ABCC7 p.Ser466Leu
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PMID: 11341822
[PubMed]
Zou X et al: "ATP hydrolysis-coupled gating of CFTR chloride channels: structure and function."
No.
Sentence
Comment
207
Mutations of some of the corresponding amino acids in CFTR (S466L in NBD1 or T1246I, S1251N, and T1252P in NBD2) are associated with CF (Figure 3).
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ABCC7 p.Ser466Leu 11341822:207:60
status: NEW
PMID: 11597353
[PubMed]
Boucherot A et al: "Role of CFTR's PDZ1-binding domain, NBF1 and Cl(-) conductance in inhibition of epithelial Na(+) channels in Xenopus oocytes."
No.
Sentence
Comment
38
Using similar PCR techniques, the NBF1 mutants of human CFTR vF508, G551D, S466L, K464A, D572N, KH483/484AA, R487Q, R516A, KR598/600GA, KK611/612AA and K615A were in vitro synthesized (Quickchange, Stratagene).
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ABCC7 p.Ser466Leu 11597353:38:75
status: NEW118 The mutants S466L, KH483/484AA, R516A and KK611/612AA demonstrated a residual Cl3 channel function, which was paralleled by a limited ability to downregulate ENaC.
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ABCC7 p.Ser466Leu 11597353:118:12
status: NEW171 We therefore introduced mutations into NBF1 sites which are essential for binding/hydrolysis of ATP and GTP and which have homology to GTP binding proteins such as Walker A (loop L1) (K464A, S466L), switch I motif (KH483/484AA, R487A), switch II motif (loop L4, G551D) and Walker B (D572N) [23].
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ABCC7 p.Ser466Leu 11597353:171:191
status: NEW