ABCMdb

ABCC7 p.Phe508Lys

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Publications

PMID: 15619636 [PubMed] Thibodeau PH et al: "Side chain and backbone contributions of Phe508 to CFTR folding."

No. Sentence Comment

92 The known polymorphism F508C and the non-CF-causing variant F508S both showed measurable quantities of band C at steady-state levels, as would be expected for non-CF-causingsubstitutions.Thehydrophobicaminoacidsubstitutions F508I,F508W and F508Y did not produce substantial steady-state levels of band C as measured by western blotting, nor did the ionizable amino acid substitutions F508D, F508E, F508K, F508H or F508R. Login to comment
113 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. Login to comment

PMID: 20667826 [PubMed] Thibodeau PH et al: "The cystic fibrosis-causing mutation deltaF508 affects multiple steps in cystic fibrosis transmembrane conductance regulator biogenesis."

No. Sentence Comment

61 In addition, the ability of a novel second-site suppressor, located within TMD2, to rescue the ⌬F508 and F508K mutants demonstrates that proper domain-domain assembly is critical to CFTR maturation. Login to comment
114 The inclusion of the -3M mutations failed to significantly rescue the folding of the F508D and F508K mutants, suggesting that the -3M suppressors do not directly influence the interaction between NBD1 and other domains of CFTR (Fig. 1B). Login to comment
230 To evaluate the potential mechanisms by which the R1070W mutation rescued ⌬F508, this mutation was also introduced into the ⌬F508-3M and F508K backgrounds (Fig. 6, C and D). Login to comment
231 F508K is expected to disrupt the interdomain interaction, as it interferes with maturation but does not affect the isolated NBD1 (26). Login to comment
234 In this regard, the R1070W mutation induced the formation of Band C in the F508K mutant predicted to disrupt the interdomain interaction, an effect not seen for low temperature or with the -3M mutations (Fig. 6D). Login to comment
250 The suppression of the ⌬F508 and F508P substitutions, but not the F508D and F508K mutants, indicates that these mutations alter CFTR folding by discrete mechanisms or are of differing severities. Login to comment
308 Mutations in ICL4 at position 1070 were evaluated for effects on the trafficking of wild type, ⌬F508, and F508K CFTR, transiently expressed in HEK293 cells. Login to comment
313 Two views, rotated by 90 degrees are shown. B, Western blots show the effects of the ICL4 Arg-1070 mutations on the trafficking of wild type, ⌬F508, and F508K CFTR. Login to comment
316 D, trafficking of the F508K missense protein was evaluated with the R1070W mutation. Login to comment
317 Trafficking of F508K was partially rescued by the R1070W mutation. Login to comment
344 Maturation of the F508K CFTR molecule was potentially facilitated by interactions between the indole side chain from R1070W and the NBD1 surface. Login to comment

PMID: 22265409 [PubMed] Mendoza JL et al: "Requirements for efficient correction of DeltaF508 CFTR revealed by analyses of evolved sequences."

No. Sentence Comment

187 See also Table S2. (C) F508K, F508R, and F508K in combination with I539T, G550E, R553M, R555K, and 3M mutations increase folding yield of NBD1, but exhibit no corresponding increase in CFTR maturation yield (dark blue circles and line, m = 0.03, R = 0.40) (&#b1;SEM, n = 9 along x axis and n = 3 along y axis). Login to comment
197 The experiments with the second-site suppressor mutations on the F508K background demonstrate, regardless of how well NBD1 folds, CFTR is unable to mature if the NBD1-ICL4 is disrupted. Login to comment
241 On the WT or DF508 CFTR models, F508K, R1070, R1070W residues were modeled using the PyMOL (Schrodinger, 2010) mutagenesis function (Figures 1B, 2B, rightmost panel, 5, 6, and S1). Login to comment