ArticleMolecular and cellular biology2000
A new family of nuclear receptor coregulators that integrate nuclear receptor signaling through CREB-binding protein.
Article in Molecular and cellular biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
47 citing papers in PubMed, 103 citations in OpenAlex.
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- Orphan Nuclear Receptors TR2 and TR4 in Erythropoiesis: From Mechanisms to Therapies.Biomolecules · 2025Review
- Multiomics analyses and machine learning of nuclear receptor coactivator 6 reveal its essential role in hepatocellular carcinoma.Cancer science · 2023Article
- Regulation of Hepatic Gluconeogenesis by Nuclear Receptor Coactivator 6.Molecules and cells · 2022Article
- The MLL3/4 H3K4 methyltransferase complex in establishing an active enhancer landscape.Biochemical Society transactions · 2021Review
- The transcriptional co-activator NCOA6 promotes estrogen-induced GREB1 transcription by recruiting ERα and enhancing enhancer-promoter interactions.The Journal of biological chemistry · 2019Article
- Uterine receptivity, embryo attachment, and embryo invasion: Multistep processes in embryo implantation.Reproductive medicine and biology · 2019Review
- Absent, small or homeotic 2-like protein (ASH2L) enhances the transcription of the estrogen receptor α gene through GATA-binding protein 3 (GATA3).The Journal of biological chemistry · 2014Article
- Structural considerations of vitamin D signaling.Frontiers in physiology · 2014Review
- Vitamin D and the RNA transcriptome: more than mRNA regulation.Frontiers in physiology · 2014Review
- Nuclear receptor coactivator-6 attenuates uterine estrogen sensitivity to permit embryo implantation.Developmental cell · 2012Article
- Progesterone signaling mechanisms in brain and behavior.Frontiers in endocrinology · 2012Article
- Identification and characterization of the alternatively spliced nuclear receptor coactivator-6 isoforms.International journal of biological sciences · 2011Article
- Wolbachia as an "infectious" extrinsic factor manipulating host signaling pathways.Frontiers in endocrinology · 2011Article
- Nuclear receptor engineering based on novel structure activity relationships revealed by farnesyl pyrophosphate.Protein engineering, design & selection : PEDS · 2010Article
- Activation of progestin receptors in female reproductive behavior: Interactions with neurotransmitters.Frontiers in neuroendocrinology · 2010Review
- PRIC295, a Nuclear Receptor Coactivator, Identified from PPARα-Interacting Cofactor Complex.PPAR research · 2010Article
- Coactivators in PPAR-Regulated Gene Expression.PPAR research · 2010Article
- Characterization of ASC-2 as an antiatherogenic transcriptional coactivator of liver X receptors in macrophages.Molecular endocrinology (Baltimore, Md.) · 2009Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
We describe the cloning and characterization of a new family of nuclear receptor coregulators (NRCs) which modulate the function of nuclear hormone receptors in a ligand-dependent manner. NRCs are expressed as alternatively spliced isoforms which may exhibit different intrinsic activities and receptor specificities. The NRCs are organized into several modular structures and contain a single functional LXXLL motif which associates with members of the steroid hormone and thyroid hormone/retinoid receptor subfamilies with high affinity. Human NRC (hNRC) harbors a potent N-terminal activation domain (AD1), which is as active as the herpesvirus VP16 activation domain, and a second activation domain (AD2) which overlaps with the receptor-interacting LXXLL region. The C-terminal region of hNRC appears to function as an inhibitory domain which influences the overall transcriptional activity of the protein. Our results suggest that NRC binds to liganded receptors as a dimer and this association leads to a structural change in NRC resulting in activation. hNRC binds CREB-binding protein (CBP) with high affinity in vivo, suggesting that hNRC may be an important functional component of a CBP complex involved in mediating the transcriptional effects of nuclear hormone receptors.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.