Abstract
The ras-genes are conserved during evolution and appear to play an essential role in the growth regulation of cells. Products of these genes are localized in the plasma membrane1,2 and exhibit well-defined biochemical activities to bind guanine nucleotides and hydrolyze GTP3–6. Because a large amount of the purified proteins can be obtained after their expression in E. coli, extensive structural studies have been carried out. The protein has been crystalized and its three dimensional structure has been determined7. Furthermore, recent identification of the GAP protein8–10 raises the possibility that protein-protein interactions involving the ras protein can be elucidated in biochemical terms.
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Tamanoi, F., Cobitz, A.R., Fujiyama, A., Goodman, L.E., Perou, C. (1989). Post-Translational Modification of ras Proteins: Palmitoylation and Phosphorylation of Yeast ras Proteins. In: Spandidos, D. (eds) ras Oncogenes. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-1235-3_29
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DOI: https://doi.org/10.1007/978-1-4757-1235-3_29
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