ABCC7 p.Lys1468*
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PMID: 12919146
[PubMed]
Bienvenu T et al: "Mutations located in exon 24 of the CFTR gene are associated with a mild cystic fibrosis phenotype."
No.
Sentence
Comment
33
Similarly, in vitro the C-terminally mutant CFTR (K1468X) did not bind to the first PDZ domain of NHERF (6).
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ABCC7 p.Lys1468* 12919146:33:50
status: NEW
No.
Sentence
Comment
61
To construct the ⌬F508-K1468X mutant plasmid, the KpnI/HpaI restriction fragment of the pcDNA3-⌬F508-CFTR plasmid, containing the ⌬F508 mutation, was cloned in frame in pcDNA3-CFTR-K1468X.
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ABCC7 p.Lys1468* 17237149:61:30
status: NEWX
ABCC7 p.Lys1468* 17237149:61:202
status: NEW174 As illustrated in Fig. 7, coexpression of ⌬F508-K1468X-CFTR with NHE-RF1 in MDCK cells did not result in any significant changes in the baseline or the forskolin-stimulated Cl-channel activity.
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ABCC7 p.Lys1468* 17237149:174:55
status: NEW190 Effect of NHE-RF1 overexpression on ⌬F508-K1468X in MDCK cells.
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ABCC7 p.Lys1468* 17237149:190:49
status: NEW191 MDCK cells were microinjected with ⌬F508-K1468X (30 g/ml) and NHE-RF1 (50 g/ml) cDNAs. Membrane permeability to halides (p, in min-1 ) was measured under baseline conditions (open bars) and after application of 10 M Fsk (filled bars).
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ABCC7 p.Lys1468* 17237149:191:48
status: NEW197 Finally, the involvement of PDZ domains in such effect is strongly suggested by the use of ⌬F508-K1468X-CFTR, a ⌬F508 mutant lacking the 13 last amino acids involved in PDZ interaction with NHE-RF1.
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ABCC7 p.Lys1468* 17237149:197:104
status: NEW224 Indeed, ⌬F508-K1468X-CFTR exhibited a low basal Cl-channel activity that was insensitive to forskolin in the presence of NHE-RF1.
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ABCC7 p.Lys1468* 17237149:224:21
status: NEW
PMID: 9671706
[PubMed]
Hall RA et al: "A C-terminal motif found in the beta2-adrenergic receptor, P2Y1 receptor and cystic fibrosis transmembrane conductance regulator determines binding to the Na+/H+ exchanger regulatory factor family of PDZ proteins."
No.
Sentence
Comment
43
The following proteins were in vitro translated by using the TNT system (Promega) in the presence of [35 S]methionine: full-length CFTR-4, CFTR-K1468X, or fusion proteins of CFTR cloned into the pET33b vector (Novagen) (C-terminal amino acids 1387-1480 or N-terminal amino acids 1-80).
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ABCC7 p.Lys1468* 9671706:43:144
status: NEW111 Conversely, neither the N-terminal portion of CFTR nor a C-terminally truncated mutant CFTR (K1468X) exhibited detectable binding to NHERF.
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ABCC7 p.Lys1468* 9671706:111:93
status: NEW163 Full-length CFTR and CFTR C terminus bound avidly to the NHERF but CFTR N terminus and CFTR K1468X did not detectably bind.
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ABCC7 p.Lys1468* 9671706:163:92
status: NEW
PMID: 22964850
[PubMed]
Castellani S et al: "NHERF1 and CFTR restore tight junction organisation and function in cystic fibrosis airway epithelial cells: role of ezrin and the RhoA/ROCK pathway."
No.
Sentence
Comment
34
Wild-type CFTR inserted in pcDNA3.1 was already described.16 CFTR K1468X lacking the 12 C-terminal amino acids,17 inserted into pTM1, was generously provided by Prof. MJ Welsh (University of Iowa, Iowa City, USA).
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ABCC7 p.Lys1468* 22964850:34:66
status: NEW103 Transfection of CFTR-NH2 and K1468X gave no effect on occludin, while in case of claudin 1 and JAM-1 it produced a less pronounced effect than transfection of wild-type CFTR and NHERF1 (Supplementary Figures 2-4).
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ABCC7 p.Lys1468* 22964850:103:29
status: NEW