Distinction of the binding modes for human nuclear receptor ERRγ between bisphenol A and 4-hydroxytamoxifen
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- Structural Characteristics of Drosophila Estrogen-related Receptor Ligand Binding Domain to Capture the Peptide and Non-peptide Ligands
- Placenta Expressing the Greatest Quantity of Bisphenol A Receptor ERRγ among the Human Reproductive Tissues : Predominant Expression of Type-1 ERRγ Isoform
- The Conformation Change-Sensing Antibodies for Retinoid-Related Orphan Receptor Family
- Structural Evidence for Endocrine Disruptor Bisphenol A Binding to Human Nuclear Receptor ERRγ
- Induced-fit Type Ligand Binding Guided by Free-rotatory Leu Residue Present in the 7th α-Helix Peptide in the Estrogen-related Receptor γ (ERRγ)
- Bisphenol A-Specific Nuclear Receptor ERRγ : Structure-Function Analysis of the Two Novel Isoforms Lacking Vital Peptide Fragment in the Ligand Binding Domain
- Conformation Change of α-Helix Peptide for Sensing of Deactivation of Nuclear Receptor : Immunoassay Using Polyclonal Antibody Specific for the C-Terminal α-Helix 12 of Estrogen-Related Receptor γ(ERRγ)
- Distinction of the binding modes for human nuclear receptor ERRγ between bisphenol A and 4-hydroxytamoxifen
- Distinction of the binding modes for human nuclear receptor ERRγ between bisphenol A and 4-hydroxytamoxifen