ABCC7 p.Ser737Cys
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PMID: 21059651
[PubMed]
Wang G et al: "The inhibition mechanism of non-phosphorylated Ser768 in the regulatory domain of cystic fibrosis transmembrane conductance regulator."
No.
Sentence
Comment
94
S768C or S737C were fixed as an anchor point to search other inhibitory targets from CL3 (Fig. 2A).
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ABCC7 p.Ser737Cys 21059651:94:9
status: NEW122 Similarly, diamide also suppressed channel activity of mutants S737C/H954C, S737C/S955C, and S737C/Q958C, and suppression was reversed by DTT (Fig. 2E).
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ABCC7 p.Ser737Cys 21059651:122:63
status: NEWX
ABCC7 p.Ser737Cys 21059651:122:76
status: NEWX
ABCC7 p.Ser737Cys 21059651:122:93
status: NEW125 Fig. 3 demonstrates that a CFTR construct with a single cysteine S768C, S737C, H950C, or H954C exhibited a clear single band no matter whether diamide or DTT was added.
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ABCC7 p.Ser737Cys 21059651:125:72
status: NEW126 In sharp contrast, CFTR constructs with a cysteine pair (Cys-free background), S737C/H950C, S737C/H954C, S768C/H950C, and S768C/H954C, exhibited an additional cross-linked (X-linked) band because it was induced by diamide but was weakened by DTT.
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ABCC7 p.Ser737Cys 21059651:126:79
status: NEWX
ABCC7 p.Ser737Cys 21059651:126:92
status: NEW128 Therefore, a disulfide bond can be formed between H950C (or H954C) and S768C or between H954C (or H950C) and S737C.
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ABCC7 p.Ser737Cys 21059651:128:109
status: NEW143 In contrast, curcumin had no such effect on S737A and H954A mutants, suggesting that they may be weak inhibitory residues, although disulfide cross-linking of S737C to H954C strongly inhibited channel activity (Figs. 2E and 4E).
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ABCC7 p.Ser737Cys 21059651:143:159
status: NEW