ABCB1 p.Ile306Ala
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PMID: 17848563
[PubMed]
Loo TW et al: "Suppressor mutations in the transmembrane segments of P-glycoprotein promote maturation of processing mutants and disrupt a subset of drug-binding sites."
No.
Sentence
Comment
99
Some changes in TM5 (I306A or G) or in TM6 (F343Y) in the ⌬Y490 P-gp mutant also caused the mutant protein to be unstable because cells expressing these mutants contained relatively large amounts of a 130-kDa degradation product (21).
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ABCB1 p.Ile306Ala 17848563:99:21
status: NEW
PMID: 23104431
[PubMed]
Gozalpour E et al: "Interaction of digitalis-like compounds with p-glycoprotein."
No.
Sentence
Comment
10
The uptake of [3 H]-N-methyl-quinidine (NMQ), the P-gp substrate in vesicular transport assays, was determined.The mutations I306A, F343A, F728A,T945A, and L975A abolished NMQ transport activity of P-gp.
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ABCB1 p.Ile306Ala 23104431:10:125
status: NEW45 Removal of the side chain resulted in loss of NMQ transport activity of five human P-gp mutants: I306A, F343A, F728A, T945A, and L975A, which seem to have key role in the transport of NMQ.
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ABCB1 p.Ile306Ala 23104431:45:97
status: NEW46 However, transport activity was preserved in L65A, I306A, I340A, F942A, and V982A.
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ABCB1 p.Ile306Ala 23104431:46:51
status: NEW62 Ten different P-gp mutants were produced: L65A, I306A, F336A, I340A, F343A, F728A, F942A, T945A, L975A, and V982A and all mutations were confirmed by sequencing of full-length P-gp cDNA.
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ABCB1 p.Ile306Ala 23104431:62:48
status: NEW122 All the indicated amino acids were replaced by alanine to remove the side chain of the residue (L65A, I306A, F336A, I340A, F343A, F728A, F942A, T945A, L975A, and V982A).
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ABCB1 p.Ile306Ala 23104431:122:102
status: NEW132 NMQ transport activity of mutants L65A, F336A, I340A, F942A, andV982A as compared with wild-type P-gp ranged from 60 to 150%, whereas NMQ transport activity of I306A, F343A, F728A, T945A, and L975A varied between 8 and 30%.
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ABCB1 p.Ile306Ala 23104431:132:160
status: NEW180 Fig. 5.ߓ Western blot analysis (A) and NMQ transport activity of wild type and L65A, I306A, F336A, I340A, F343A, F728A, F942A, T945A, L975A, and V982A mutant P-gp (B).
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ABCB1 p.Ile306Ala 23104431:180:91
status: NEW190 The first group of mutants (I306A, F343A, F728A, T945A, and L975A) exhibited a significantly lower NMQ transport activity (8-30% of wild-type P-gp).
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ABCB1 p.Ile306Ala 23104431:190:28
status: NEW
No.
Sentence
Comment
56
Nine different P-gp mutants, I306A, F336A, I340A, F343A, F728A, F942A, T945A, L975A, and V982A, were produced and sequencing of full-length P-gp cDNA was used to confirm all mutations (Gozalpour et al., 2013).
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ABCB1 p.Ile306Ala 25264938:56:29
status: NEW154 Nine amino acids were replaced by alanine (I306A, F336A, I340A, F343A, F728A, F942A, T945A, L975A, and V982A) and P-gp mutants were expressed in HEK293 cells to produce membrane vesicles.
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ABCB1 p.Ile306Ala 25264938:154:43
status: NEW167 NMQ transport activity of P-gp mutants I306A, F343A and F728A was less than 40% of wild type.
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ABCB1 p.Ile306Ala 25264938:167:39
status: NEW170 Convallatoxin and NMQ transport activity were not significantly different for I306A, F336A, I340A, F728A, F942A, T945A, and L975A (Fig. 5C), whereas they differed significantly for F343A and V982A (Fig. 5D and E).
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ABCB1 p.Ile306Ala 25264938:170:78
status: NEW253 The P-gp mutants, I306A, F343A and F728A exhibited a NMQ transport activity that was less than 30% of the wild type activity.
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ABCB1 p.Ile306Ala 25264938:253:18
status: NEW255 Convallatoxin transport activity of most mutants (I306A, F336A, I340A, F728A, F942A, T945, and L975) was similar to that of NMQ.
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ABCB1 p.Ile306Ala 25264938:255:50
status: NEW