ABCC7 p.Val397Ala
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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.Val397Ala 8548288:135:4
status: NEW148 (b) Effect of V397A substitution compared with the wild-type CFTR (n = 5).
X
ABCC7 p.Val397Ala 8548288:148:14
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.Val397Ala 8548288:152:45
status: NEW134 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).
X
ABCC7 p.Val397Ala 8548288:134:4
status: NEW147 (b) Effect of V397A substitution compared with the wild-type CFTR (n = 5).
X
ABCC7 p.Val397Ala 8548288:147:14
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.
X
ABCC7 p.Val397Ala 8548288:151:45
status: NEW