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10.1073/pnas.1415751111

http://scihub22266oqcxt.onion/10.1073/pnas.1415751111
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C4273333!4273333!25468964
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suck abstract from ncbi


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pmid25468964      Proc+Natl+Acad+Sci+U+S+A 2014 ; 111 (50): E5354-62
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  • Sodium recognition by the Na+/Ca2+ exchanger in the outward-facing conformation #MMPMID25468964
  • Marinelli F; Almagor L; Hiller R; Giladi M; Khananshvili D; Faraldo-Gómez JD
  • Proc Natl Acad Sci U S A 2014[Dec]; 111 (50): E5354-62 PMID25468964show ga
  • Na+/Ca2+ exchangers (NCXs) have a key role in the homeostasis of cellular Ca2+ and consequently are implicated in diverse human-health disorders, including neurodegenerative and cardiovascular diseases. A detailed understanding of the molecular mechanisms of these membrane proteins is therefore of interest from fundamental and biomedical standpoints. Here, we establish the structural mechanism of Na+ recognition in a prokaryotic NCX homolog, using atomistic molecular-dynamics simulations based on recently reported crystallographic data, as well as experimental transport assays of wild-type and mutagenized exchangers. The results have general implications pertaining to the ion exchange stoichiometry and electrogenicity of the Na+/Ca2+ transport cycle across the NCX family, and provide the basis for future investigations of the conformational mechanism of these important transporters.
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