A topological switch in CFTR modulates channel activity and sensitivity to unfolding-Reference-Cited by-同舟云学术

A topological switch in CFTR modulates channel activity and sensitivity to unfolding

Published:2021-08-02 Issue:9 Volume:17 Page:989-997
ISSN:1552-4450
Container-title:Nature Chemical Biology
language:en
Short-container-title:Nat Chem Biol

Author:

Scholl Daniel^ORCID,Sigoillot Maud,Overtus Marie,Martinez Rafael Colomer,Martens Chloé,Wang Yiting,Pardon Els^ORCID,Laeremans Toon,Garcia-Pino Abel,Steyaert Jan^ORCID,Sheppard David N.^ORCID,Hendrix Jelle^ORCID,Govaerts Cédric^ORCID

Publisher

Springer Science and Business Media LLC

Subject

Cell Biology,Molecular Biology

Link

https://www.nature.com/articles/s41589-021-00844-0.pdf

Reference60 articles.

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3. Zhang, Z., Liu, F. & Chen, J. Molecular structure of the ATP-bound, phosphorylated human CFTR. Proc. Natl Acad. Sci. USA 115, 12757–12762 (2018).

4. Lukacs, G. L. & Verkman, A. S. CFTR: folding, misfolding and correcting the ΔF508 conformational defect. Trends Mol. Med. 18, 81–91 (2012).

5. Serohijos, A. W. R. et al. Phenylalanine-508 mediates a cytoplasmic-membrane domain contact in the CFTR 3D structure crucial to assembly and channel function. Proc. Natl Acad. Sci. USA 105, 3256–3261 (2008).

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