ArticleJournal of controlled release : official journal of the Controlled Release Society2007
Optimizing the protein switch: altering nuclear import and export signals, and ligand binding domain.
Article in Journal of controlled release : official journal of the Controlled Release Society, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 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
18 citing papers in PubMed.
- A Novel PTPN2 Isoform Differentially Regulates Immune Response.European journal of immunology · 2026Article
- A Genetically Encoded Assay System to Quantify O-GlcNAc Transferase (OGT) Activity in Live Cells.Angewandte Chemie (International ed. in English) · 2025Article
- A chemical magnet: Approaches to guide precise protein localization.Bioorganic & medicinal chemistry · 2024Article
- μDamID: A Microfluidic Approach for Joint Imaging and Sequencing of Protein-DNA Interactions in Single Cells.Cell systems · 2020Article
- Functional Characterization of Glucocorticoid Receptor Variants Is Required to Avoid Misinterpretation of NGS Data.Journal of the Endocrine Society · 2019Article
- Nup2 performs diverse interphase functions in Aspergillus nidulans.Molecular biology of the cell · 2018Article
- Go in! Go out! Inducible control of nuclear localization.Current opinion in chemical biology · 2016Review
- Tuning response curves for synthetic biology.ACS synthetic biology · 2013Article
- Controlled access of p53 to the nucleus regulates its proteasomal degradation by MDM2.Molecular pharmaceutics · 2013Article
- Utilizing the estrogen receptor ligand-binding domain for controlled protein translocation to the insoluble fraction.Pharmaceutical research · 2012Article
- Selective targeting of c-Abl via a cryptic mitochondrial targeting signal activated by cellular redox status in leukemic and breast cancer cells.Pharmaceutical research · 2012Article
- Changing the subcellular location of the oncoprotein Bcr-Abl using rationally designed capture motifs.Pharmaceutical research · 2012Article
- Disruption of Bcr-Abl coiled coil oligomerization by design.The Journal of biological chemistry · 2011Article
- Controlling subcellular delivery to optimize therapeutic effect.Therapeutic delivery · 2010Review
- The nuclear translocation assay for intracellular protein-protein interactions and its application to the Bcr coiled-coil domain.BioTechniques · 2010Article
- Effect of anabolic-androgenic steroids and glucocorticoids on the kinetics of hAR and hGR nucleocytoplasmic translocation.Molecular pharmaceutics · 2010Article
- Controlling subcellular localization to alter function: Sending oncogenic Bcr-Abl to the nucleus causes apoptosis.Journal of controlled release : official journal of the Controlled Release Society · 2009Article
- Signal sequences for targeting of gene therapy products to subcellular compartments: the role of CRM1 in nucleocytoplasmic shuttling of the protein switch.Pharmaceutical research · 2007Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
Abstract
Ligand regulated localization controllable protein constructs were optimized in this study. Several constructs were made from a classical nuclear export signal (HIV-rev, MAPKK, or progesterone receptor) in combination with a SV40 T-antigen type nuclear import signal. Different ligand binding domains (LBDs from glucocorticoid receptor or progesterone receptor) were also tested for their ability to impart control over localization of proteins. This study was designed to create constructs which are cytoplasmic in the absence of ligand and nuclear in the presence of ligand, and also to regulate the amount of protein translocating to the nucleus on ligand induction. The balance between the strengths of import and export signals was critical for overall localization of proteins. The amount of protein entering the nucleus was also affected by the dose of ligand (10-100 nM). However, the overall import characteristics were determined by the strengths of localization signals and the inherent localization properties of the LBD used. This study established that the amount of protein present in a particular compartment can be regulated by the use of localization signals of various strengths. These optimized localization controllable protein constructs can be used to correct for diseases due to aberrant localization of proteins.
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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.