ABCB1 p.Phe1086Arg
[switch to full view]Comments [show]
None has been submitted yet.
PMID: 23733192
[PubMed]
Loo TW et al: "Human P-glycoprotein contains a greasy ball-and-socket joint at the second transmission interface."
No.
Sentence
Comment
175
Fig. 5A shows that the F1086D or F1086R mutations inhibited maturation of P-gp.
X
ABCB1 p.Phe1086Arg 23733192:175:33
status: NEW177 Mutants F1086D and F1086R could still be rescued if they were expressed in the presence of a drug substrate (Fig. 5B).
X
ABCB1 p.Phe1086Arg 23733192:177:19
status: NEW179 Mutants F1086D and F1086R were first expressed in the presence of cyclosporine A to promote maturation before isolating the histidine-tagged protein.
X
ABCB1 p.Phe1086Arg 23733192:179:19
status: NEW212 A, F1086X mutants were expressed in the absence of drug substrates. B, processing mutants F1086D and F1086R were expressed in the presence (af9;) or absence (afa;) of cyclosporine A (Cyclo), and whole cell SDS extracts were subjected to immunoblot analysis.
X
ABCB1 p.Phe1086Arg 23733192:212:101
status: NEW214 Histidine-tagged mutants F1086D and F1086R were first expressed in the presence of cyclosporine A to promote maturation of P-gp before isolation of the protein by nickel-chelate chromatography. Each value is the mean afe; S.D. (n afd; 3).
X
ABCB1 p.Phe1086Arg 23733192:214:36
status: NEW
PMID: 25987565
[PubMed]
Loo TW et al: "The Transmission Interfaces Contribute Asymmetrically to the Assembly and Activity of Human P-glycoprotein."
No.
Sentence
Comment
15
Mutation of Phe-1086 or Tyr-1087 to arginine at the NBD2 socket blocked activity or assembly while the equivalent mutations at the NBD1 socket had only modest effects.
X
ABCB1 p.Phe1086Arg 25987565:15:12
status: NEW178 Mutants F1086A, F1086L, and F1086W yielded mature 170 kDa protein as the major product, whereas F1086R yielded little mature P-gp (b0d;5%) (Fig. 4A).
X
ABCB1 p.Phe1086Arg 25987565:178:96
status: NEW185 While the F1086A and F1086R mutations FIGURE 3.
X
ABCB1 p.Phe1086Arg 25987565:185:21
status: NEW276 The F1086R or Y1087R mutations at the NBD2 socket blocked maturation and activity while P-gp showed substantial activity when the comparable mutations (L443R, Y444R) were made to the NBD1 socket.
X
ABCB1 p.Phe1086Arg 25987565:276:4
status: NEW