ABCG2 p.Arg309Gly
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PMID: 11807788
[PubMed]
Kage K et al: "Dominant-negative inhibition of breast cancer resistance protein as drug efflux pump through the inhibition of S-S dependent homodimerization."
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151
to Ala and Tyr-605 to Cys), HABCRP-37 (Thr-82 to Ala) or HABCRP-74 (Ser-25 to Pro, Arg-309 to Gly and Ala-632 to Val), also expressed mutant BCRP protein, but cells transfected with HABCRP-86 (Lys-86 to Ile) did not express BCRP protein and therefore exhibited no drug resistance.
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ABCG2 p.Arg309Gly 11807788:151:83
status: VERIFIED
PMID: 17027309
[PubMed]
Li YF et al: "Towards understanding the mechanism of action of the multidrug resistance-linked half-ABC transporter ABCG2: a molecular modeling study."
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174
Subsequently, a symmetric dimer Y.-F Li et al. / Journal of Molecular Graphics and Modelling 25 (2007) 837-851844 Table 4 Locations of mutations as predicted by the ABCG2 model and functional correlation Mutation Position in ABCG2 Phenotype Reference V12M N-terminal Membrane localization, SNP, and somewhat lower expression and lower resistance [22] S25Pa N-terminal Low drug resistance for the cell line due to lower expression at cell surface [42] T82Aa NBD, Walker A Low drug resistance for the cell line due to lower expression at cell surface [42] K86M NBD, Walker A No expression at cell surface, retained in the Golgi [43] K86I NBD, Walker A No expressed at cell surface [43] Q141K NBD SNP with lower protein expression and low drug resistance [22,23] T237V NBD Fully functional b I239K,R NBD Loss of expression may be due to structural disruption b R309G Linkerc Low drug resistance [42] D315-6 Linker Deletion mutant for A315 and T316.
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ABCG2 p.Arg309Gly 17027309:174:858
status: VERIFIED