↑Lowe DG, Capon DJ, Delwart E, Sakaguchi AY, Naylor SL, Goeddel DV (February 1987). "Structure of the human and murine R-ras genes, novel genes closely related to ras proto-oncogenes". Cell. 48 (1): 137–46. doi:10.1016/0092-8674(87)90364-3. PMID3098437.
↑Fernandez-Sarabia MJ, Bischoff JR (November 1993). "Bcl-2 associates with the ras-related protein R-ras p23". Nature. 366 (6452): 274–5. doi:10.1038/366274a0. PMID8232588.
↑Wang B, Zou JX, Ek-Rylander B, Ruoslahti E (February 2000). "R-Ras contains a proline-rich site that binds to SH3 domains and is required for integrin activation by R-Ras". J. Biol. Chem. 275 (7): 5222–7. doi:10.1074/jbc.275.7.5222. PMID10671570.
↑Ortiz-Vega S, Khokhlatchev A, Nedwidek M, Zhang XF, Dammann R, Pfeifer GP, Avruch J (February 2002). "The putative tumor suppressor RASSF1A homodimerizes and heterodimerizes with the Ras-GTP binding protein Nore1". Oncogene. 21 (9): 1381–90. doi:10.1038/sj.onc.1205192. PMID11857081.
Further reading
Carboni JM, Yan N, Cox AD, Bustelo X, Graham SM, Lynch MJ, Weinmann R, Seizinger BR, Der CJ, Barbacid M (1995). "Farnesyltransferase inhibitors are inhibitors of Ras but not R-Ras2/TC21, transformation". Oncogene. 10 (10): 1905–13. PMID7761092.
Fernandez-Sarabia MJ, Bischoff JR (1993). "Bcl-2 associates with the ras-related protein R-ras p23". Nature. 366 (6452): 274–5. doi:10.1038/366274a0. PMID8232588.
Linnemann T, Geyer M, Jaitner BK, Block C, Kalbitzer HR, Wittinghofer A, Herrmann C (1999). "Thermodynamic and kinetic characterization of the interaction between the Ras binding domain of AF6 and members of the Ras subfamily". J. Biol. Chem. 274 (19): 13556–62. doi:10.1074/jbc.274.19.13556. PMID10224125.
Choy E, Chiu VK, Silletti J, Feoktistov M, Morimoto T, Michaelson D, Ivanov IE, Philips MR (1999). "Endomembrane trafficking of ras: the CAAX motif targets proteins to the ER and Golgi". Cell. 98 (1): 69–80. doi:10.1016/S0092-8674(00)80607-8. PMID10412982.
Wang B, Zou JX, Ek-Rylander B, Ruoslahti E (2000). "R-Ras contains a proline-rich site that binds to SH3 domains and is required for integrin activation by R-Ras". J. Biol. Chem. 275 (7): 5222–7. doi:10.1074/jbc.275.7.5222. PMID10671570.
Suzuki J, Kaziro Y, Koide H (2000). "Positive regulation of skeletal myogenesis by R-Ras". Oncogene. 19 (9): 1138–46. doi:10.1038/sj.onc.1203402. PMID10713701.
Ohba Y, Mochizuki N, Yamashita S, Chan AM, Schrader JW, Hattori S, Nagashima K, Matsuda M (2000). "Regulatory proteins of R-Ras, TC21/R-Ras2, and M-Ras/R-Ras3". J. Biol. Chem. 275 (26): 20020–6. doi:10.1074/jbc.M000981200. PMID10777492.
Oertli B, Han J, Marte BM, Sethi T, Downward J, Ginsberg M, Hughes PE (2000). "The effector loop and prenylation site of R-Ras are involved in the regulation of integrin function". Oncogene. 19 (43): 4961–9. doi:10.1038/sj.onc.1203876. PMID11042683.
Tian X, Feig LA (2001). "Basis for signaling specificity difference between Sos and Ras-GRF guanine nucleotide exchange factors". J. Biol. Chem. 276 (50): 47248–56. doi:10.1074/jbc.M107407200. PMID11560935.
Ortiz-Vega S, Khokhlatchev A, Nedwidek M, Zhang XF, Dammann R, Pfeifer GP, Avruch J (2002). "The putative tumor suppressor RASSF1A homodimerizes and heterodimerizes with the Ras-GTP binding protein Nore1". Oncogene. 21 (9): 1381–90. doi:10.1038/sj.onc.1205192. PMID11857081.
Yu Y, Feig LA (2002). "Involvement of R-Ras and Ral GTPases in estrogen-independent proliferation of breast cancer cells". Oncogene. 21 (49): 7557–68. doi:10.1038/sj.onc.1205961. PMID12386818.
Rincón-Arano H, Rosales R, Mora N, Rodriguez-Castañeda A, Rosales C (2003). "R-Ras promotes tumor growth of cervical epithelial cells". Cancer. 97 (3): 575–85. doi:10.1002/cncr.11093. PMID12548599.
Furuhjelm J, Peränen J (2003). "The C-terminal end of R-Ras contains a focal adhesion targeting signal". J. Cell Sci. 116 (Pt 18): 3729–38. doi:10.1242/jcs.00689. PMID12890755.
Mitin NY, Ramocki MB, Zullo AJ, Der CJ, Konieczny SF, Taparowsky EJ (2004). "Identification and characterization of rain, a novel Ras-interacting protein with a unique subcellular localization". J. Biol. Chem. 279 (21): 22353–61. doi:10.1074/jbc.M312867200. PMID15031288.