ABCA1 p.Lys2031Arg
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PMID: 23221702
[PubMed]
Tomioka M et al: "The effects of neurological disorder-related codon variations of ABCA13 on the function of the ABC protein."
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66
Hence we established HEK293 cells that stably expressed ABCA1 containing ABCA13 SNPs, ABCA1-T1088A, ABCA1- K2031C, and ABCA1-K2031R (as control).
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ABCA1 p.Lys2031Arg 23221702:66:125
status: NEW70 However, the K2031C SNP did not significantly affect cholesterol efflux as compared to the wild type or K2031R (Fig. 2A).
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ABCA1 p.Lys2031Arg 23221702:70:104
status: NEW71 ApoA-I binding of HEK/ABCA1-SNP mutants at the plasma membrane We have reported that the first step in high-density lipoprotein (HDL) formation is apoA-I binding to the extracellular domains of ABCA1.13) Hence we examined to determine whether the loss in the cholesterol efflux ability of T1088A was due to a change in apoA-I binding.
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ABCA1 p.Lys2031Arg 23221702:71:104
status: NEW79 For K2031C and wild-type K2031R, most of the protein was resistant to EndoH, but 50% or more of ABCA1-T1088 was sensitive to EndoH (Fig. 4), suggesting that the T1088A mutation caused improper folding of the protein.
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ABCA1 p.Lys2031Arg 23221702:79:25
status: NEW67 Hence we established HEK293 cells that stably expressed ABCA1 containing ABCA13 SNPs, ABCA1-T1088A, ABCA1- K2031C, and ABCA1-K2031R (as control).
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ABCA1 p.Lys2031Arg 23221702:67:125
status: NEW80 For K2031C and wild-type K2031R, most of the protein was resistant to EndoH, but 50% or more of ABCA1-T1088 was sensitive to EndoH (Fig. 4), suggesting that the T1088A mutation caused improper folding of the protein.
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ABCA1 p.Lys2031Arg 23221702:80:25
status: NEW