ABCB1 p.Phe728Ala
[switch to full view]Comments [show]
None has been submitted yet.
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.
X
ABCB1 p.Phe728Ala 23104431:10:139
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.
X
ABCB1 p.Phe728Ala 23104431:45:111
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.
X
ABCB1 p.Phe728Ala 23104431:62:76
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).
X
ABCB1 p.Phe728Ala 23104431:122:130
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%.
X
ABCB1 p.Phe728Ala 23104431:132:174
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).
X
ABCB1 p.Phe728Ala 23104431:180:119
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).
X
ABCB1 p.Phe728Ala 23104431:190:42
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).
X
ABCB1 p.Phe728Ala 25264938:56:57
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.
X
ABCB1 p.Phe728Ala 25264938:154:71
status: NEW167 NMQ transport activity of P-gp mutants I306A, F343A and F728A was less than 40% of wild type.
X
ABCB1 p.Phe728Ala 25264938:167:56
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).
X
ABCB1 p.Phe728Ala 25264938:170:99
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.
X
ABCB1 p.Phe728Ala 25264938:253:35
status: NEW255 Convallatoxin transport activity of most mutants (I306A, F336A, I340A, F728A, F942A, T945, and L975) was similar to that of NMQ.
X
ABCB1 p.Phe728Ala 25264938:255:71
status: NEW