ArticleNature protocols2012
Overexpressing human membrane proteins in stably transfected and clonal human embryonic kidney 293S cells.
Article in Nature protocols, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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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
50 citing papers in PubMed, 76 citations in OpenAlex.
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- Protein production from HEK293 cell line-derived stable pools with high protein quality and quantity to support discovery research.PloS one · 2023Article
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- Structural and mechanistic basis of the EMC-dependent biogenesis of distinct transmembrane clients.eLife · 2020Article
- Thermostability of a recombinant G protein-coupled receptor expressed at high level in mammalian cell culture.Scientific reports · 2020Article
- Identification of targets of AMPylating Fic enzymes by co-substrate-mediated covalent capture.Nature chemistry · 2020Article
- Production of Recombinant Transmembrane Proteins from Mammalian Cells for Biochemical and Structural Analyses.Current protocols in cell biology · 2020Article
- Cryo-EM structure of the Hedgehog release protein Dispatched.Science advances · 2020Article
- Design, Expression, Purification, and Characterization of a YFP-Tagged 2019-nCoV Spike Receptor-Binding Domain Construct.Frontiers in bioengineering and biotechnology · 2020Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
X-ray crystal structures of human membrane proteins, although potentially of extremely great impact, are highly underrepresented relative to those of prokaryotic membrane proteins. One key reason for this is that human membrane proteins can be difficult to express at a level, and at a quality, suitable for structural studies. This protocol describes the methods that we use to overexpress human membrane proteins from clonal human embryonic kidney 293 (HEK293S) cells lacking N-acetylglucosaminyltransferase I (GnTI(-)), and was recently used in our 2.1-Å X-ray crystal structure determination of human RhCG. Upon identification of highly expressing cell lines, suspension cell cultures are scaled up in a facile manner either using spinner flasks or cellbag bioreactors, resulting in a final purified yield of ∼0.5 mg of membrane protein per liter of medium. The protocol described here is reliable and cost effective, can be used to express proteins that would otherwise be toxic to mammalian cells and can be completed in 8-10 weeks.
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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.