Site-specific N-terminal labelling of proteins in vitro and in vivo using N-myristoyl transferase and bioorthogonal ligation chemistry

Chemical Communications : Chem Comm
William P HealEdward W Tate

Abstract

N-Myristoyl transferase-mediated modification with azide-bearing substrates is introduced as a highly selective and practical method for in vitro and in vivo N-terminal labelling of a recombinant protein using bioorthogonal ligation chemistry.

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Citations

Jul 2, 2009·Journal of Chemical Biology·Edward W Tate
Nov 10, 2009·Journal of Chemical Biology·Megan H WrightEdward W Tate
Sep 17, 2011·Chemical Reviews·Howard C Hang, Maurine E Linder
Mar 17, 2010·Journal of the American Chemical Society·Kavita J RanganHoward C Hang
Jan 13, 2009·Nature Methods·Brent R Martin, Benjamin F Cravatt
Jan 12, 2011·Chemical Communications : Chem Comm·William P HealEdward W Tate
Jul 18, 2012·Chemical Communications : Chem Comm·Pamela V Chang, Carolyn R Bertozzi
Jul 26, 2012·Journal of Lipid Research·Francesca RampoldiStefan Porubsky
Jun 20, 2008·Organic & Biomolecular Chemistry·William P HealEdward W Tate
Aug 14, 2009·Organic & Biomolecular Chemistry·Murat Sunbul, Jun Yin
May 8, 2010·Organic & Biomolecular Chemistry·Karunakaran A KaleshShao Q Yao
Jun 21, 2011·Chemical Society Reviews·Christine I SchillingStefan Bräse
Nov 9, 2010·Biochimie·Dale D O MartinLuc G Berthiaume
Aug 25, 2009·Current Opinion in Chemical Biology·Guillaume CharronHoward C Hang
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