ABCC1 p.Glu1089Asp
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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
7
The mutation E1089D showed the same phenotype as MRP1, while the E1089Q substitution markedly decreased resistance to anthracyclines without affecting LTC4 and E217betaG transport.
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ABCC1 p.Glu1089Asp 11278596:7:13
status: NEW110 Thus, glutamate 1089 was mutated to aspartate, glutamine, alanine, leucine, and lysine and chemosensitivity assays were carried out.
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ABCC1 p.Glu1089Asp 11278596:110:6
status: NEW116 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.Glu1089Asp 11278596:116:100
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.Glu1089Asp 11278596:146:254
status: NEW231 This was supported by the results obtained by substitution of glutamate 1089 with aspartate, which resulted in no detectable change in resistance profile, and by conversion to lysine, which essentially eliminated resistance to both anthracyclines and vincristine, and substantially decreased resistance to VP-16.
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ABCC1 p.Glu1089Asp 11278596:231:62
status: NEW
PMID: 12706887
[PubMed]
Grailles M et al: "The Drosophila melanogaster multidrug-resistance protein 1 (MRP1) homolog has a novel gene structure containing two variable internal exons."
No.
Sentence
Comment
155
Site directed mutagenesis was used to change Glu 1089 to Gln, Asp, Ala, Leu or Lys.
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ABCC1 p.Glu1089Asp 12706887:155:45
status: NEW153 Site directed mutagenesis was used to change Glu 1089 to Gln, Asp, Ala, Leu or Lys.
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ABCC1 p.Glu1089Asp 12706887:153:45
status: NEW