ABCG2 p.Arg482Asp
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PMID: 14566825
[PubMed]
Miwa M et al: "Single amino acid substitutions in the transmembrane domains of breast cancer resistance protein (BCRP) alter cross resistance patterns in transfectants."
No.
Sentence
Comment
48
Among PA/E446X1 transfectants, PA/E446D expressed a small amount of BCRP. Among PA/R482X2, PA/R482D and PA/R482K expressed lesser amounts of BCRP than the other transfectants.
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ABCG2 p.Arg482Asp 14566825:48:94
status: VERIFIED61 Most of the PA/ R482X2 cells (except for PA/R482D and PA/R482K) showed similar or somewhat lower levels of SN-38 resistance as compared to PA/WT2.
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ABCG2 p.Arg482Asp 14566825:61:44
status: VERIFIED64 PA/R482N, PA/R482C, PA/R482M, PA/R482S, PA/R482T, PA/R482V, PA/R482A, PA/R482G, PA/R482E PA/R482W and PA/R482D (Group 2) showed higher degrees of resistance to mitoxantrone than to SN-38.
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ABCG2 p.Arg482Asp 14566825:64:105
status: VERIFIED65 The drug resistance of PA/R482D was weak because of the low expression level of BCRP protein.
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ABCG2 p.Arg482Asp 14566825:65:26
status: VERIFIED163 Group 2 members (PA/R482N, PA/R482C, PA/R482M, PA/R482S, PA/R482T, PA/R482V, PA/ R482A, PA/R482G, PA/R482E PA/R482W and PA/R482D) showed higher degrees of resistance to mitoxantrone than to SN-38.
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ABCG2 p.Arg482Asp 14566825:163:123
status: VERIFIED
PMID: 15670731
[PubMed]
Ozvegy-Laczka C et al: "Single amino acid (482) variants of the ABCG2 multidrug transporter: major differences in transport capacity and substrate recognition."
No.
Sentence
Comment
48
The two internal complementary primer pairs containing the specific mutation were: 5V-tta tta cca atg atc atg tta cc-3Vand 5-Vgg taa cat gat cat tgg taa taa-3V (R482I), 5V-tta tca gat cta tta ccc atg-3Vand 5V-gg taa cat cat cat ggg taa t-3V(R482M), 5V-ta ccc atg tcg atg tta cca a-3Vand 5V-t tgg taa cat cga cat ggg ta-3V(R482S), 5V-cc atg gac atg tta cca tcg att ata-3V and 5V-tat aat cga tgg taa cat gtc cat gg-3V (R482D), 5V-atg tta cca tcg att ata ttt acc-3Vand 5V-cc atg aat atg tta cca tcg att ata-3V (R482N), 5V-tta tta cct atg aag atg tta-3V cc and 5V-gg taa cat ctt cat agg taa taa-3V(R482K) and 5V-tta tta cct atg tac atg tta cc-3Vand 5V-gg taa cat gta cat agg taa taa-3V (R482Y).
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ABCG2 p.Arg482Asp 15670731:48:417
status: VERIFIED82 The expression levels of the R482I and the R482D variants were usually somewhat lower than those for the other mutants.
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ABCG2 p.Arg482Asp 15670731:82:43
status: VERIFIED
PMID: 24384916
[PubMed]
Telbisz A et al: "Regulation of the function of the human ABCG2 multidrug transporter by cholesterol and bile acids: effects of mutations in potential substrate and steroid binding sites."
No.
Sentence
Comment
92
To examine how the characteristics of amino acid 482 influence the cholesterol-sensing capability of ABCG2, we have analyzed seven additional R482 mutants (R482D, I, M, N, S, Y, and K).
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ABCG2 p.Arg482Asp 24384916:92:156
status: NEW95 In cholesterol-loaded membranes, the basal ATPase activity of most of these variants increased (see Supplemental Table 1), but the increase in membrane cholesterol levels did not change the relative substrate stimulation of the R482D, G, N, S, and T variants (Fig. 1A).
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ABCG2 p.Arg482Asp 24384916:95:228
status: NEW111 In contrast, we did not observe a significant effect of cholesterol on the Hst transport by the R482D, G, N, S, and T variants.
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ABCG2 p.Arg482Asp 24384916:111:96
status: NEW