GTPase activity of dynamin and resulting conformation change are essential for endocytosis
Author:
Publisher
Springer Science and Business Media LLC
Subject
Multidisciplinary
Link
http://www.nature.com/articles/35065645.pdf
Reference29 articles.
1. Urrutia, R., Henley, J. R., Cook, T. & McNiven, M. A. The dynamins: redundant or distinct functions for an expanding family of related GTPases? Proc. Natl Acad. Sci. USA 94, 377–384 (1997).
2. van der Bliek, A. M. Functional diversity in the dynamin family. Trends Cell Biol. 9, 96–102 (1999).
3. Warnock, D. E., HInshaw, J. E. & Schmid, S. L. Dynamin self-assembly stimulates its GTPase activity. J. Biol. Chem. 271, 22310–22314 (1996).
4. Roos, J. & Kelly, R. B. Is dynamin really a ‘pinchase’? Trends Cell Biol. 7, 257–259 (1997).
5. Sever, S., Muhlberg, A. B. & Schmid, S. L. Impairment of dynamin's GAP domain stimulates receptor-mediated endocytosis. Nature 398, 481–486 (1999).
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