The Mechanism of Ras GTPase Activation by Neurofibromin
Author:
Affiliation:
1. National Institute for Medical Research, Mill Hill, London NW7 1AA, United Kingdom
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi027316z
Reference50 articles.
1. Brunger, A. T., Milburn, M. V., Tong, L., de Vos, A. M., Jancarik, J., Yamaizumi, Z., Nishimura, S., Ohtsuka, E., and Kim, S. H. (1990) Crystal structure of an active form of RAS protein, a complex of a GTP analogue and the HRAS p21 catalytic domain,Proc. Natl. Acad. Sci. U.S.A.87, 4849−4853.
2. Pai, E. F., Kabsch, W., Krengel, U., Holmes, K. C., John, J., and Wittinghofer, A. (1989) Structure of the guanine-nucleotide-binding domain of the Ha-ras oncogene product p21 in the triphosphate conformation,Nature341, 209−214.
3. Trahey, M., and McCormick, F. (1987) A cytoplasmic protein stimulates normal N-ras p21 GTPase, but does not affect oncogenic mutants,Science238, 542−545.
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