ABCC7 p.Glu115Arg
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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
124
To probe the potential mechanisms by which mutation of these charged residues leads to CF, we first recorded the single-channel behavior of a series of CFTR channel mutants bearing a single mutation at one of the six charged sites (D110R, D112R, K114D, E115R, E116R, or R117A).
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ABCC7 p.Glu115Arg 25024266:124:253
status: NEW132 In contrast, D112R- and E115R-CFTR each mainly opened to the full open state with subconductance states appearing as rare events and mean burst durations very close to that of WT-CFTR.
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ABCC7 p.Glu115Arg 25024266:132:24
status: NEW145 (A) Representative single-channel current traces and their all-points histograms for WT-, D110R-, D112R-, K114D-, E115R-, E116R-, and R117A-CFTR from inside-out membrane patches excised from Xenopus oocytes, with symmetrical 150 mM Cl&#e032; solution in the presence of 1 mM MgATP and 50 U/ml PKA.
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ABCC7 p.Glu115Arg 25024266:145:114
status: NEW149 (B and C) Single-channel amplitudes of the full open state (B) and mean burst durations (C) of WT-, D110R-, D112R-, K114D-, E115R-, E116R-, and R117A-CFTR.
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ABCC7 p.Glu115Arg 25024266:149:124
status: NEW