Expression, purification, and characterization of multiple, multifunctional human glucocorticoid receptor proteins
Protein Expression and Purification, ISSN: 1046-5928, Vol: 62, Issue: 1, Page: 29-35
2008
- 6Citations
- 27Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
Metrics Details
- Citations6
- Citation Indexes6
- CrossRef6
- Captures27
- Readers27
- 27
Article Description
The glucocorticoid receptor (GR) is a nuclear receptor protein that plays a central role in glucose homeostasis, the stress response, control of the hypothalamic-pituitary-adrenal axis, and immuno-inflammatory processes via binding of the natural steroid, cortisol. GR is a well-validated drug target and continues to be an important target for new drug discovery efforts. Here, we describe a basic and simple method for Escherichia coli expression and purification of a variety of human GR proteins that contain all three of the functional domains of the protein: the activation function-1 domain, the DNA-binding domain, and the ligand-binding domain. We present characterization data to show that these purified, multifunctional GR proteins are active for ligand, coactivator, and DNA-binding. The work presented here should serve as a reference for future mechanistic, structural and drug discovery efforts that require purified, full or near full length, GR protein.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S1046592808001800; http://dx.doi.org/10.1016/j.pep.2008.07.008; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=52949141437&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/18694832; https://linkinghub.elsevier.com/retrieve/pii/S1046592808001800; https://dx.doi.org/10.1016/j.pep.2008.07.008
Elsevier BV
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