ABCC7 p.Ser955Ala
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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."
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141
Similarly, curcumin also activated mutants K946A, K951A, S955A, and Q958A to a different extent in the presence of ATP (Fig. 4E).
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ABCC7 p.Ser955Ala 21059651:141:57
status: NEW145 Especially, S768A and S955A, together with CFTR-⌬R, completely removed PKA dependence (Fig. 4F).
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ABCC7 p.Ser955Ala 21059651:145:22
status: NEW234 Error bars, S.E. TABLE 1 Potential roles in hydrogen bonding at the CL3-R domain interface Note that mutants whose channel activity was increased by curcumin in the presence of ATP are highlighted in boldface type. Residues Role in H-bond Mutants Arg Strong donor H950R, S768R, H950R/S768R, H950R/S768D, H950D/S768R Asp Strong acceptor H950D, S768D, H950D/S768D, H950R/S768D, H950D/S768R Thr, Gln, Ser, His Donor/Acceptor H950Q, S768T, WT Ala Negative control K946A, H950A, K951A, H954A, S955A, Q958A, S737A, S768A, ⌬R Inhibition of CFTR by Ser768 JANUARY 21, 2011•VOLUME 286•NUMBER 3 JOURNAL OF BIOLOGICAL CHEMISTRY 2177 matter whether cAMP was present or not in the extracellular perfusate.
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ABCC7 p.Ser955Ala 21059651:234:488
status: NEW314 On the other hand, K946A, K951A, S955A, and Q958A still promoted channel opening by ATP followed by curcumin (Fig. 4, E and F).
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ABCC7 p.Ser955Ala 21059651:314:33
status: NEW