The Experts below are selected from a list of 37458 Experts worldwide ranked by ideXlab platform
Garry N Hannan - One of the best experts on this subject based on the ideXlab platform.
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the x ray structure of a Hemipteran ecdysone receptor ligand binding domain comparison with a lepidopteran ecdysone receptor ligand binding domain and implications for insecticide design
Journal of Biological Chemistry, 2005Co-Authors: Jennifer A Carmichael, Lloyd D Graham, Michael C Lawrence, Patricia A Pilling, Leonie Noyce, George O Lovrecz, David A Winkler, Anna Pawlakskrzecz, Ruth E Eaton, Garry N HannanAbstract:Abstract The ecdysone receptor is a hormone-dependent transcription factor that plays a central role in regulating the expression of vast networks of genes during development and reproduction in the phylum Arthropoda. The functional receptor is a heterodimer of the two nuclear receptor proteins ecdysone receptor (EcR) and ultraspiracle protein. The receptor is the target of the environmentally friendly bisacylhydrazine insecticides, which are effective against Lepidoptera but not against Hemiptera or several other insect orders. Here we present evidence indicating that much of the selectivity of the bisacylhydrazine insecticides can be studied at the level of their binding to purified ecdysone receptor ligand-binding domain (LBD) heterodimers. We report the crystal structure of the ecdysone receptor LBD heterodimer of the Hemipteran Bemisia tabaci (Bt, sweet potato whitefly) in complex with the ecdysone analogue ponasterone A. Although comparison with the corresponding known LBD structure from the lepidopteran Heliothis virescens (Hv) ecdysone receptor revealed the overall mode of ponasterone A binding to be very similar in the two cases, we observed that the BtEcR ecdysteroid-binding pocket is structured differently to that of HvEcR in those parts that are not in contact with ponasterone A. We suggest that these differences in the ligand-binding pocket may provide a molecular basis for the taxonomic order selectivity of bisacylhydrazine insecticides.
Jennifer A Carmichael - One of the best experts on this subject based on the ideXlab platform.
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the x ray structure of a Hemipteran ecdysone receptor ligand binding domain comparison with a lepidopteran ecdysone receptor ligand binding domain and implications for insecticide design
Journal of Biological Chemistry, 2005Co-Authors: Jennifer A Carmichael, Lloyd D Graham, Michael C Lawrence, Patricia A Pilling, Leonie Noyce, George O Lovrecz, David A Winkler, Anna Pawlakskrzecz, Ruth E Eaton, Garry N HannanAbstract:Abstract The ecdysone receptor is a hormone-dependent transcription factor that plays a central role in regulating the expression of vast networks of genes during development and reproduction in the phylum Arthropoda. The functional receptor is a heterodimer of the two nuclear receptor proteins ecdysone receptor (EcR) and ultraspiracle protein. The receptor is the target of the environmentally friendly bisacylhydrazine insecticides, which are effective against Lepidoptera but not against Hemiptera or several other insect orders. Here we present evidence indicating that much of the selectivity of the bisacylhydrazine insecticides can be studied at the level of their binding to purified ecdysone receptor ligand-binding domain (LBD) heterodimers. We report the crystal structure of the ecdysone receptor LBD heterodimer of the Hemipteran Bemisia tabaci (Bt, sweet potato whitefly) in complex with the ecdysone analogue ponasterone A. Although comparison with the corresponding known LBD structure from the lepidopteran Heliothis virescens (Hv) ecdysone receptor revealed the overall mode of ponasterone A binding to be very similar in the two cases, we observed that the BtEcR ecdysteroid-binding pocket is structured differently to that of HvEcR in those parts that are not in contact with ponasterone A. We suggest that these differences in the ligand-binding pocket may provide a molecular basis for the taxonomic order selectivity of bisacylhydrazine insecticides.
Frederic Francis - One of the best experts on this subject based on the ideXlab platform.
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insight into salivary gland proteomes of two polyphagous stink bugs nezara viridula l and halyomorpha halys stal
Proteomics, 2019Co-Authors: Laurent Serteyn, Frederic FrancisAbstract:The invasive brown marmorated stink bug (BMSB), Halyomorpha halys Stal, and the southern green stink bugs (SGSBs), Nezara viridula L., are widely distributed in Europe, even if the date of introduction and the diet differ. Saliva of Hemipteran pests plays essential roles in the interaction between insects and their host plants. The salivary proteomes of several aphid species have been studied and found to differ according to the species, while no comparative investigation between phytophagous stink bugs has been performed yet. Here, the salivary proteins from two bugs, BMSB and SGSB, are analyzed using LC-MS/MS. Data are available via ProteomeXchange with identifiers PXD011920 and PXD011976. A total of 238 and 305 proteins are identified in salivary glands of BMSB and SGSB, respectively. In comparison with salivary proteome from other Hemiptera, the most striking feature of the salivary gland proteomes of SGSB and BMSB is the similar pattern of protein functions between both species. Some of the proteins are speculated to play a significant role in plant-insect interactions. The results herein provide a framework for future research to elucidate the molecular basis of differential impact of piercing-sucking insects on host plants.
Leonie Noyce - One of the best experts on this subject based on the ideXlab platform.
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the x ray structure of a Hemipteran ecdysone receptor ligand binding domain comparison with a lepidopteran ecdysone receptor ligand binding domain and implications for insecticide design
Journal of Biological Chemistry, 2005Co-Authors: Jennifer A Carmichael, Lloyd D Graham, Michael C Lawrence, Patricia A Pilling, Leonie Noyce, George O Lovrecz, David A Winkler, Anna Pawlakskrzecz, Ruth E Eaton, Garry N HannanAbstract:Abstract The ecdysone receptor is a hormone-dependent transcription factor that plays a central role in regulating the expression of vast networks of genes during development and reproduction in the phylum Arthropoda. The functional receptor is a heterodimer of the two nuclear receptor proteins ecdysone receptor (EcR) and ultraspiracle protein. The receptor is the target of the environmentally friendly bisacylhydrazine insecticides, which are effective against Lepidoptera but not against Hemiptera or several other insect orders. Here we present evidence indicating that much of the selectivity of the bisacylhydrazine insecticides can be studied at the level of their binding to purified ecdysone receptor ligand-binding domain (LBD) heterodimers. We report the crystal structure of the ecdysone receptor LBD heterodimer of the Hemipteran Bemisia tabaci (Bt, sweet potato whitefly) in complex with the ecdysone analogue ponasterone A. Although comparison with the corresponding known LBD structure from the lepidopteran Heliothis virescens (Hv) ecdysone receptor revealed the overall mode of ponasterone A binding to be very similar in the two cases, we observed that the BtEcR ecdysteroid-binding pocket is structured differently to that of HvEcR in those parts that are not in contact with ponasterone A. We suggest that these differences in the ligand-binding pocket may provide a molecular basis for the taxonomic order selectivity of bisacylhydrazine insecticides.
Lloyd D Graham - One of the best experts on this subject based on the ideXlab platform.
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the x ray structure of a Hemipteran ecdysone receptor ligand binding domain comparison with a lepidopteran ecdysone receptor ligand binding domain and implications for insecticide design
Journal of Biological Chemistry, 2005Co-Authors: Jennifer A Carmichael, Lloyd D Graham, Michael C Lawrence, Patricia A Pilling, Leonie Noyce, George O Lovrecz, David A Winkler, Anna Pawlakskrzecz, Ruth E Eaton, Garry N HannanAbstract:Abstract The ecdysone receptor is a hormone-dependent transcription factor that plays a central role in regulating the expression of vast networks of genes during development and reproduction in the phylum Arthropoda. The functional receptor is a heterodimer of the two nuclear receptor proteins ecdysone receptor (EcR) and ultraspiracle protein. The receptor is the target of the environmentally friendly bisacylhydrazine insecticides, which are effective against Lepidoptera but not against Hemiptera or several other insect orders. Here we present evidence indicating that much of the selectivity of the bisacylhydrazine insecticides can be studied at the level of their binding to purified ecdysone receptor ligand-binding domain (LBD) heterodimers. We report the crystal structure of the ecdysone receptor LBD heterodimer of the Hemipteran Bemisia tabaci (Bt, sweet potato whitefly) in complex with the ecdysone analogue ponasterone A. Although comparison with the corresponding known LBD structure from the lepidopteran Heliothis virescens (Hv) ecdysone receptor revealed the overall mode of ponasterone A binding to be very similar in the two cases, we observed that the BtEcR ecdysteroid-binding pocket is structured differently to that of HvEcR in those parts that are not in contact with ponasterone A. We suggest that these differences in the ligand-binding pocket may provide a molecular basis for the taxonomic order selectivity of bisacylhydrazine insecticides.
