ArticlePharmaceutical research2012
Utilizing the estrogen receptor ligand-binding domain for controlled protein translocation to the insoluble fraction.
Article in Pharmaceutical research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
2 citing papers in PubMed, 4 citations in OpenAlex.
- Controlled access of p53 to the nucleus regulates its proteasomal degradation by MDM2.Molecular pharmaceutics · 2013Article
- A single mutant, A276S of p53, turns the switch to apoptosis.Molecular pharmaceutics · 2013Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
purposeThe estrogen receptor forms insoluble aggregates in the insoluble cytoskeletal subcellular fraction when bound to the antagonist fulvestrant. The ligand-binding domain was isolated and fused to signal sequences to target subcellular compartments. Sequestering a pro-apoptotic peptide tested the utility of a protein targeted to the insoluble fraction.
methodsThe ligand-binding domain of the estrogen receptor was isolated and fused with signal sequences, either a nuclear localization signal or nuclear export signal. The subcellular localization when bound to drug fulvestrant was examined, specifically its interaction with cytokeratins 8 and 18. The ability to target a therapeutic peptide to the insoluble fraction was tested by fusing a therapeutic coiled-coil from Bcr-Abl in K562 cells.
resultsThe estrogen receptor ligand-binding domain responds to fulvestrant by translocating to the insoluble fraction. Adding a signal sequence significantly limited the translocation to either the nucleus or cytoplasm. The cytokeratin 8/18 status of the cell did not alter this response. The therapeutic coiled-coil fused to ERLBD was inactivated upon ligand induction.
conclusionsIsolating the ligand-binding domain of the estrogen receptor creates a ligand-controllable protein capable of translocation to the insoluble fraction. This can be used to sequester an active peptide to alter its function.
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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.