ABCC1 p.Glu1089Ala

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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
8 Conversion of Glu-1089 to Asn, Ala, or Leu had a similar effect on resistance to anthracyclines, while conversion to a positive amino acid, Lys, completely eliminated resistance to anthracyclines and vincristine without affecting transport of LTC4, E217betaG, and the GSH-dependent substrate, estrone-3-sulfate.
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ABCC1 p.Glu1089Ala 11278596:8:14
status: NEW
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113 In addition, mutation of glutamate 1089 to glutamine, alanine, and leucine decreased the relative resistance to vincristine by 55-65%, while mutation to lysine essentially eliminated resistance to this drug.
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ABCC1 p.Glu1089Ala 11278596:113:25
status: NEW
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PMID: 17295059 [PubMed] Chang XB et al: "A molecular understanding of ATP-dependent solute transport by multidrug resistance-associated protein MRP1."
No. Sentence Comment
114 E1089Q, E1089A, E1089L or E1089N mutations in TM14 markedly decreased resistance to anthracyclines without affecting LTC4 and E217βG transport [81].
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ABCC1 p.Glu1089Ala 17295059:114:8
status: NEW
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PMID: 19949927 [PubMed] Chang XB et al: "Molecular mechanism of ATP-dependent solute transport by multidrug resistance-associated protein 1."
No. Sentence Comment
104 Mutations of C43S in TM1 (112); P343A, K332L and K332D in TM6 (113, 114); W445A and P448A in TM8 (113, 115); T550A, T556A and P557A in TM10 (113, 116); N590A, F594A, P595A, N597A, S604A and S605A in TM11 (113, 117, 118); E1089Q, E1089A, E1089L, E1089N, K1092, S1097 and N1100 in TM14 (119, 120); R1197K in TM16 (121); Y1236F, T1241A, T1242A, T1242C, T1242S, T1242L, Y1243F, N1245A, W1246C, W1246A, W1246F, W1246Y or R1249K in TM17 (121-124) significantly affect MRP1 function.
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ABCC1 p.Glu1089Ala 19949927:104:229
status: NEW
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