Crystal structure of human estrogen-related receptor alpha in complex with a synthetic inverse agonist reveals its novel molecular mechanism (Q27645400)

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English	Crystal structure of human estrogen-related receptor alpha in complex with a synthetic inverse agonist reveals its novel molecular mechanism	scientific article

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scholarly article

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Crystal structure of human estrogen-related receptor alpha in complex with a synthetic inverse agonist reveals its novel molecular mechanism (English)

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crystal structure

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author name string

Joerg Kallen

1

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Rene Lattmann

2

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Rene Beerli

3

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Anke Blechschmidt

4

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Marcel J J Blommers

5

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Martin Geiser

6

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Johannes Ottl

7

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Jean-Marc Schlaeppi

8

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Andre Strauss

9

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Brigitte Fournier

10

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language of work or name

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publication date

10 August 2007

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Journal of Biological Chemistry

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282

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32

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23231-9

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The nuclear receptor superfamily: the second decade

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Orphan nuclear receptors: from gene to function

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Identification of a new class of steroid hormone receptors

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Transcriptional targets shared by estrogen receptor- related receptors (ERRs) and estrogen receptor (ER) alpha, but not by ERbeta

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To ERR in the estrogen pathway

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Reduced fat mass in mice lacking orphan nuclear receptor estrogen-related receptor alpha

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The estrogen-related receptor alpha (ERRalpha) functions in PPARgamma coactivator 1alpha (PGC-1alpha)-induced mitochondrial biogenesis

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Estrogen receptor-related receptor alpha: a mediator of estrogen response in bone.

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Molecular basis for the constitutive activity of estrogen-related receptor alpha-1.

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Evidence for ligand-independent transcriptional activation of the human estrogen-related receptor alpha (ERRalpha): crystal structure of ERRalpha ligand binding domain in complex with peroxisome proliferator-activated receptor coactivator-1alpha

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Identification of a selective inverse agonist for the orphan nuclear receptor estrogen-related receptor alpha

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Processing of X-ray diffraction data collected in oscillation mode

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MOLREP: an Automated Program for Molecular Replacement

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The CCP4 suite: programs for protein crystallography

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Refinement of macromolecular structures by the maximum-likelihood method

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Improved methods for building protein models in electron density maps and the location of errors in these models

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PROCHECK: a program to check the stereochemical quality of protein structures

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Spin labels as a tool to identify and characterize protein-ligand interactions by NMR spectroscopy

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Identifiers

10.1074/JBC.M703337200

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