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Characterization of prenylcysteines that interact with P-glycoprotein and inhibit drug transport in tumor cells.
Zhang L, Sachs CW, Fu HW, Fine RL, Casey PJ. Zhang L, et al. J Biol Chem. 1995 Sep 29;270(39):22859-65. doi: 10.1074/jbc.270.39.22859. J Biol Chem. 1995. PMID: 7559420 Free article.
Prenylcysteine methyl esters that represent the C-terminal structures of prenylated proteins demonstrate specific substrate-like interactions with P-glycoprotein (Zhang, L., Sachs, C. W., Fine, R. L., and Casey, P. J. (1994) J. Biol. Chem. 269, 15973-15976). …
Prenylcysteine methyl esters that represent the C-terminal structures of prenylated proteins demonstrate specific substrate-like interaction …
Mutations in the hydrophobic surface of an amphipathic groove of 14-3-3zeta disrupt its interaction with Raf-1 kinase.
Wang H, Zhang L, Liddington R, Fu H. Wang H, et al. Among authors: zhang l. J Biol Chem. 1998 Jun 26;273(26):16297-304. doi: 10.1074/jbc.273.26.16297. J Biol Chem. 1998. PMID: 9632690 Free article.
Consistently, mutations on the charged surface of the groove (Lys-49, Arg-56, and Arg-60) decrease the binding of 14-3-3zeta to the ligands tested (Zhang, L., Wang, H., Liu, D., Liddington, R., and Fu, H. (1997) J. Biol. Chem. 272, 13717-13724). ...
Consistently, mutations on the charged surface of the groove (Lys-49, Arg-56, and Arg-60) decrease the binding of 14-3-3zeta to the ligands …
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