ABCC7 p.Phe508Gly
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PMID: 15619636
[PubMed]
Thibodeau PH et al: "Side chain and backbone contributions of Phe508 to CFTR folding."
No.
Sentence
Comment
91
Band C levels in F508A, F508G, F508L and F508V as well as the polar amino acid substitutions F508S, F508T, F508N and F508Q were evident, but substantially reduced relative to wild-type band C levels.
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ABCC7 p.Phe508Gly 15619636:91:24
status: NEW113 W ild type ∆∆F508 F508 F508D F508K F508E F508R F508H F508S F508T F508N F508Q C B Charged Polar F508A F508C F508I F508L ∆F508 F508 W ild type C B F508W F508Y F508G F508P Hydrophobic F508M F508V ̅̆ ̆ ̅ Figure 3 Maturation of full-length CFTR mutants.
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ABCC7 p.Phe508Gly 15619636:113:178
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
69
These results in concert with the effect of F508E, F508R, F508G, F508S, F508D, and F508N mutations revealed that the CD4T-NBD1 PM density was proportional to the domain stability if the NBD1 Tm was >38 C (Figures 3D and S4D).
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ABCC7 p.Phe508Gly 22265408:69:58
status: NEW