ABCB1 p.Pro709Gly
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PMID: 16442101
[PubMed]
Frelet A et al: "Insight in eukaryotic ABC transporter function by mutation analysis."
No.
Sentence
Comment
519
Loo et al. [256] demonstrated that mutations affecting the processing and targeting of Pgp disrupted interactions between the NBDs such as in DY490, G269V (ICL2), P709G (linker), G722A (TM7) and A841L (TM9).
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ABCB1 p.Pro709Gly 16442101:519:163
status: NEW
PMID: 10455147
[PubMed]
Loo TW et al: "The transmembrane domains of the human multidrug resistance P-glycoprotein are sufficient to mediate drug binding and trafficking to the cell surface."
No.
Sentence
Comment
29
EXPERIMENTAL PROCEDURES Generation of Deletion Mutants-The cDNAs coding for full-length MDR1 (36), mutant P709G (37), or the N-half and C-half P-gp molecules (14) and containing the epitope for monoclonal antibody A52 at the C-terminal ends were subcloned into the mammalian expression vector pMT21.
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ABCB1 p.Pro709Gly 10455147:29:106
status: NEW43 For expression studies involving drug resistance assays, the cDNAs of the A52-tagged wild-type, mutant P709G, N-half, C-half, and TMD1ϩ2 were also inserted into the Epstein-Barr virus-based vector, pREP4 (Invitrogen Inc.).
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ABCB1 p.Pro709Gly 10455147:43:103
status: NEW137 The cDNAs for the A52-tagged wild-type, and P-gp mutants P709G, N-half, C-half, and TMD1ϩ2 were inserted into the pREP4 vector and transfected into HEK 293(EBNA-1) cells.
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ABCB1 p.Pro709Gly 10455147:137:57
status: NEW138 Mutant P709G was included because it shows similar processing defects as mutant TMD1ϩ2.
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ABCB1 p.Pro709Gly 10455147:138:7
status: NEW139 When mutant P709G is expressed in HEK 293 cells in the absence of drug substrate, the major product is a protein of 150 kDa that is retained in the endoplasmic reticulum as a core-glycosylated intermediate (37).
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ABCB1 p.Pro709Gly 10455147:139:12
status: NEW145 For mutant P709G, the major product in the absence of drug substrate was the 150-kDa (core-glycosylated) protein, while the 170-kDa protein was the major product in the presence of substrate. When N-half (90-kDa) P-gp was co-expressed with C-half P-gp in the presence of substrate, another N-half protein of 115 kDa was present.
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ABCB1 p.Pro709Gly 10455147:145:11
status: NEW155 Fig. 6A shows that the mature forms of wild-type, mutant P709G, N-half, and TMD1ϩ2 P-gps were still present in the cells after treatment with cyclosporin A followed by vinblastine.
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ABCB1 p.Pro709Gly 10455147:155:57
status: NEW170 In mutant P709G or in the half-molecules of P-gp, preincubation of the cells with cyclosporin A greatly increased the relative resistance to vinblastine.
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ABCB1 p.Pro709Gly 10455147:170:10
status: NEW171 The cells expressing mutant P709G that were not pretreated with cyclosporin A showed about an 8-fold increase in resistance to vinblastine relative to the control cells.
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ABCB1 p.Pro709Gly 10455147:171:28
status: NEW195 A, HEK 293(EBNA-1) cells were transfected with pREP4 vector (B, Control) or pREP4 vectors containing cDNAs for full-length wild-type P-gp (Wild), mutant P709G, or TMD1ϩ2, or they were cotransfected with the cDNAs for the N-half and C-half of P-gp (Halves).
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ABCB1 p.Pro709Gly 10455147:195:153
status: NEW
PMID: 15530432
[PubMed]
Loo TW et al: "Thapsigargin or curcumin does not promote maturation of processing mutants of the ABC transporters, CFTR, and P-glycoprotein."
No.
Sentence
Comment
69
A processing mutation in NBD2 is P1194A, while P709G is in the linker region.
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ABCB1 p.Pro709Gly 15530432:69:47
status: NEW