Structural basis for antagonist-mediated recruitment of nuclear co-repressors by PPARalpha (Q27637763)

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Thomas B Stanley

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Valerie G Montana

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Millard H Lambert

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Barry G Shearer

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Jeffery E Cobb

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David D McKee

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Cristin M Galardi

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Kelli D Plunket

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Robert T Nolte

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Derek J Parks

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John T Moore

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Steven A Kliewer

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Timothy M Willson

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Julie B Stimmel

Ligand-independent repression by the thyroid hormone receptor mediated by a nuclear receptor co-repressor

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language of work or name

English

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publication date

14 February 2002

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published in

Nature

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volume

415

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issue

6873

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page(s)

813-7

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cites work

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A transcriptional co-repressor that interacts with nuclear hormone receptors

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Nuclear receptor repression mediated by a complex containing SMRT, mSin3A, and histone deacetylase

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Histone deacetylase activity is required for full transcriptional repression by mSin3A

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Histone deacetylases associated with the mSin3 corepressor mediate mad transcriptional repression

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SMRT corepressor interacts with PLZF and with the PML-retinoic acid receptor α (RARα) and PLZF-RARα oncoproteins associated with acute promyelocytic leukemia

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Fusion proteins of the retinoic acid receptor-alpha recruit histone deacetylase in promyelocytic leukaemia

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The partial agonist activity of antagonist-occupied steroid receptors is controlled by a novel hinge domain-binding coactivator L7/SPA and the corepressors N-CoR or SMRT

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Activation of a member of the steroid hormone receptor superfamily by peroxisome proliferators

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Structural determinants of ligand binding selectivity between the peroxisome proliferator-activated receptors

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Sequence and characterization of a coactivator for the steroid hormone receptor superfamily

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The structural basis of estrogen receptor/coactivator recognition and the antagonism of this interaction by tamoxifen

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Structure and specificity of nuclear receptor-coactivator interactions

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

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

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A signature motif in transcriptional co-activators mediates binding to nuclear receptors

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Discrete roles for peroxisome proliferator-activated receptor gamma and retinoid X receptor in recruiting nuclear receptor coactivators

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Mechanism of corepressor binding and release from nuclear hormone receptors.

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The CoRNR motif controls the recruitment of corepressors by nuclear hormone receptors

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Molecular determinants of nuclear receptor-corepressor interaction

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Nuclear receptors have distinct affinities for coactivators: characterization by fluorescence resonance energy transfer.

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Molecular recognition of fatty acids by peroxisome proliferator-activated receptors

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Differing roles for zinc fingers in DNA recognition: structure of a six-finger transcription factor IIIA complex

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

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A peroxisome proliferator-activated receptor gamma ligand inhibits adipocyte differentiation

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Luminescent oxygen channeling immunoassay: measurement of particle binding kinetics by chemiluminescence.

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Thyroid hormone resistance syndrome manifests as an aberrant interaction between mutant T3 receptors and transcriptional corepressors

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inferred from DOI database lookup

7 January 2021

based on heuristic

Processing of X-ray diffraction data collected in oscillation mode

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