ABCB1 p.Tyr444*
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PMID: 25987565
[PubMed]
Loo TW et al: "The Transmission Interfaces Contribute Asymmetrically to the Assembly and Activity of Human P-glycoprotein."
No.
Sentence
Comment
195
A52-tagged mutants Y444X were constructed so that tyrosine was replaced with a small (Ala), hydrophobic (Phe, Leu) or charged(Arg,Glu)residue.Forcomparison,thepreviouslycon- structed Y1087A, Y1087F, and Y1087L mutants were included (38) and additional mutants Y1087R and Y1087E were also constructed.
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ABCB1 p.Tyr444* 25987565:195:19
status: NEW199 All the Y444X mutants except Y444E differed from their Tyr-1087 counterparts as they yielded detectable levels of mature 170 kDa P-gp.
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ABCB1 p.Tyr444* 25987565:199:8
status: NEW205 The activity of Y1087 was almost completely inhibited when it was mutated to A, L, R, or E. In contrast, the Y444X mutations had less severe effects.
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ABCB1 p.Tyr444* 25987565:205:109
status: NEW