(Q27635210)

English

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

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Niklas Blomberg

4

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author name string

P Cronet

1

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J F Petersen

2

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R Folmer

3

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K Sjöblom

5

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U Karlsson

6

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E L Lindstedt

7

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K Bamberg

8

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publication date

August 2001

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9

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8

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699-706

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Peroxisome proliferator-activated receptors: three isotypes for a multitude of functions

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PPARdelta is an APC-regulated target of nonsteroidal anti-inflammatory drugs

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Cyclo-oxygenase-2-derived prostacyclin mediates embryo implantation in the mouse via PPARdelta

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The PPARs: from orphan receptors to drug discovery

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

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Thiazolidinediones: an update.

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Regulation of Lipoprotein Metabolism by Thiazolidinediones Occurs through a Distinct but Complementary Mechanism Relative to Fibrates

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

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

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Crystal structure of the ligand binding domain of the human nuclear receptor PPARgamma

1 reference

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Molecular recognition of fatty acids by peroxisome proliferator-activated receptors

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Structural role of a detergent molecule in retinoic acid nuclear receptor crystals

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Ligand-induced stabilization of PPARgamma monitored by NMR spectroscopy: implications for nuclear receptor activation

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Crystal structure of the RAR-gamma ligand-binding domain bound to all-trans retinoic acid

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Dynamic stabilization of nuclear receptor ligand binding domains by hormone or corepressor binding

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The CCP4 suite: programs for protein crystallography

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Rapid automated molecular replacement by evolutionary search

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

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Errors in protein structures

1 reference

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Processing of X-ray diffraction data collected in oscillation mode

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Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution

1 reference

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Sensitivity enhancement in the TROSY experiment

1 reference

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NMR View: A computer program for the visualization and analysis of NMR data

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Identifiers

10.1016/S0969-2126(01)00634-7

1 reference

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

PubMed publication ID

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

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