ABCC1 p.Thr1241Ala
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PMID: 11925441
[PubMed]
Zhang DW et al: "Determinants of the substrate specificity of multidrug resistance protein 1: role of amino acid residues with hydrogen bonding potential in predicted transmembrane helix 17."
No.
Sentence
Comment
4
In contrast, mutations Y1236F and T1241A decreased resistance to vincristine but not to VP-16, doxorubicin, and epirubicin.
X
ABCC1 p.Thr1241Ala 11925441:4:34
status: NEW113 Mutation of one polar-aromatic residue, Y1243F, caused an approximately 2-3-fold reduction of resistance to all four drugs, whereas three mutations, Y1236F, T1241A, and N1245A, resulted in a 2-3-fold loss of resistance to only certain drugs.
X
ABCC1 p.Thr1241Ala 11925441:113:157
status: NEW114 Interestingly, both mutation Y1236F and mutation T1241A decreased vincristine resistance ϳ3-fold without a significant effect on the resistance to VP-16, doxorubicin, and epirubicin.
X
ABCC1 p.Thr1241Ala 11925441:114:49
status: NEW117 Subcellular Localization of Mutant and Wild Type MRP1 in Transfected HEK293 Cells-To determine whether effects of mutations Y1236F, T1241A, Y1243F, and N1245A on the drug FIG. 1.
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ABCC1 p.Thr1241Ala 11925441:117:132
status: NEW141 ATP-dependent transport of [3 H]E217betaG was also examined (Fig. 5), but none of the mutations S1233A, S1235A, Y1236F, S1237A, Q1239A, and T1241A had any effect.
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ABCC1 p.Thr1241Ala 11925441:141:140
status: NEW211 The similar effect of the mutation, T1241A, on the resistance to vincristine might be also due to the elimination of the hydrogen bonding capability.
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ABCC1 p.Thr1241Ala 11925441:211:36
status: NEW
PMID: 16442101
[PubMed]
Frelet A et al: "Insight in eukaryotic ABC transporter function by mutation analysis."
No.
Sentence
Comment
474
Other mutations either affected the transport of LTC4 and/or E217G (Y1243F) or reduced resistance to drugs (Y1236F, T1241A and Y1243F), suggesting that residues of the cytoplasmic half of TM17 with side chain hydrogen bonding potential participate in the formation of a substrate-binding site [218].
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ABCC1 p.Thr1241Ala 16442101:474:116
status: NEW
PMID: 17295059
[PubMed]
Chang XB et al: "A molecular understanding of ATP-dependent solute transport by multidrug resistance-associated protein MRP1."
No.
Sentence
Comment
117
Many mutations in TM17, such as Y1236F, T1241A, T1242A, T1242C, T1242S, T1242L, Y1243F, N1245A, W1246C, W1246A, W1246F, W1246Y, or R1249K, significantly affect MRP1 function [83-86].
X
ABCC1 p.Thr1241Ala 17295059:117:40
status: NEW
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.
X
ABCC1 p.Thr1241Ala 19949927:104:326
status: NEW