Structure of human guanylate-binding protein 1 representing a unique class of GTP-binding proteins
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Publisher
Springer Science and Business Media LLC
Subject
Multidisciplinary
Link
http://www.nature.com/articles/35000617.pdf
Reference30 articles.
1. Cheng, Y.-S. E., Colonno, R. J. & Yin, F. H. Interferon induction of fibroblast proteins with guanylate binding activity J. Biol. Chem. 258, 7746–7750 (1983).
2. Cheng, Y.-S. E., Patterson, C. E. & Staeheli, P. Interferon-induced guanylate-binding proteins lack an N(T)KXD consensus motif and bind GMP in addition to GDP and GTP Mol. Cell. Biol. 11, 4717–4725 (1991).
3. Schwemmle, M. & Staeheli, P. The interferon-induced 67-kDa guanylate-binding protein (hGBP1) is a GTPase that converts GTP to GMP J. Biol. Chem. 269, 11299–11305 (1994).
4. Anderson, S. L., Carton, J. M., Lou, J., Xing, L. & Rubin, B. Y. Interferon-induced guanylate-binding protein-1 (GBP-1) mediates an antiviral effect against vesicular stomatitis virus and encephalomyocarditis virus Virology 256, 8–14 (1999).
5. van der Bliek, A. M. Functional diversity in the dynamin family Trends Cell Biol. 9, 96–102 (1999).
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