The X-ray Structure of RU486 Bound to the Progesterone Receptor in a Destabilized Agonistic Conformation - Wikidata - wikimedia - TriplyDB

The X-ray Structure of RU486 Bound to the Progesterone Receptor in a Destabilized Agonistic Conformation

The X-ray Structure of RU486 Bound to the Progesterone Receptor in a Destabilized Agonistic Conformation

http://www.wikidata.org/entity/Q27654859

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Structural Basis for Agonism and Antagonism for a Set of Chemically Related Progesterone Receptor Modulators Revealing a steroid receptor ligand as a unique PPARγ agonist Divergent Sequence Tunes Ligand Sensitivity in Phospholipid-regulated Hormone Receptors X-ray Structures of Progesterone Receptor Ligand Binding Domain in Its Agonist State Reveal Differing Mechanisms for Mixed Profiles of 11 -Substituted Steroids Differential responses of progesterone receptor membrane component-1 (Pgrmc1) and the classical progesterone receptor (Pgr) to 17β-estradiol and progesterone in hippocampal subregions that support synaptic remodeling and neurogenesis A new strategy for selective targeting of progesterone receptor with passive antagonists.Insights on glucocorticoid receptor activity modulation through the binding of rigid steroids.Diosgenin relieves goiter via the inhibition of thyrocyte proliferation in a mouse model of Graves' disease.A theoretical entropy score as a single value to express inhibitor selectivity.Melanoma antigen-A11 (MAGE-A11) enhances transcriptional activity by linking androgen receptor dimers.Tracking progesterone receptor-mediated actions in breast cancer Influence of domain interactions on conformational mobility of the progesterone receptor detected by hydrogen/deuterium exchange mass spectrometry.Structural and functional analysis of domains of the progesterone receptor.Exploring Flexibility of Progesterone Receptor Ligand Binding Domain Using Molecular Dynamics.Differential targeting of brain stress circuits with a selective glucocorticoid receptor modulator.Fluorescent ligand for human progesterone receptor imaging in live cells.Endocrine disrupting activities of the flavonoid nutraceuticals luteolin and quercetin.Recent patent trends in the field of progesterone receptor agonists and modulators.Structure of the glucocorticoid receptor, a flexible protein that can adapt to different ligands.A structural perspective on nuclear receptors as targets of environmental compounds.Development of N-(4-Phenoxyphenyl)benzenesulfonamide Derivatives as Novel Nonsteroidal Progesterone Receptor Antagonists.

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The X-ray Structure of RU486 Bound to the Progesterone Receptor in a Destabilized Agonistic Conformation

http://www.wikidata.org/entity/Q27654859

description

2009 nî lūn-bûn

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2009 թուականի Յուլիսին հրատարակուած գիտական յօդուած

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2009 թվականի հուլիսին հրատարակված գիտական հոդված

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2009年の論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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The X-ray Structure of RU486 B ...... bilized Agonistic Conformation

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The X-ray Structure of RU486 B ...... bilized Agonistic Conformation

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The X-ray Structure of RU486 B ...... bilized Agonistic Conformation

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The X-ray Structure of RU486 B ...... bilized Agonistic Conformation

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The X-ray Structure of RU486 B ...... bilized Agonistic Conformation

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The X-ray Structure of RU486 B ...... bilized Agonistic Conformation

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JBC.M109.007872

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Journal of Biological Chemistry

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The X-ray Structure of RU486 B ...... bilized Agonistic Conformation

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Hans C A Raaijmakers

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Joost C M Uitdehaag

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Judith E Versteegh

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P2860

The three-dimensional structures of antagonistic and agonistic forms of the glucocorticoid receptor ligand-binding domain: RU-486 induces a transconformation that leads to active antagonism

A structural and in vitro characterization of asoprisnil: a selective progesterone receptor modulator

NFκB selectivity of estrogen receptor ligands revealed by comparative crystallographic analyses

Crystal structures of rat vitamin D receptor bound to adamantyl vitamin D analogs: structural basis for vitamin D receptor antagonism and partial agonism

Atomic structure of progesterone complexed with its receptor

A graphical user interface to the CCP4 program suite

Refinement of macromolecular structures by the maximum-likelihood method

Nonsteroidal progesterone receptor ligands with unprecedented receptor selectivity

Determination of conformational changes in the progesterone receptor using ELISA-like assays

In vitro antiprogestational/antiglucocorticoid activity and progestin and glucocorticoid receptor binding of the putative metabolites and synthetic derivatives of CDB-2914, CDB-4124, and mifepristone

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10.1074/JBC.M109.007872

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