Proteolytic elimination of N-myristoyl modifications by the Shigella virulence factor IpaJ-Reference-Cited by-同舟云学术

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Proteolytic elimination of N-myristoyl modifications by the Shigella virulence factor IpaJ

Published:2013-03-27 Issue:7443 Volume:496 Page:106-109
ISSN:0028-0836
Container-title:Nature
language:en
Short-container-title:Nature

Author:

Burnaevskiy Nikolay,Fox Thomas G.,Plymire Daniel A.,Ertelt James M.,Weigele Bethany A.,Selyunin Andrey S.,Way Sing Sing,Patrie Steven M.,Alto Neal M.

Publisher

Springer Science and Business Media LLC

Subject

Multidisciplinary

Link

http://www.nature.com/articles/nature12004.pdf

Reference36 articles.

1. Farazi, T. A., Waksman, G. & Gordon, J. I. The biology and enzymology of protein N-myristoylation. J. Biol. Chem. 276, 39501–39504 (2001)

2. Maurer-Stroh, S. et al. MYRbase: analysis of genome-wide glycine myristoylation enlarges the functional spectrum of eukaryotic myristoylated proteins. Genome Biol. 5, R21 (2004)

3. McLaughlin, S. & Aderem, A. The myristoyl-electrostatic switch: a modulator of reversible protein-membrane interactions. Trends Biochem. Sci. 20, 272–276 (1995)

4. Kahn, R. A. Toward a model for Arf GTPases as regulators of traffic at the Golgi. FEBS Lett. 583, 3872–3879 (2009)

5. Dong, N. et al. Structurally distinct bacterial TBC-like GAPs link Arf GTPase to Rab1 inactivation to counteract host defenses. Cell 150, 1029–1041 (2012)

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