ABCB1 p.Ala985Cys
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PMID: 16492138
[PubMed]
Loo TW et al: "Transmembrane segment 1 of human P-glycoprotein contributes to the drug-binding pocket."
No.
Sentence
Comment
41
A series of double cysteine mutants containing L65C in TM1 with another cysteine in TMD2 (C-terminal TMD containing TM7-TM12) predicted to line the drug-binding pocket [34] (i.e. F942C or T945C in TM11 and L975C, V981C, V982C, G984C or A985C in TM12) were also constructed for cross-linking analysis.
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ABCB1 p.Ala985Cys 16492138:41:236
status: NEW60 Disulphide cross-linking analysis Mutants L65C, F942C, T945C, L975C, V981C, V982C, G984C, A985C, L65C/F942C, L65C/T945C, L65C/975C, L65C/V981C, L65C/V982C, L65C/G984C and L65C/A985C were transiently expressed in HEK-293 cells.
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ABCB1 p.Ala985Cys 16492138:60:90
status: NEWX
ABCB1 p.Ala985Cys 16492138:60:176
status: NEW160 Accordingly, Figure 6 Disulphide cross-linking of P-gp mutants (A) Membranes were prepared from HEK-293 cells (A) expressing mutants L65C, L65C/T945C, L65C/V982C, L65C/G984C or L65C/A985C.
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ABCB1 p.Ala985Cys 16492138:160:184
status: NEW
PMID: 9405384
[PubMed]
Loo TW et al: "Identification of residues in the drug-binding site of human P-glycoprotein using a thiol-reactive substrate."
No.
Sentence
Comment
21
We show that the drug-stimulated ATPase activities of mutants L339C and A342C (TM6) and L975C, V982C, and A985C (TM12) were particularly sensitive to inhibition by dBBn and that the inhibition was prevented by various drug substrates.
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ABCB1 p.Ala985Cys 9405384:21:106
status: NEW83 There was no detectable activity with mutants S344C, G341C, and G984C, whereas mutants A342C, G346C, Q347C, A985C, G989C, and Q990C had much reduced activity (10-40%).
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ABCB1 p.Ala985Cys 9405384:83:108
status: NEW86 A similar pattern was observed for mutants G346C, A985C, G989C, and Q990C, suggesting that the low ATPase activity in these mutants was not due to a processing defect.
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ABCB1 p.Ala985Cys 9405384:86:50
status: NEW98 In contrast, mutants L339C, A342C, L975C, V982C, and A985C were significantly inhibited by dBBn, because they retained only 10, 40, 13, 25, and 32% of their activities, respectively.
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ABCB1 p.Ala985Cys 9405384:98:53
status: NEW99 The concentration of dBBn required to give 50% inhibition of ATPase activity for mutants L339C, L975C, V982C, A985C, and A342C were 90, 112, 320, 480, and 700 M, respectively.
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ABCB1 p.Ala985Cys 9405384:99:110
status: NEW111 The P-glycoproteins(His)10 of Cys-less and mutants L339C, A342C, L975C, V982C, and A985C were mixed with lipid and then preincubated for 15 min at 4 °C without drug or in the presence of 2 mM verapamil (Ver.
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ABCB1 p.Ala985Cys 9405384:111:83
status: NEW114 Mutants A342C and A985C were preincubated with verapamil only.
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ABCB1 p.Ala985Cys 9405384:114:18
status: NEW121 Due to the low ATPase activities of mutants A342C and A985C, their protection assays were done only in the presence of verapamil.
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ABCB1 p.Ala985Cys 9405384:121:54
status: NEW123 As shown in Fig. 4, mutants A342C and A985C were protected from dBBn inactivation by verapamil.
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ABCB1 p.Ala985Cys 9405384:123:38
status: NEW