ABCC7 p.Glu1126Cys
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PMID: 25024266
[PubMed]
Cui G et al: "Three charged amino acids in extracellular loop 1 are involved in maintaining the outer pore architecture of CFTR."
No.
Sentence
Comment
402
The single-channel amplitudes of R117C- and R117C/E1126C-CFTR were slightly, but significantly, smaller than that of WT-CFTR (Fig. 12 C).
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ABCC7 p.Glu1126Cys 25024266:402:50
status: NEW410 (A) Representative single-channel current traces of E1126R-, R117E/E1126R-, R117C-, and R117C/E1126C-CFTR recorded under the same experimental conditions as Fig. 2 and their all-points amplitude histograms (right).
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ABCC7 p.Glu1126Cys 25024266:410:94
status: NEW412 #, P < 0.01 indicates a significant difference between WTand R117C-CFTR; **, P < 0.01 indicates a significant difference between WTand E1126R-CFTR, between R117C and R117E/E1126R-CFTR, and between R117C and R117C/E1126C.
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ABCC7 p.Glu1126Cys 25024266:412:213
status: NEW431 R117C/E1126C-CFTR exhibited very brief openings to multiple open states, including s1, s2, and f, with significantly shorter mean burst duration compared with R117C-CFTR (P < 0.01), likely caused by mutual repulsion by the partial negative charges at the two cysteines, leading to unstable open states (Fig. 12, A and B).
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ABCC7 p.Glu1126Cys 25024266:431:6
status: NEW