ABCC1 p.Glu1089Lys
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PMID: 11278596
[PubMed]
Zhang DW et al: "Identification of an amino acid residue in multidrug resistance protein 1 critical for conferring resistance to anthracyclines."
No.
Sentence
Comment
116
Typical survival curves for transfectants expressing wild type MRP1 and the mutant proteins E1089Q, E1089D, and E1089K are shown in Fig. 4.
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ABCC1 p.Glu1089Lys 11278596:116:112
status: NEW146 In view of the effect of mutations of glutamate 1089 in the human protein on resistance to vincristine and VP-16 in addition to the anthracyclines, we also examined LTC4 and E217betaG transport by wild type and mutant human MRP1, including MRP1, E1089Q, E1089D, and E1089K.
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ABCC1 p.Glu1089Lys 11278596:146:266
status: NEW147 However, none of these mutations had any detectable influence on transport including the E1089K mutation that significantly decreased resistance to all drugs tested (Fig. 6, B and D).
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ABCC1 p.Glu1089Lys 11278596:147:89
status: NEW172 However, mutation of glutamate 1089 to lysine completely eliminated resistance to both anthracyclines and vincristine (Table II).
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ABCC1 p.Glu1089Lys 11278596:172:21
status: NEW
PMID: 12867490
[PubMed]
Nunoya K et al: "Molecular cloning and pharmacological characterization of rat multidrug resistance protein 1 (mrp1)."
No.
Sentence
Comment
301
Previously, we showed that the hMRP1 TM 14 mutations E1089Q and E1089K, which either reduce or completely eliminate resistance to doxorubicin and vincristine, had no effect on estrone 3-sulfate transport (Zhang et al., 2001b).
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ABCC1 p.Glu1089Lys 12867490:301:64
status: NEW
PMID: 17295059
[PubMed]
Chang XB et al: "A molecular understanding of ATP-dependent solute transport by multidrug resistance-associated protein MRP1."
No.
Sentence
Comment
151
Mutation of E1089K completely eliminated resistance to anthracyclines and vincristine without affecting LTC4 and E217βG transport [81].
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ABCC1 p.Glu1089Lys 17295059:151:12
status: NEW