ABCC7 p.Phe508*
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PMID: 18324337
[PubMed]
Rogers CS et al: "Production of CFTR-null and CFTR-DeltaF508 heterozygous pigs by adeno-associated virus-mediated gene targeting and somatic cell nuclear transfer."
No.
Sentence
Comment
73
Therefore, F508X would be expected to trigger nonsense-mediated mRNA decay as well as prematurely interrupt any translation of CFTR.
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ABCC7 p.Phe508* 18324337:73:11
status: NEW
PMID: 18463704
[PubMed]
Serohijos AW et al: "Diminished self-chaperoning activity of the DeltaF508 mutant of CFTR results in protein misfolding."
No.
Sentence
Comment
170
Interestingly, Thibodeau et al. found that NBD1F508W , the only F508X mutant with a lower folding efficiency than NBD1DF508 , can be rescued by introducing the compensating mutation W496F, which is exactly in the same loop that contains Q493 and F594 [9].
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ABCC7 p.Phe508* 18463704:170:64
status: NEW
PMID: 22265408
[PubMed]
Rabeh WM et al: "Correction of both NBD1 energetics and domain interface is required to restore DeltaF508 CFTR folding and function."
No.
Sentence
Comment
117
These and additional results discussed in the following section show that both folding efficiency and PM density of WT variants increased at $37- and $14-fold steeper slopes, respectively, than their DF508 or F508X counterparts as a function of NBD1 Tm (Figures 5A and 5B) and suggest that NBD1 folding energetics can define the WT but not DF508 CFTR domain-domain assembly.
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ABCC7 p.Phe508* 22265408:117:209
status: NEW118 These and additional results discussed in the following section show that both folding efficiency and PM density of WT variants increased at 37- and 14-fold steeper slopes, respectively, than their DF508 or F508X counterparts as a function of NBD1 Tm (Figures 5A and 5B) and suggest that NBD1 folding energetics can define the WT but not DF508 CFTR domain-domain assembly.
X
ABCC7 p.Phe508* 22265408:118:209
status: NEW