A critical role of helix 3-helix 5 interaction in steroid hormone receptor function - Wikidata - wikimedia - TriplyDB

A critical role of helix 3-helix 5 interaction in steroid hormone receptor function

A critical role of helix 3-helix 5 interaction in steroid hormone receptor function

http://www.wikidata.org/entity/Q33864134

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Dibutyltin disrupts glucocorticoid receptor function and impairs glucocorticoid-induced suppression of cytokine production Vestigialization of an Allosteric Switch: Genetic and Structural Mechanisms for the Evolution of Constitutive Activity in a Steroid Hormone Receptor Epithelial sodium transport and its control by aldosterone: the story of our internal environment revisited A Natural Mutation in Helix 5 of the Ligand Binding Domain of Glucocorticoid Receptor Enhances Receptor-Ligand Interaction Hydrogen/deuterium exchange reveals distinct agonist/partial agonist receptor dynamics within vitamin D receptor/retinoid X receptor heterodimer Structural analysis of the evolution of steroid specificity in the mineralocorticoid and glucocorticoid receptors.A substitution in the ligand binding domain of the porcine glucocorticoid receptor affects activity of the adrenal gland.DNA binding alters coactivator interaction surfaces of the intact VDR-RXR complex.Structure-Based Drug Design of Mineralocorticoid Receptor Antagonists to Explore Oxosteroid Receptor Selectivity.Characterization of a novel gain of function glucocorticoid receptor knock-in mouse Helix 3-helix 5 interactions in steroid hormone receptor function Unique ligand binding patterns between estrogen receptor alpha and beta revealed by hydrogen-deuterium exchange.A screening assay for Selective Dimerizing Glucocorticoid Receptor Agonists and Modulators (SEDIGRAM) that are effective against acute inflammation

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A critical role of helix 3-helix 5 interaction in steroid hormone receptor function

http://www.wikidata.org/entity/Q33864134

description

2005 nî lūn-bûn

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2005 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2005 թվականի փետրվարին հրատարակված գիտական հոդված

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2005年の論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年论文

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name

A critical role of helix 3-helix 5 interaction in steroid hormone receptor function

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A critical role of helix 3-helix 5 interaction in steroid hormone receptor function

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type

label

A critical role of helix 3-helix 5 interaction in steroid hormone receptor function

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A critical role of helix 3-helix 5 interaction in steroid hormone receptor function

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prefLabel

A critical role of helix 3-helix 5 interaction in steroid hormone receptor function

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A critical role of helix 3-helix 5 interaction in steroid hormone receptor function

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Proceedings of the National Academy of Sciences of the United States of America

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A critical role of helix 3-helix 5 interaction in steroid hormone receptor function

@en

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David S Geller

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Francis T F Tsai

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Jessica Simisky

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Junhui Zhang

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P2860

CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice

Crystal structure of the human RXRalpha ligand-binding domain bound to its natural ligand: 9-cis retinoic acid

Crystal structure of a heterodimeric complex of RAR and RXR ligand-binding domains

Asymmetry in the PPARgamma/RXRalpha crystal structure reveals the molecular basis of heterodimerization among nuclear receptors

Crystal structure of the glucocorticoid receptor ligand binding domain reveals a novel mode of receptor dimerization and coactivator recognition

Molecular basis of agonism and antagonism in the oestrogen receptor

Atomic structure of progesterone complexed with its receptor

Activating mineralocorticoid receptor mutation in hypertension exacerbated by pregnancy

Functional probing of the human glucocorticoid receptor steroid-interacting surface by site-directed mutagenesis. Gln-642 plays an important role in steroid recognition and binding

The mechanism of RU486 antagonism is dependent on the conformation of the carboxy-terminal tail of the human progesterone receptor.

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2707-2712

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scholarly article

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10.1073/PNAS.0409663102

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8

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15710879

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549476

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