(Q27644330)

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Insights into the mechanism of partial agonism: crystal structures of the peroxisome proliferator-activated receptor gamma ligand-binding domain in the complex with two enantiomeric ligands

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scholarly article

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Insights into the mechanism of partial agonism: crystal structures of the peroxisome proliferator-activated receptor gamma ligand-binding domain in the complex with two enantiomeric ligands (English)

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crystal structure

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based on heuristic

inferred from title

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based on heuristic

inferred from title

Antonio Laghezza

object named as

Antonio Laghezza

10

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Giuseppe Fracchiolla

object named as

Giuseppe Fracchiolla

8

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Maurizio Crestani

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Maurizio Crestani

14

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object named as

Nico Mitro

3

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Antonio Lavecchia

object named as

Antonio Lavecchia

11

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Ettore Novellino

object named as

Ettore Novellino

12

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Giorgio Pochetti

1

object named as

Giorgio Pochetti

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2

object named as

Cristina Godio

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Fulvio Loiodice

7

object named as

Fulvio Loiodice

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Paolo Tortorella

9

object named as

Paolo Tortorella

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13

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Fernando Mazza

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author name string

Donatella Caruso

4

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Andrea Galmozzi

5

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Samuele Scurati

6

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language of work or name

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publication date

8 June 2007

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Journal of Biological Chemistry

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282

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17314-24

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23

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PPARs: therapeutic targets for metabolic disease

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The mechanisms of action of PPARs

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Fatty acids and eicosanoids regulate gene expression through direct interactions with peroxisome proliferator-activated receptors alpha and gamma

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Structural studies on nuclear receptors.

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Peroxisome proliferator-activated receptors: nuclear control of metabolism

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The peroxisome proliferator-activated receptor:retinoid X receptor heterodimer is activated by fatty acids and fibrate hypolipidaemic drugs

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Crystal structure of a mutant hERalpha ligand-binding domain reveals key structural features for the mechanism of partial agonism

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An antidiabetic thiazolidinedione is a high affinity ligand for peroxisome proliferator-activated receptor gamma (PPAR gamma)

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A novel partial agonist of peroxisome proliferator-activated receptor-gamma (PPARgamma) recruits PPARgamma-coactivator-1alpha, prevents triglyceride accumulation, and potentiates insulin signaling in vitro

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A peroxisome proliferator-activated receptor gamma ligand inhibits adipocyte differentiation

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Coordinated control of cholesterol catabolism to bile acids and of gluconeogenesis via a novel mechanism of transcription regulation linked to the fasted-to-fed cycle

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Structure of the PPARalpha and -gamma ligand binding domain in complex with AZ 242; ligand selectivity and agonist activation in the PPAR family

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Synthesis and biological and structural characterization of the dual-acting peroxisome proliferator-activated receptor alpha/gamma agonist ragaglitazar

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Processing of X-ray diffraction data collected in oscillation mode

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Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

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Ligand binding and co-activator assembly of the peroxisome proliferator-activated receptor-gamma

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Molecular determinants of the balance between co-repressor and co-activator recruitment to the retinoic acid receptor.

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1 reference

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

1 reference

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Alteration of a Single Amino Acid in Peroxisome Proliferator-Activated Receptor- (PPAR ) Generates a PPAR Phenotype

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Identifiers

10.1074/JBC.M702316200

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

OpenCitations bibliographic resource ID

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

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