Structure and function of Nurr1 identifies a class of ligand-independent nuclear receptors (Q27641344)

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Gérard Benoit

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Jinsong Liu

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Srividya Prasad

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Piia Aarnisalo

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Xiaohong Liu

6

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Haoda Xu

7

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Nigel P C Walker

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Thomas Perlmann

The nuclear receptor superfamily: the second decade

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language of work or name

English

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publication date

29 May 2003

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published in

Nature

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volume

423

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page(s)

555-60

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issue

6939

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cites work

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The nuclear receptor ligand-binding domain: structure and function.

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Nuclear receptors and lipid physiology: opening the X-files

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Orphan nuclear receptors: shifting endocrinology into reverse

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Hepatocyte nuclear factor 4 is a transcription factor that constitutively binds fatty acids

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Crystal structure of the HNF4 alpha ligand binding domain in complex with endogenous fatty acid ligand

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Dopamine neuron agenesis in Nurr1-deficient mice

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Nurr1 is essential for the induction of the dopaminergic phenotype and the survival of ventral mesencephalic late dopaminergic precursor neurons

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Mutations in NR4A2 associated with familial Parkinson disease

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Activity of the Nurr1 Carboxyl-terminal Domain Depends on Cell Type and Integrity of the Activation Function 2

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A canonical structure for the ligand-binding domain of nuclear receptors

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

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Molecular basis of agonism and antagonism in the oestrogen receptor

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

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Structural and functional evidence for ligand-independent transcriptional activation by the estrogen-related receptor 3

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Structure and specificity of nuclear receptor-coactivator interactions

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

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Defining requirements for heterodimerization between the retinoid X receptor and the orphan nuclear receptor Nurr1.

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Evolution of the nuclear receptor superfamily: early diversification from an ancestral orphan receptor

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Ligand binding was acquired during evolution of nuclear receptors

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Phosphorylation and intramolecular stabilization of the ligand binding domain in the nuclear receptor steroidogenic factor 1.

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Structure-function analysis of the Rev-erbA and RVR ligand-binding domains reveals a large hydrophobic surface that mediates corepressor binding and a ligand cavity occupied by side chains

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The CCP4 suite: programs for protein crystallography

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Automated MAD and MIR structure solution

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[27] Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods.

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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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Identifiers

DOI

10.1038/NATURE01645

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Consolidated OpenCitations Corpus – April 2017

Dimensions Publication ID

1624652

1010597579

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Fatcat ID

release_marr53ad3fgynlubwc2ntifuzm

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1624652

1 reference

Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

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