ARAP3
Author:
Publisher
Springer International Publishing
Link
http://link.springer.com/content/pdf/10.1007/978-3-319-67199-4_611
Reference30 articles.
1. Bao H, Li F, Wang C, Wang N, Jiang Y, Tang Y, et al. Structural basis for the specific recognition of RhoA by the dual GTPase-activating protein ARAP3. J Biol Chem. 2016;291:16709–19. https://doi.org/10.1074/jbc.M116.736140.
2. Boato F, Hendrix S, Huelsenbeck SC, Hofmann F, Grosse G, Djalali S, et al. C3 peptide enhances recovery from spinal cord injury by improved regenerative growth of descending fiber tracts. J Cell Sci. 2010;123:1652–62. https://doi.org/10.1242/jcs.066050.
3. Bos JL, Rehmann H, Wittinghofer A. GEFs and GAPs: critical elements in the control of small G proteins. Cell. 2007;129:865–77. https://doi.org/10.1016/j.cell.2007.05.018.
4. Craig HE, Coadwell J, Guillou H, Vermeren S. ARAP3 binding to phosphatidylinositol-(3,4,5)-trisphosphate depends on N-terminal tandem PH domains and adjacent sequences. Cell Signal. 2010;22:257–64. https://doi.org/10.1016/j.cellsig.2009.09.025.
5. Gambardella L, Anderson KE, Jakus Z, Kovács M, Voigt S, Hawkins PT, et al. Phosphoinositide 3-OH kinase regulates integrin-dependent processes in neutrophils by signaling through its effector ARAP3. J Immunol. 2013;190:381–91. https://doi.org/10.4049/jimmunol.1201330. (Baltimore, Md : 1950)
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