ArticleAAPS pharmSci2002
Model system to study classical nuclear export signals.
Article in AAPS pharmSci, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 26 citations in OpenAlex.
- Properties of LINE-1 proteins and repeat element expression in the context of amyotrophic lateral sclerosis.Mobile DNA · 2018Article
- Review
- Article
- Beyond NF-κB activation: nuclear functions of IκB kinase α.Journal of biomedical science · 2013Review
- Nuclear export of proteins and drug resistance in cancer.Biochemical pharmacology · 2012Review
- Identification of a functional, CRM-1-dependent nuclear export signal in hepatitis C virus core protein.PloS one · 2011Article
- Ubiquitin-regulated nuclear-cytoplasmic trafficking of the Nipah virus matrix protein is important for viral budding.PLoS pathogens · 2010Article
- 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
- The Caenorhabditis elegans Elongator complex regulates neuronal alpha-tubulin acetylation.PLoS genetics · 2010Article
- 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
- Optimizing the protein switch: altering nuclear import and export signals, and ligand binding domain.Journal of controlled release : official journal of the Controlled Release Society · 2007Article
- Controlling protein compartmentalization to overcome disease.Pharmaceutical research · 2007Review
- Geldanamycin, an inhibitor of Hsp90, blocks cytoplasmic retention of progesterone receptors and glucocorticoid receptors via their respective ligand binding domains.The AAPS journal · 2006Article
- Progesterone receptor isoform identification and subcellular localization in endometrial cancer.Gynecologic oncology · 2005Article
- Correlation among agonist dose, rate of import, and transcriptional activity of liganded progesterone receptor B isoform in living cells.Pharmaceutical research · 2003Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Signal-mediated protein transport through the nuclear pore complex is of considerable interest in the field of molecular pharmaceutics. Nuclear localization signals can be used to target genes/antisense delivery systems to the nucleus. Studying nuclear export is useful in enhancing the expression and the efficiency of action of these therapeutic agents. The mechanism of nuclear import has been well studied and most of the proteins participating in this mechanism have been identified. The subject of nuclear export is still in the initial stages, and there is a considerable amount of uncertainty in this area. Two main export receptors identified so far are Exportin 1 (Crm1) and Calreticulin. Crm1 recognizes certain leucine-rich amino acid sequences in the proteins it exports called classical nuclear export signals. This paper describes a model system to study, identify, and establish these classical nuclear export signals using green fluorescent protein (GFP). Two putative export signals in the human progesterone receptor (PR) and the strongest nuclear export signal known (from mitogen activated protein kinase kinase [MAPKK]) were studied using this model system.
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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.