Formylglycine Aldehyde Tag-Protein Engineering through a Novel Post-translational Modification

Frese M-A, Dierks T (2009)
CHEMBIOCHEM 10(3): 425-427.

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Oxidation of a specific cysteine residue to C(alpha)-formylglycine is a novel post-translational modification that is directed by a short recognition motif commonly found in pro- and eukaryotic sulfatases. As recently shown by C. Bertozzi and co-workers, this system can be employed in protein engineering to equip proteins with genetically encoded aldehyde tags for site-specific labeling, conjugation and immobilization.
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Frese M-A, Dierks T. Formylglycine Aldehyde Tag-Protein Engineering through a Novel Post-translational Modification. CHEMBIOCHEM. 2009;10(3):425-427.
Frese, M. - A., & Dierks, T. (2009). Formylglycine Aldehyde Tag-Protein Engineering through a Novel Post-translational Modification. CHEMBIOCHEM, 10(3), 425-427.
Frese, M. - A., and Dierks, T. (2009). Formylglycine Aldehyde Tag-Protein Engineering through a Novel Post-translational Modification. CHEMBIOCHEM 10, 425-427.
Frese, M.-A., & Dierks, T., 2009. Formylglycine Aldehyde Tag-Protein Engineering through a Novel Post-translational Modification. CHEMBIOCHEM, 10(3), p 425-427.
M.-A. Frese and T. Dierks, “Formylglycine Aldehyde Tag-Protein Engineering through a Novel Post-translational Modification”, CHEMBIOCHEM, vol. 10, 2009, pp. 425-427.
Frese, M.-A., Dierks, T.: Formylglycine Aldehyde Tag-Protein Engineering through a Novel Post-translational Modification. CHEMBIOCHEM. 10, 425-427 (2009).
Frese, Marc-Andre, and Dierks, Thomas. “Formylglycine Aldehyde Tag-Protein Engineering through a Novel Post-translational Modification”. CHEMBIOCHEM 10.3 (2009): 425-427.
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6 Citations in Europe PMC

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