ABCC7 p.Phe833Leu

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PMID: 21594798 [PubMed] Kanelis V et al: "NMR spectroscopy to study the dynamics and interactions of CFTR."
No. Sentence Comment
127 As a disordered protein having a high fraction of charged residues, the R region was more easily amenable to solution NMR studies, once a better behaved construct containing the polymorphism F833L was identified (20).
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ABCC7 p.Phe833Leu 21594798:127:191
status: NEW
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PMID: 22278744 [PubMed] Liang X et al: "Phosphorylation-dependent 14-3-3 protein interactions regulate CFTR biogenesis."
No. Sentence Comment
261 The human CFTR R region (654- 838; F833L) was expressed from a pPROEX HTb vector (Invitrogen) with an N-terminal hexahistidine tag and purified as described previously (Baker et al., 2007).
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ABCC7 p.Phe833Leu 22278744:261:34
status: NEW
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262 (Note that the F833L polymorphism yields an R region that is significantly more soluble.)
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ABCC7 p.Phe833Leu 22278744:262:15
status: NEW
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PMID: 24191035 [PubMed] Bozoky Z et al: "Regulatory R region of the CFTR chloride channel is a dynamic integrator of phospho-dependent intra- and intermolecular interactions."
No. Sentence Comment
237 The human CFTR R region (aa 654-838; F833L) was prepared as described in the work by Baker et al. (23), and the F833L polymorphism was used to optimize solubility.
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ABCC7 p.Phe833Leu 24191035:237:37
status: NEW
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ABCC7 p.Phe833Leu 24191035:237:112
status: NEW
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