ArticleThe EMBO journal1992
Cooperation of proto-signals for nuclear accumulation of estrogen and progesterone receptors.
Article in The EMBO journal, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 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
80 citing papers in PubMed, 314 citations in OpenAlex.
- Endothelial ERα promotes glucose tolerance by enhancing endothelial insulin transport to skeletal muscle.Nature communications · 2023Article
- A highly selective cell-based fluorescent biosensor for genistein detection.Engineering microbiology · 2023Article
- Promising Perspectives of the Antiproliferative GPER Inverse Agonist ERα17p in Breast Cancer.Cells · 2023Article
- Identification of a human estrogen receptor α tetrapeptidic fragment with dual antiproliferative and anti-nociceptive action.Scientific reports · 2023Article
- The emerging role of estrogen's non-nuclear signaling in the cardiovascular disease.Frontiers in cardiovascular medicine · 2023Review
- Demystifying the Functional Role of Nuclear Receptors in Esophageal Cancer.International journal of molecular sciences · 2022Review
- Importins involved in the nuclear transportation of steroid hormone receptors:Frontiers in endocrinology · 2022Article
- The Antitumor Peptide ERα17p Exerts Anti-Hyperalgesic and Anti-Inflammatory Actions Through GPER in Mice.Frontiers in endocrinology · 2021Article
- Transportin-2 plays a critical role in nucleocytoplasmic shuttling of oestrogen receptor-α.Scientific reports · 2020Article
- Selective Progesterone Receptor Modulators-Mechanisms and Therapeutic Utility.Endocrine reviews · 2020Review
- R269C variant of ESR1: high prevalence and differential function in a subset of pancreatic cancers.BMC cancer · 2020Article
- Article
- The Peptide ERα17p Is a GPER Inverse Agonist that Exerts Antiproliferative Effects in Breast Cancer Cells.Cells · 2019Article
- Estrogen receptor subcellular localization and cardiometabolism.Molecular metabolism · 2018Review
- Review
- Development of selective androgen receptor modulators (SARMs).Molecular and cellular endocrinology · 2018Review
- The N-terminal domain of the androgen receptor drives its nuclear localization in castration-resistant prostate cancer cells.The Journal of steroid biochemistry and molecular biology · 2014Article
- Rapid estrogen signaling negatively regulates PTEN activity through phosphorylation in endometrial cancer cells.Hormones & cancer · 2014Article
- Androgen receptor gene mutation, rearrangement, polymorphism.Translational andrology and urology · 2013Article
- Controlled access of p53 to the nucleus regulates its proteasomal degradation by MDM2.Molecular pharmaceutics · 2013Article
20 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
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Multiple proto-signals (p-NLSs) for nuclear targeting, none of which suffices on its own, cooperate in the estrogen (ER) and progesterone (PR) receptors. In the ER, an estrogen-inducible p-NLS was found in the hormone binding domain (HBD), in addition to three lysine/arginine-rich motifs resembling prototype constitutive nuclear localization signals (NLSs). The inducible and the constitutive ER p-NLSs cooperate in the presence of estrogen and hydroxy-tamoxifen, but not in the presence of ICI 164,384. In the PR, three p-NLSs, two of which are located within and directly adjacent to the second zinc finger, cooperate with each other and a weak hormone-inducible p-NLS in the PR HBD. No 'masking' of p-NLSs by the HBD was observed for ER and PR, while the ligand-free glucocorticoid receptor HBD inhibited the activity of both homologous and heterologous NLSs. Nuclear co-translocation experiments indicated that in vivo the stability of ER and PR dimers is hormonally controlled, but that, in the absence of the cognate ligand, ER dimers are more stable than PR dimers. This is likely to account for the differential hormone requirement of ER and PR DNA binding in vitro.
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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.