ABCC7 p.Lys420Ala
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PMID: 8548288
[PubMed]
Sullivan SK et al: "Identification and partial characterization of a domain in CFTR that may bind cyclic nucleotides directly."
No.
Sentence
Comment
135
The V397A mutant displayed a cGMP response that was enhanced by 66 + 19 % (n = 5; p < 0.05) relative to the wild-type channel (Fig. 7a,b).
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ABCC7 p.Lys420Ala 8548288:135:4
status: NEW136 The K420A substitution, which produced the largest effect, reduced the cGMP response by 75 ± 6 % (n = 4; p < 0.005; Fig. 7a,c) compared with the wild-type channel.
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ABCC7 p.Lys420Ala 8548288:136:4
status: NEW148 (b) Effect of V397A substitution compared with the wild-type CFTR (n = 5).
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ABCC7 p.Lys420Ala 8548288:148:23
status: NEW149 (c) Effect of G406A or K420A substitutions compared with wild-type CFTR (n= 4).
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ABCC7 p.Lys420Ala 8548288:149:23
status: NEW152 The three other single-substitution mutants (V397A, G406A and K420A) produced functional channels that responded to cAMP in a manner identical to wild type, Direct activation may also be modulated by phosphorylation.
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ABCC7 p.Lys420Ala 8548288:152:62
status: NEW178 The substitution of an alanine for the lysine at position 420 was predicted to disrupt an ionic interaction with exocyclic phosphate oxygen, resulting in reduced activation by cGMP.
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ABCC7 p.Lys420Ala 8548288:178:23
status: NEW151 The three other single-substitution mutants (V397A, G406A and K420A) produced functional channels that responded to cAMP in a manner identical to wild type, Direct activation may also be modulated by phosphorylation.
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ABCC7 p.Lys420Ala 8548288:151:62
status: NEW177 The substitution of an alanine for the lysine at position 420 was predicted to disrupt an ionic interaction with exocyclic phosphate oxygen, resulting in reduced activation by cGMP.
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ABCC7 p.Lys420Ala 8548288:177:23
status: NEW