ABCB4 p.Glu1125Gln
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PMID: 11087362
[PubMed]
Urbatsch IL et al: "Mutational analysis of conserved carboxylate residues in the nucleotide binding sites of P-glycoprotein."
No.
Sentence
Comment
69
Mutagenic oligos for the D1093N, E1125Q, D1203, and E1249Q mutations were 5'-CTTTGCCATTTA- GAAACAC-3', 5'-GGCAATGTTCTGCGCAATGCTGCAG- TC-3', 5'-TCAGCTCTGAATACAGAAAG-3', and 5'-AAG- GTCAAGCAGCACGGC-3', respectively.
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ABCB4 p.Glu1125Gln 11087362:69:33
status: NEW137 Single-point mutations D450N, E482Q, E552Q, D558N, D592N, and E604Q were introduced into the NB1 of Mdr3, and mutations D1093N, E1125Q, E1197Q, D1203N, D1237N, and E1249Q were introduced independently into the NB2.
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ABCB4 p.Glu1125Gln 11087362:137:128
status: NEW153 Cells expressing WT Mdr3 or the NB1 mutants D450N, E482Q, D592N, and E604Q (Figure 3A) or their NB2 counterparts D1093N, E1125Q, D1237N, and E1249Q (Figure 3B) were all resistant to FK506.
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ABCB4 p.Glu1125Gln 11087362:153:121
status: NEW169 Mating frequencies of mutants D450N (104%), E482Q (127%), D592N (22%), and E604Q (85%) in NB1 (Figure 4) or their counterparts D1093N (72%), E1125Q (101%), D1237N (68%), and E1249Q (118%) in NB2 (Figure 4) were similar to that of the Mdr3 WT control.
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ABCB4 p.Glu1125Gln 11087362:169:141
status: NEW259 Single-point mutations D450N, E482Q, D592N, and E604Q were introduced in NB1 and their homologous substitutions D1093N, E1125Q, D1237N, and E1249Q created in NB2, and the mutants were transformed in the yeast S. cereVisiae to assess their biological activity.
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ABCB4 p.Glu1125Gln 11087362:259:120
status: NEW