ABCC7 p.Glu1124Arg
[switch to full view]Comments [show]
None has been submitted yet.
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
224
Tab l e 1 Reversal potentials of WT-CFTR and mutants in ND96 bath solution CFTR n Vrev mV WT 14 &#e032;27.75 &#b1; 0.78 R334A 6 &#e032;12.15 &#b1; 1.64a R117A 6 &#e032;22.51 &#b1; 0.85a E116R 5 &#e032;21.45 &#b1; 1.14a K114D 5 &#e032;24.68 &#b1; 3.22 D110R 5 &#e032;27.64 &#b1; 3.29 R104E 5 &#e032;21.15 &#b1; 1.08a R899C 4 &#e032;25.30 &#b1; 3.94 D891C 6 &#e032;25.81 &#b1; 2.44 K892E 5 &#e032;23.70 &#b1; 3.62 E1124R 5 &#e032;18.32 &#b1; 0.43a E1126R 5 &#e032;20.67 &#b1; 3.16b R117E/E1126R 6 &#e032;23.06 &#b1; 1.37b R104E/E116R 6 &#e032;27.17 &#b1; 1.08 Values are mean &#b1; SEM.
X
ABCC7 p.Glu1124Arg 25024266:224:412
status: NEW240 Mutants D891C- and E1124R- CFTRexhibitedslightchangesinrectificationcompared with WT-CFTR (Fig. S4 C), and reversal potentials were also similar to that of WT-CFTR; the reversal potential of E1124R-CFTR was shifted toward zero (Table 1).
X
ABCC7 p.Glu1124Arg 25024266:240:19
status: NEWX
ABCC7 p.Glu1124Arg 25024266:240:191
status: NEW