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- W1522954144 abstract "Several proteins associated with signal transduction in eukaryotes are carboxyl methylated at COOH-terminal S-farnesylcysteine residues. These include members of the Ras superfamily and gamma-subunits of heterotrimeric G-proteins. The enzymes that catalyze the carboxyl methylation reaction also methylate small molecules such as N-acetyl-S-trans, trans-farnesyl-L-cysteine (AFC). AFC inhibits carboxyl methylation of p21ras and related proteins both in vitro and in vivo. Saturating concentrations of AFC cause a greater than 80% inhibition of chemotactic responses of mouse peritoneal macrophages. Our results suggest that carboxyl methylation may play a role in the regulation of receptor-mediated signal transduction processes in eukaryotic cells." @default.
- W1522954144 created "2016-06-24" @default.
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- W1522954144 date "1991-11-01" @default.
- W1522954144 modified "2023-10-18" @default.
- W1522954144 title "Effects of farnesylcysteine analogs on protein carboxyl methylation and signal transduction." @default.
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- W1522954144 doi "https://doi.org/10.1016/s0021-9258(18)54669-x" @default.
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