ReviewThe Biochemical journal1996
Steroid hormone receptors and their regulation by phosphorylation.
Review in The Biochemical journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It is linked to trial NCT03261336 (A Phase II Study of Oral Calcitriol in Combination With Ketoconazole in Castration Resistant Prostate Cancer, Progressing Despite Primary ADT and Abiraterone), which is not on this map. Cited by 70 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.
The trial behind it
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.
A Phase II Study of Oral Calcitriol in Combination With Ketoconazole in Castration Resistant Prostate Cancer, Progressing Despite Primary ADT and Abiraterone
Who cites it
70 citing papers in PubMed, 357 citations in OpenAlex.
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- New insights into the role of thyroid hormone in cardiac remodeling: time to reconsider?Heart failure reviews · 2011Review
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- CDK9 regulates AR promoter selectivity and cell growth through serine 81 phosphorylation.Molecular endocrinology (Baltimore, Md.) · 2010Article
- The progesterone receptor hinge region regulates the kinetics of transcriptional responses through acetylation, phosphorylation, and nuclear retention.Molecular endocrinology (Baltimore, Md.) · 2010Article
- Phosphorylation of estrogen receptor beta at serine 105 is associated with good prognosis in breast cancer.The American journal of pathology · 2010Article
- ERalpha increases expression and interacts with TERT in cataractous canine lens epithelial cells.Molecular vision · 2009Article
- Integrated actions of progesterone receptor and cell cycle machinery regulate breast cancer cell proliferation.Steroids · 2009Review
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- Progesterone receptors act as sensors for mitogenic protein kinases in breast cancer models.Endocrine-related cancer · 2009Review
- A novel role of Shc adaptor proteins in steroid hormone-regulated cancers.Endocrine-related cancer · 2009Review
- Glucocorticoid receptor phosphorylation differentially affects target gene expression.Molecular endocrinology (Baltimore, Md.) · 2008Article
10 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The steroid/thyroid hormone receptor superfamily of ligand-activated transcription factors encompasses not only the receptors for steroids, thyroid hormone, retinoids and vitamin D, but also a large number of proteins whose functions and/or ligands are unknown and which are thus termed orphan receptors. Recent studies have highlighted the importance of phosphorylation in receptor function. Although most of the phosphorylation sites are serine and threonine residues, a few of the family members are also phosphorylated on tyrosine. Those steroid receptor family members that are bound to heat-shock proteins in the absence of ligand typically are basally phosphorylated and exhibit increases in phosphorylation upon ligand binding. Most of these sites contain Ser-Pro motifs, and there is evidence that cyclin-dependent kinases and MAP kinases (mitogen-activated protein kinases) phosphorylate subsets of these sites. In contrast, phosphorylation sites identified thus far in members of the family that bind to DNA in the absence of hormone typically do not contain Ser-Pro motifs and are frequently casein kinase II or protein kinase A sites. Phosphorylation has been implicated in DNA binding, transcriptional activation and stability of the receptors. The finding that some of the steroid receptor family members can be activated in the absence of ligand by growth factors or neurotransmitters that modulate kinase and/or phosphatase pathways underscores the role of phosphorylation in receptor function. Hence this family of transcription factors integrates signals from ligands as well as from signal transduction pathways, resulting in alterations in mRNA and protein expression that are unique to the complex signals received.
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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.