ABCB1 p.Gly54Val
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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.Gly54Val 8995353:64:169
status: NEW
PMID: 9287132
[PubMed]
Taguchi Y et al: "Amino acid substitutions in the first transmembrane domain (TM1) of P-glycoprotein that alter substrate specificity."
No.
Sentence
Comment
87
It was reported [21] that no Vbl- or Col-resistant colonies were obtained from cells transfected with either Gly54 -> Val, Ala58 -> Leu, or Gly62 -> Val mutant P-glycoprotein cDNA, and that the major products from these three mutant cDNAs were protein with an apparent mass of 150 kDa when their cDNAs were transiently expressed in HEK 293 cells, suggesting that these mutations in TMl affected the proper folding In this study, we examined whether the substitution of amino acids near His61 in TMl affect substrate specificity of P-glycoprotein.
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ABCB1 p.Gly54Val 9287132:87:109
status: NEW