ArticleProceedings of the National Academy of Sciences of the United States of America2017
Efficient, ultra-high-affinity chromatography in a one-step purification of complex proteins.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 72 citations in OpenAlex.
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- Application of a Novel CL7/Im7 Affinity System in Purification of Complex and Pharmaceutical Proteins.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Cost-Effective Production of ATP and S-Adenosylmethionine Using Engineered Multidomain Scaffold Proteins.Biomolecules · 2021Article
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- A Method for Rapid Screening, Expression, and Purification of Antimicrobial Peptides.Microorganisms · 2021Article
- The SESAME complex regulates cell senescence through the generation of acetyl-CoA.Nature metabolism · 2021Article
- High-yield production in E. coli and characterization of full-length functional p13Protein expression and purification · 2020Article
Corrections and comments
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Authors and funding
10 authors at 1 institution in 1 country.
Funding
Abstract
Protein purification is an essential primary step in numerous biological studies. It is particularly significant for the rapidly emerging high-throughput fields, such as proteomics, interactomics, and drug discovery. Moreover, purifications for structural and industrial applications should meet the requirement of high yield, high purity, and high activity (HHH). It is, therefore, highly desirable to have an efficient purification system with a potential to meet the HHH benchmark in a single step. Here, we report a chromatographic technology based on the ultra-high-affinity (
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