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Activation of the Ras superfamily of small GTPases

✍ Scribed by Zheng, Yi; Quilliam, Lawrence A.


Book ID
110033610
Publisher
Nature Publishing Group
Year
2003
Tongue
English
Weight
169 KB
Volume
4
Category
Article
ISSN
1469-221X

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πŸ“œ SIMILAR VOLUMES


Stimulation of ras GTPase activity by an
✍ Sherry Agellon; James C. Stone πŸ“‚ Article πŸ“… 1996 πŸ› John Wiley and Sons 🌐 English βš– 766 KB

Wild-type ras has GTPase activity, and this activity is accelerated substantially by GTPase-activating proteins (GAPs). Oncogenic ras species have an abnormally low intrinsic GTPase activity, and this activity is insensitive to GAPs. We confirmed that the anti-ras monoclonal antibody Y13-238 inhibit

Ras interaction with the GTPase-activati
✍ Michael D. Schaber; Victor M. Garsky; Douglas Boylan; Wendy S. Hill; Edward M. S πŸ“‚ Article πŸ“… 1989 πŸ› John Wiley and Sons 🌐 English βš– 946 KB

Biologically active forms of Ras complexed to GTP can bind to the GTPase-activating protein (GAP), which has been implicated as possible target of Ras in mammalian cells. In order to study the structural features of Ras required for this interaction, we have evaluated a series of mutant ras proteins

Guanine nucleotide exchange factors: Act
✍ Ashley F. Overbeck; Teresa R. Brtva; Adrienne D. Cox; Suzanne M. Graham; Shayne πŸ“‚ Article πŸ“… 1995 πŸ› John Wiley and Sons 🌐 English βš– 973 KB

## Abstract Members of the Ras superfamily of proteins function as regulated GDP/GTP switches that cycle between active GTP‐complexed and inactive GDP‐complexed states. Guanine nucleotide exchange factors (GEFs) stimulate formation of the GTP‐bound state, whereas GTPase activating proteins (GAPs) c