ecdysone/кариес зубов

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Highly flexible ligand binding pocket of ecdysone receptor: a single amino acid change leads to discrimination between two groups of nonsteroidal ecdysone agonists.

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The insect steroid hormone 20-hydroxyecdysone works through a ligand-activated nuclear receptor, the ecdysone receptor (EcR), which plays critical roles in insect development and reproduction. The EcR has been exploited to develop insecticides to control pests and gene switches for gene regulation.

Sequencing and structural homology modeling of the ecdysone receptor in two chrysopids used in biological control of pest insects.

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In insects, the process of molting and metamorphosis are mainly regulated by a steroidal hormone 20-hydroxyecdysone (20E) and its analogs (ecdysteroids) that specifically bind to the ecdysone receptor ligand-binding domain (EcR-LBD). Currently, several synthetic non-steroidal ecdysone agonists,

Structural changes under low evolutionary constraint may decrease the affinity of dibenzoylhydrazine insecticides for the ecdysone receptor in non-lepidopteran insects.

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Understanding how variations in genetic sequences are conveyed into structural and biochemical properties is of increasing interest in the field of molecular evolution. In order to gain insight into this process, we studied the ecdysone receptor (EcR), a transcription factor that controls moulting

Interpretation of scoring functions using 3D molecular fields. Mapping the diacyl-hydrazine-binding pocket of an insect ecdysone receptor.

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A method is presented for the interpretation of receptor docking score values (rough measures of binding affinities) of ligands in terms of 3D molecular field interaction contributions. The FlexX and FlexX-Pharm methods were used to dock the structures of designed sets of ligands into the

Dual inhibition of BACE1 and Aβ aggregation by β-ecdysone: Application of a phytoecdysteroid scaffold in Alzheimer's disease therapeutics.

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Current medications for the complex neurological disorder, Alzheimer's disease (AD), can neither stop disease progression nor revert back disease pathogenesis. The present study demonstrates the applicability of a phytoecdysteroid, β-ecdysone, as a multi-potent agent in AD therapeutics. β-ecdysone

Molecular cloning and characterization of Ecdysone oxidase and 3-dehydroecdysone-3α-reductase involved in the ecdysone inactivation pathway of silkworm, Bombyx mori.

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Molting hormone (ecdysteroid) is one of the most important hormones in insects. The synthesis and inactivation of the ecdysteroid regulate the developmental process of insects. A major pathway of ecdysone inactivation is that ecdysone is converted to 3-dehydroecdysone, and then further to

Molecular determinants of juvenile hormone action as revealed by 3D QSAR analysis in Drosophila.

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BACKGROUND Postembryonic development, including metamorphosis, of many animals is under control of hormones. In Drosophila and other insects these developmental transitions are regulated by the coordinate action of two principal hormones, the steroid ecdysone and the sesquiterpenoid juvenile hormone

Insect growth regulators as potential insecticides to control olive fruit fly (Bactrocera oleae Rossi): insect toxicity bioassays and molecular docking approach.

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BACKGROUND Olive fruit fly, Bactrocera oleae (Rossi), is a key pest in olive orchards, causing serious economic damage. To date, the pest has already developed resistance to the insecticides commonly applied to control it. Thus, in searching for new products for an accurate resistance management

Lenticles: innervated secretory structures that are expressed at every other larval moult.

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Lenticles are dome-shaped circles or ovals of cuticle with a dark rim. They occur with a precise segmental arrangement in the larvae and pupae of lycaenid and hesperiid butterflies. In Calpodes ethlius (Lepidoptera, Hesperiidae) each lenticle is secreted by a pair of large polyploid epidermal cells.

Selectivity of diacylhydrazine insecticides to the predatory bug Orius laevigatus: in vivo and modelling/docking experiments.

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BACKGROUND Knowledge of pesticide selectivity to natural enemies is necessary for a successful implementation of biological and chemical control methods in integrated pest management (IPM) programmes. Diacylhydrazine (DAH)-based ecdysone agonists, also known as moulting-accelerating compounds

Structural and functional characterization of the c-terminal domain of the ecdysteroid phosphate phosphatase from bombyx mori reveals a new enzymatic activity.

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Here, we present the crystal structure of the ecdysone phosphate phosphatase (EPPase) phosphoglycerate mutase (PGM) homology domain, the first structure of a steroid phosphate phosphatase. The structure reveals an alpha/beta-fold common to members of the two histidine (2H)-phosphatase superfamily

The structure of the ultraspiracle ligand-binding domain reveals a nuclear receptor locked in an inactive conformation.

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Ultraspiracle (USP) is the invertebrate homologue of the mammalian retinoid X receptor (RXR). RXR plays a uniquely important role in differentiation, development, and homeostasis through its ability to serve as a heterodimeric partner to many other nuclear receptors. RXR is able to influence the

Structure-based analysis of the ultraspiracle protein and docking studies of putative ligands.

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The ultraspiracle protein (USP) is the insect ortholog of the mammalian retinoid X receptor (RXR). Fundamental questions concern the functional role of USP as the heterodimerization partner of insect nuclear receptors such as the ecdysone receptor. The crystallographic structures of the ligand

The retinoid-X receptor ortholog, ultraspiracle, binds with nanomolar affinity to an endogenous morphogenetic ligand.

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The in vivo ligand-binding function and ligand-binding activity of the Drosophila melanogaster retinoid-X receptor (RXR) ortholog, ultraspiracle, toward natural farnesoid products of the ring gland were assessed. Using an equilibrium fluorescence-binding assay, farnesoid products in the juvenile

Insecticidal Constituents and Activity of Alkaloids from Cynanchum mongolicum.

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Based on MS and NMR data and bioassay-guided tracing, three insecticidal alkaloids I, II and III from Cynanchum mongolicum were identified to be antofine N-oxide, antofine and tylophorine. Alkaloid I was more toxic than alkaloids II and III, but they were less active against Spodoptera litura than

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