Since IPL allows the fusion of synthetic peptides, as well as bacterially expressed proteins, with an N-terminal cysteine, to a protein expressed in the IMPACT system, IPL has been used in a variety of ways including:
The expression of cytotoxic proteins (1).
The labeling of proteins with radioactive compounds as well as with synthetic peptides containing biotin or fluorescein (1-3).
The study of protein-protein interactions (4).
The generation of kinase substrates by varying the kinase recognition site at the protein level instead of at the DNA level (5, 6).
The generation of phosphatase substrates (7).
The isotopic labeling of proteins for NMR analysis (8).
Generation of substrates for protein arrays (9).
Site specifically incorporating lipid moieties into a protein (10).
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Chong, S. et al. (1997) Gene 192: 271-281. PMID: 9224900
Muir, T. et al. (1998) Proc. Natl. Acad. Sci. USA 95:6705-6710. PMID: 9618476
Severinov, K. et al. (1998) J. Biol. Chem. 273:16205-16209. PMID: 9632677
Ghosh, I. et al. (2004) J. of Imm. Methods. 293:85-95. PMID: 15541279
Xu, J., Sun, L., Ghosh, I., and Xu, M.-Q. (2004) Biotechniques. 36:976-998. PMID: 15211748
Kochinyan, S. et. al. (2007) Biotechniques 42(1): 63-9. PMID: 17269486
Xu, R. et al. (1999) Proc. Natl. Acad. Sci. USA 96, 388-393. PMID: 9892643
Sun, L., et al. (2004) Biotechniques. 37: 430-443. PMID: 15470898
Rak, A. et al. (2003) Science 302, 646-650. PMID: 14576435
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