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- W2085303977 abstract "Ras proteins play critical roles in regulating cell growth and differentiation, and mutated Ras genes are expressed in a variety of human cancers. Consequently, much interest has centered on the binding partners of Ras, including the Ras-binding domain (RBD) of Raf kinase. Here evidence is presented that domains homologous to the Raf RBD are present in tandem in RGS12, RGS14 and LOCO, and singly in molecules similar to mouse Tiam-1. In addition, RGS12, RGS14 and LOCO are shown to contain single LGN motifs that are guanine nucleotide exchange factors specific for the alpha-subunit of G proteins. These findings indicate cross-talk interactions between signalling pathways involving Ras and Rap and pathways involving Rho, Rac and G alpha GTPases." @default.
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- W2085303977 date "1999-10-01" @default.
- W2085303977 modified "2023-09-29" @default.
- W2085303977 title "Raf-like Ras/Rap-binding domains in RGS12- and still-life-like signalling proteins" @default.
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- W2085303977 doi "https://doi.org/10.1007/s001099900054" @default.
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