Crystal structures reveal the molecular basis of ion translocation in sodium/proton antiporters
Author:
Publisher
Springer Science and Business Media LLC
Subject
Molecular Biology,Structural Biology
Link
http://www.nature.com/articles/nsmb.3164.pdf
Reference63 articles.
1. Brett, C.L., Donowitz, M. & Rao, R. Evolutionary origins of eukaryotic sodium/proton exchangers. Am. J. Physiol. Cell Physiol. 288, C223–C239 (2005).
2. Fuster, D.G. & Alexander, R.T. Traditional and emerging roles for the SLC9 Na+/H+ exchangers. Pflugers Arch. 466, 61–76 (2014).
3. Verma, V., Bali, A., Singh, N. & Jaggi, A.S. Implications of sodium hydrogen exchangers in various brain diseases. J. Basic Clin. Physiol. Pharmacol. 26, 417–426 (2015).
4. Hunte, C. et al. Structure of a Na+/H+ antiporter and insights into mechanism of action and regulation by pH. Nature 435, 1197–1202 (2005).
5. Lee, C. et al. Crystal structure of the sodium-proton antiporter NhaA dimer and new mechanistic insights. J. Gen. Physiol. 144, 529–544 (2014).
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