ABCC7 p.Cys866Ser

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Publications
PMID: 15272010 [PubMed] Chen EY et al: "The DeltaF508 mutation disrupts packing of the transmembrane segments of the cystic fibrosis transmembrane conductance regulator."
No. Sentence Comment
57 The construction of Cys-less CFTR (C76S/C126S/C225S/C276S/C343S/C491S/C524S/C590S/C592S/C657S/C832S/C866S/C1344S/C1355S/C1395S/C1400S/C1410S/C1458S) was performed using the following cDNA fragments.
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ABCC7 p.Cys866Ser 15272010:57:100
status: NEW
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58 Point mutations C76/126S were generated in sequence in the PstI (bp 1) 3 XbaI (bp 573) fragment; point mutations C225S/C276S/C343S were generated in sequence in the XbaI (bp 573) 3 KpnI (bp 1370) fragment; point mutations C491S/C524S/C590S/C592S/C657S were generated in sequence in the KpnI (bp 1370) 3 ApaI (bp 2333) fragment; point mutations C832S/C866S were generated in sequence in the ApaI (bp 2333) 3 EcoRI (bp 3643) fragment; point mutations C1344S/C1355S/ C1395S/C1400S/C1410S/C1458S were generated in sequence in the EcoRI (bp 3643) 3 XhoI (bp 4560) fragment, the five insert fragments were then ligated and inserted into the PstI and XhoI sites of plasmid vector pMT21.
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ABCC7 p.Cys866Ser 15272010:58:350
status: NEW
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PMID: 17036051 [PubMed] Mense M et al: "In vivo phosphorylation of CFTR promotes formation of a nucleotide-binding domain heterodimer."
No. Sentence Comment
180 CFTR with substitutions C128S, C225S, C343S and C866S was provided by Dr DC Dawson (OHSU, Portland, OR, USA).
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ABCC7 p.Cys866Ser 17036051:180:48
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PMID: 19754156 [PubMed] Alexander C et al: "Cystic fibrosis transmembrane conductance regulator: using differential reactivity toward channel-permeant and channel-impermeant thiol-reactive probes to test a molecular model for the pore."
No. Sentence Comment
42 The Cys-less CFTR construct (C76S, C126S, C225S, C276S, C343S, C491S, C524S, C590L, C592L, C657S, C832S, C866S, C1344S, C1355S, C1395S, C1400S, C1410S, C1458S) was a gift from Drs. Martin Mense and David Gadsby and was used in their pGEMHE vector previously described (13).
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ABCC7 p.Cys866Ser 19754156:42:105
status: NEW
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PMID: 21796426 [PubMed] Holstead RG et al: "Functional Differences in Pore Properties Between Wild-Type and Cysteine-Less Forms of the CFTR Chloride Channel."
No. Sentence Comment
4 Other cysteine substitutions (C128S, C225S, C376S, C866S) were without effect.
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ABCC7 p.Cys866Ser 21796426:4:51
status: NEW
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58 In contrast, other point mutants studied (C128S, C225S, C276S, C866S) had conductances that were not significantly different from wild type but were significantly different from cys-less (Fig. 2d).
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ABCC7 p.Cys866Ser 21796426:58:63
status: NEW
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PMID: 16766608 [PubMed] Serrano JR et al: "CFTR: Ligand exchange between a permeant anion ([Au(CN)2]-) and an engineered cysteine (T338C) blocks the pore."
No. Sentence Comment
23 MATERIALS AND METHODS Mutagenesis and in vitro transcription The Cys-less CFTR construct (C76S, C126S, C225S, C276S, C343S, C491S, C524S, C590L, C592L, C657S, C832S, C866S, C1344S, C1355S, C1395S, C1400S, C1410S, C1458S) was a gift from Drs. Martin Mense and Submitted December 28, 2005, and accepted for publication May 19, 2006.
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ABCC7 p.Cys866Ser 16766608:23:166
status: NEW
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