ABCC7 p.Ser1149Cys

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PMID: 21796338 [PubMed] Qian F et al: "Functional arrangement of the 12th transmembrane region in the CFTR chloride channel pore based on functional investigation of a cysteine-less CFTR variant."
No. Sentence Comment
80 Application of MTSES (200 μM) or MTSET (2 mM) to the intracellular solution after channel activation with PKA, ATP, and PPi significantly altered macroscopic current amplitude in nine out of 19 cysteine-substituted mutants tested (N1138C, M1140C, S1141C, T1142C, Q1144C, W1145C, V1147C, N1148C, and S1149C; Figs. 1 and 2).
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ABCC7 p.Ser1149Cys 21796338:80:305
status: NEW
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86 However, unlike previous findings in TM6 [9], we observed a third pattern for cysteines introduced closest to the putative cytoplasmic end of TM12 (V1147C, N1148C, and S1149C).
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ABCC7 p.Ser1149Cys 21796338:86:168
status: NEW
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87 Here, macroscopic current amplitude was decreased by MTSES application but either decreased (V1147C, S1149C) or not significantly affected (N1148C) by MTSET application.
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ABCC7 p.Ser1149Cys 21796338:87:101
status: NEW
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PMID: 22042986 [PubMed] Bai Y et al: "Structural basis for the channel function of a degraded ABC transporter, CFTR (ABCC7)."
No. Sentence Comment
209 However, although they detected reactivity in N1138C and S1149C, we found that these sites appear nonreactive.
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ABCC7 p.Ser1149Cys 22042986:209:57
status: NEW
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