234 | ||
| Crystal structure of insecticidal delta-endotoxin from Bacillus thuringiensis at 2.5 A resolution | Q28305378 | ||
| Monomer-monomer interactions drive the prepore to pore conversion of a beta-barrel-forming cholesterol-dependent cytolysin | Q30167667 | ||
| A high-speed atomic force microscope for studying biological macromolecules. | Q30732098 | ||
| Crystallization and preliminary X-ray crystallographic analysis of a full-length active form of the Cry4Ba toxin from Bacillus thuringiensis | Q33902171 | ||
| The structure and organization within the membrane of the helices composing the pore-forming domain of Bacillus thuringiensis delta-endotoxin are consistent with an "umbrella-like" structure of the pore | Q36522944 | ||
| Cadherin binding is not a limiting step for Bacillus thuringiensis subsp. israelensis Cry4Ba toxicity to Aedes aegypti larvae. | Q36940099 | ||
| Two conformational states of the membrane-associated Bacillus thuringiensis Cry4Ba delta-endotoxin complex revealed by electron crystallography: implications for toxin-pore formation | Q36975000 | ||
| The 3-dimensional structure of a hepatitis C virus p7 ion channel by electron microscopy | Q37293306 | ||
| Bacillus thuringiensis Cry1A toxins are versatile proteins with multiple modes of action: two distinct pre-pores are involved in toxicity | Q37671417 | ||
| Crystallizing membrane proteins using lipidic bicelles | Q37943570 | ||
| Bacillus thuringiensis insecticidal three-domain Cry toxins: mode of action, insect resistance and consequences for crop protection. | Q38006022 | ||
| High-speed atomic force microscopy | Q38071844 | ||
| Aedes aegypti membrane-bound alkaline phosphatase expressed in Escherichia coli retains high-affinity binding for Bacillus thuringiensis Cry4Ba toxin | Q38628253 | ||
| Two specific membrane-bound aminopeptidase N isoforms from Aedes aegypti larvae serve as functional receptors for the Bacillus thuringiensis Cry4Ba toxin implicating counterpart specificity | Q38887522 | ||
| Single molecule fluorescence study of the Bacillus thuringiensis toxin Cry1Aa reveals tetramerization | Q39712066 | ||
| Combined molecular dynamics and continuum solvent studies of the pre-pore Cry4Aa trimer suggest its stability in solution and how it may form pore | Q39829861 | ||
| Functional expression in insect cells of glycosylphosphatidylinositol-linked alkaline phosphatase from Aedes aegypti larval midgut: a Bacillus thuringiensis Cry4Ba toxin receptor | Q42018763 | ||
| P433 | issue | 34 | |
| P407 | language of work or name | English | Q1860 |
| P921 | main subject | Bacillus thuringiensis | Q310467 |
| P304 | page(s) | 20793-20803 | |
| P577 | publication date | 2015-06-25 | |
| P1433 | published in | Journal of Biological Chemistry | Q867727 |
| P1476 | title | Potential Prepore Trimer Formation by the Bacillus thuringiensis Mosquito-specific Toxin: MOLECULAR INSIGHTS INTO A CRITICAL PREREQUISITE OF MEMBRANE-BOUND MONOMERS. | |
| P478 | volume | 290 |
| Q37728092 | Biological Control Strategies for Mosquito Vectors of Arboviruses |
| Q37727963 | Functional Contributions of Positive Charges in the Pore-Lining Helix 3 of the Bordetella pertussis CyaA-Hemolysin to Hemolytic Activity and Ion-Channel Opening |
| Q41989174 | Functional characterization of Bacillus thuringiensis Cry toxin receptors explains resistance in insects. |
| Q55540372 | Helix α-3 inter-molecular salt bridges and conformational changes are essential for toxicity of Bacillus thuringiensis 3D-Cry toxin family. |
| Q64252697 | The C-Terminal Domain of the Cry4Ba Mosquito-Specific Toxin Serves as a Potential Membrane Anchor |
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