Larval diapause termination in the bamboo borer, Omphisa fuscidentalis. [PDF]
In insects, juvenile hormone (JH) and 20-hydroxyecdysone (20E) regulate larval growth and molting. However, little is known about how this cooperative control is terminating larval diapause especially in the bamboo borer, Omphisa fuscidentalis.
Suphawan Suang+7 more
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Identification of Ecdysone Hormone Receptor Agonists as a Therapeutic Approach for Treating Filarial Infections. [PDF]
BACKGROUND:A homologue of the ecdysone receptor has previously been identified in human filarial parasites. As the ecdysone receptor is not found in vertebrates, it and the regulatory pathways it controls represent attractive potential chemotherapeutic ...
Amruta S Mhashilkar+8 more
doaj +1 more source
Critical Role of Desolvation in the Binding of 20-Hydroxyecdysone to the Ecdysone Receptor [PDF]
The insect steroid hormone 20-hydroxyecdysone (20E) binds to its cognate nuclear receptor composed of the ecdysone receptor (EcR) and Ultraspiracle (USP) and triggers the main developmental transitions, in particular molting and metamorphosis. We present the crystal structure of the ligand-binding domains of EcR/USP in complex with 20E at 2.4A ...
Christopher R. Browning+7 more
openalex +6 more sources
Molecular evidence for a functional ecdysone signaling system in Brugia malayi. [PDF]
BACKGROUND:Filarial nematodes, including Brugia malayi, the causative agent of lymphatic filariasis, undergo molting in both arthropod and mammalian hosts to complete their life cycles.
George Tzertzinis+7 more
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The ecdysone receptor puzzle [PDF]
The present article reviews some recent findings on the functional ecdysone† receptor which is a heterodimer of two proteins: ecdysone receptor (EcR) and Ultraspiracle (USP). Emphasis is given to some unique aspects of this receptor, in particular to its dimerization, binding to DNA, and transactivation capabilities.
Thomas Bergman+3 more
openaire +2 more sources
Interactions of ultraspiracle with ecdysone receptor in the transduction of ecdysone‐ and juvenile hormone‐signaling [PDF]
Analyses of integration of two‐hormone signaling through the vertebrate nuclear hormone receptors, for which the retinoid X receptor is one partner, have generated a number of mechanistic models, including those described as ‘subordination’ models wherein ligand‐activation of one partner is subordinate to the liganded state of the other partner ...
Fang Fang+3 more
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26-[125I]iodoponasterone A is a potent ecdysone and a sensitive radioligand for ecdysone receptors. [PDF]
The effects of ecdysone, the steroid molting hormone of arthropods, are of considerable interest both to insect physiologists and to those studying steroid-regulated gene expression. Yet progress in understanding ecdysone receptors has been inhibited by the lack of a suitable highly radioactive hormone analog with high affinity for the receptor.
Shoei-Sheng Lee+3 more
openaire +3 more sources
Nuclear receptor DHR4 controls the timing of steroid hormone pulses during Drosophila development. [PDF]
In insects, precisely timed periodic pulses of the molting hormone ecdysone control major developmental transitions such as molts and metamorphosis. The synthesis and release of ecdysone, a steroid hormone, is itself controlled by PTTH (prothoracicotopic
Qiuxiang Ou+2 more
doaj +1 more source
Plasticity of the Ecdysone Receptor DNA Binding Domain [PDF]
Ecdysteroids coordinate molting and metamorphosis in insects via a heterodimer of two nuclear receptors, the ecdysone receptor (EcR) and the ultraspiracle (Usp) protein. Here we show how the DNA-recognition alpha-helix and the T box region of the EcR DNA-binding domain (EcRDBD) contribute to the specific interaction with the natural response element ...
Anna Zoglowek+10 more
openaire +3 more sources
Cryptocephal, the Drosophila melanogaster ATF4, is a specific coactivator for ecdysone receptor isoform B2. [PDF]
The ecdysone receptor is a heterodimer of two nuclear receptors, the Ecdysone receptor (EcR) and Ultraspiracle (USP). In Drosophila melanogaster, three EcR isoforms share common DNA and ligand-binding domains, but these proteins differ in their most N ...
Sebastien A Gauthier+4 more
doaj +1 more source