ABCC7 p.Gly406Ala
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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
133
The G406A mutant responded normally to cGMP (Fig. 7a,c).
X
ABCC7 p.Gly406Ala 8548288:133:4
status: NEW148 (b) Effect of V397A substitution compared with the wild-type CFTR (n = 5).
X
ABCC7 p.Gly406Ala 8548288:148:14
status: NEW149 (c) Effect of G406A or K420A substitutions compared with wild-type CFTR (n= 4).
X
ABCC7 p.Gly406Ala 8548288:149:14
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.
X
ABCC7 p.Gly406Ala 8548288:152:52
status: NEW175 The substitution of an alanine for the glycine at position 406, which replaced the minimal proton with a bulkier methyl group, had no effect on activation by cGMP As this glycine is invariant, the substitution was predicted to be disruptive.
X
ABCC7 p.Gly406Ala 8548288:175:23
status: NEW132 The G406A mutant responded normally to cGMP (Fig. 7a,c).
X
ABCC7 p.Gly406Ala 8548288:132:4
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.Gly406Ala 8548288:151:52
status: NEW174 The substitution of an alanine for the glycine at position 406, which replaced the minimal proton with a bulkier methyl group, had no effect on activation by cGMP As this glycine is invariant, the substitution was predicted to be disruptive.
X
ABCC7 p.Gly406Ala 8548288:174:23
status: NEW