ABCC7 p.Ser955Cys
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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
118
Supporting this argument, internal diamide also inhibited activity of a mutant S768C/K951C, S768C/H954C, or S768C/ S955C, and inhibition was reversed by 4-6 mM DTT (Fig. 2E).
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ABCC7 p.Ser955Cys 21059651:118:115
status: NEW119 In sharp contrast, both diamide and DTT had no effect on such CFTR constructs as K951C, H954C, and S955C.
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ABCC7 p.Ser955Cys 21059651:119:99
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.Ser955Cys 21059651:122:82
status: NEW162 Because disulfide cross-linking of S768C to H950C inhibited more channel activity than that of S768C to S955C (Fig. 2E), it is more possible for His950 to form an inhibitory H-bond with Ser768 .
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ABCC7 p.Ser955Cys 21059651:162:104
status: NEW