ABCC7 p.Cys590Leu
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PMID: 15657297
[PubMed]
Wang W et al: "Reversible silencing of CFTR chloride channels by glutathionylation."
No.
Sentence
Comment
45
A CFTR construct lacking all 18 cysteines (16CS C590L/592L) was provided by D. Gadsby (Rockefeller University, New York, NY) (Mense et al., 2004).
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ABCC7 p.Cys590Leu 15657297:45:48
status: NEW
PMID: 17036051
[PubMed]
Mense M et al: "In vivo phosphorylation of CFTR promotes formation of a nucleotide-binding domain heterodimer."
No.
Sentence
Comment
26
Nor could C590 and C592 be replaced by alanine, threonine or phenylalanine (Figure 2B), but function was similar to that of the 16CS background when they were replaced by leucines (16CS þ C590L/C592L; Figure 2A and B) or valines (16CS þ C590V/C592V; Figure 2B).
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ABCC7 p.Cys590Leu 17036051:26:193
status: NEW30 (A) Two-microelectrode voltage-clamp current recordings from uninjected oocyte and oocytes expressing WT CFTR (2.5 ng cRNA) or HA-tagged Cys-free CFTR 16CS þ C590L/C592L (20 ng cRNA); vertical current deflections monitor conductance, which was transiently increased by brief exposure to 40 mM forskolin (between arrows).
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ABCC7 p.Cys590Leu 17036051:30:163
status: NEW199 For recording macroscopic currents of split CFTR channels in excised patches (Figure 10), oocytes were Table I Forward primers for site-directed mutagenesis PCR C76S 50 -GCCCTTCGGCGATcgTTTTTCTGGAG-30 C276S 50 -CTGTTAAGGCCTACTcCTGGGAAGAAGC-30 C832S 50 -CGAAGAAGACCTTAAGGAGTcCTTTTTTGATGATATGGAGAGC-30 EagI site 50 -GGTAAAATTAAGCACAGcGGccGAATTTCATTCTGTTCTC-30 HA epitope 50 -CGGGCCGCCATGtAcccatAcGACGttccgGAttAcgcaAGGTCGCCTCTGG-30 CFTR 16CS C590A/C592A 50 -GGAGATCTTCGAGAGCgCTGTCgCTAAACTGATGGC-30 CFTR 16CS C590F/C592F 50 -GGAGATCTTCGAGAGCTtTGTCTtTAAACTGATGGC-30 CFTR 16CS C590L/C592L 50 -GGAGATCTTCGAGAGCctTGTCctTAAACTGATGGC-30 CFTR 16CS C590T/C592T 50 -GGAGATCTTCGAGAGCaCTGTCaCTAAACTGATGGC-30 CFTR 16CS C590V/C592V 50 -GGAGATCTTCGAGAGCgtcGTCgtTAAACTGATGGC-30 S434C 50 -CCTCTTCTTCAGTAATTTCTgtCTaCTTGGTACTCCTGTC-30 S459C 50 -GTTGGCGGTTGCTGGATgCACTGGAGCAGGCAAG-3 A462C 50 -GCTGGATCCACTGGGtgcGGCAAGACTTCACTTC-30 L549C 50 -GGTGGAATCACACtatGcGGAGGTCAACGAGCACG-30 S605C 50 -GGATTTTGGTCACaTgTAAAATGGAAC-30 S1248C 50 -CCTCTTGGGAAGAACCGGtTgtGGGAAGAGTAC-30 D1336C 50 -GTTTCCTGGGAAGCTTtgCTTTGTCCTTGTGG-30 L1346C 50 -GGATGGGGGCTCTGTCTgtAGTCATGGCCACAAGC-30 A1374C 50 -GATGAACCAAGCtgTCATTTAGATCC-30 V1379C 50 -GCTCATTTAGATCCgtgcACATACCAAATAATTCG-30 The underlined bases are the codons for the introduced serines, cysteines or other residues; lowercase letters mark base changes from the original sequence, including those for introducing diagnostic restriction endonuclease sites.
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ABCC7 p.Cys590Leu 17036051:199:570
status: NEW
PMID: 17911111
[PubMed]
Wang Y et al: "Correctors promote maturation of cystic fibrosis transmembrane conductance regulator (CFTR)-processing mutants by binding to the protein."
No.
Sentence
Comment
23
Cys-less CFTR was constructed by replacing Cys590 and Cys592 with leucine (9) and the other 16 endogenous cysteines at positions 76, 126, 225, 276, 343, 491, 524, 657, 832, 866, 1344, 1355, 1395, 1400, 1410, and 1458 with alanine.
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ABCC7 p.Cys590Leu 17911111:23:43
status: NEW
PMID: 18361776
[PubMed]
Loo TW et al: "Correctors promote folding of the CFTR in the endoplasmic reticulum."
No.
Sentence
Comment
46
A cysteine-less CFTR was constructed by replacing Cys590 and Cys592 with leucine and by changing all other endogenous cysteine residues to alanine [23].
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ABCC7 p.Cys590Leu 18361776:46:50
status: NEW92 Cysteine-less CFTR, in which Cys590 and Cys592 were replaced with leucine and the remaining cysteine residues were changed to alanine [23], did not mature at 37◦ C unless Val510 (in NBD1) was changed to alanine [17].
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ABCC7 p.Cys590Leu 18361776:92:29
status: NEW
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.Cys590Leu 19754156:42:77
status: NEW
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.Cys590Leu 16766608:23:138
status: NEW
PMID: 23709221
[PubMed]
Cui G et al: "Two salt bridges differentially contribute to the maintenance of cystic fibrosis transmembrane conductance regulator (CFTR) channel function."
No.
Sentence
Comment
49
All cRNAs for single channel recording were prepared from constructs encoding WT-CFTR or Cys-less CFTR (16C 3 S, C590L, C592L) in the pGEMHE vector, which was kindly provided by Dr. D. Gadsby (Rockefeller University) as reported previously (21).
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ABCC7 p.Cys590Leu 23709221:49:113
status: NEW