ABCB1 p.Glu707Ala
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PMID: 8995353
[PubMed]
Loo TW et al: "Correction of defective protein kinesis of human P-glycoprotein mutants by substrates and modulators."
No.
Sentence
Comment
64
In addition to the mutants G268V and ⌬Y490, we were able to facilitate processing of P-glycoproteins with mutations in the predicted transmembrane segments (TM1, G54V; TM5, G300V; TM7, A718L; and TM9, A841L), in the extracellular loops between transmembrane segments (G854V), in the cytoplasmic loops (G251V and W803A), in the nucleotide-binding domains (G427C and S434C), and in the linker region connecting the two halves of the molecule (E707A) (data not shown).
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ABCB1 p.Glu707Ala 8995353:64:448
status: NEW140 Another interesting observation is that misfolded mutants that are temperatureand glycerol-insensitive, such as G251V, G268V, and E707A could also be rescued by these drug substrates when expressed in either HEK 293 or NIH 3T3 cells (data not shown).
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ABCB1 p.Glu707Ala 8995353:140:130
status: NEW
PMID: 9614062
[PubMed]
Loo TW et al: "Superfolding of the partially unfolded core-glycosylated intermediate of human P-glycoprotein into the mature enzyme is promoted by substrate-induced transmembrane domain interactions."
No.
Sentence
Comment
48
Misprocessing mutations are located throughout the molecule; these include the transmembrane domains (e.g. A123L), intracellular (e.g. E243A) and extracellular (e.g. Y853C) loops, the linker region (e.g. E707A), and both nucleotide-binding domains (e.g. G427C, P1194A).
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ABCB1 p.Glu707Ala 9614062:48:204
status: NEW