The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
CFTR channel opening by ATP-driven tight dimerization of its nucleotide-binding domains
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Citations
Cites
Smith, P. C., Karpowich, N., Millen, L., Moody, J. E., Rosen, J., Thomas, P. J., & Hunt, J. F. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00576-2 · Cited by 773
Cited by
Inwardly Rectifying Potassium Channels: Their Structure, Function, and Physiological Roles
Hibino, H., Inanobe, A., Furutani, K., Murakami, S., Findlay, I., & Kurachi, Y. (2010) · Physiological Reviews · doi:10.1152/physrev.00021.2009 · Cited by 1,539
CFTR Function and Prospects for Therapy
Riordan, J. R. (2008) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.103004.142532 · Cited by 610
Molecular Structure of the Human CFTR Ion Channel
Liu, F., Zhang, Z., Csanády, L., Gadsby, D. C., & Chen, J. (2017) · Cell · doi:10.1016/j.cell.2017.02.024 · Cited by 523
Self-citationCFTR: folding, misfolding and correcting the ΔF508 conformational defect
Lukacs, G. L., & Verkman, A. S. (2012) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2011.10.003 · Cited by 375
Structure, Gating, and Regulation of the CFTR Anion Channel
Csanády, L., Vergani, P., & Gadsby, D. C. (2019) · Physiological Reviews · doi:10.1152/physrev.00007.2018 · Cited by 262
Self-citation
Metadata
- Authors
- Vergani, P., Lockless, S. W., Nairn, A. C., & Gadsby, D. C.
- Venue
- Nature
- Published
- 2005-02
- Volume
- 433
- Issue
- 7028
- Pages
- 876-880
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2004844038
- Cited by
- 416
- References
- 1
- FWCI
- 23.43
- Type
- journal article
- Language
- en
- Open access
- green
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- CoChat. (2026). Citation check: CFTR channel opening by ATP-driven tight dimerization of its nucleotide-binding domains. https://app.cochat.ai/papers/10.1038/nature03313
- The paper
- Vergani, P., Lockless, S. W., Nairn, A. C., & Gadsby, D. C. (2005). CFTR channel opening by ATP-driven tight dimerization of its nucleotide-binding domains. Nature. https://doi.org/10.1038/nature03313
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
