D443 of the N Domain of Na+,K+-ATPase Interacts with the ATP−Mg2+ Complex, Possibly via a Second Mg2+ Ion
Author:
Affiliation:
1. Department of Biological Chemistry, Weizmann Institute of Science, Rehovoth 76100, Israel
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi051921v
Reference37 articles.
1. OCCLUDED CATIONS IN ACTIVE TRANSPORT
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1. The Conformation of ATP within the Na,K-ATPase Nucleotide Site: A Statistically Constrained Analysis of REDOR Solid-State NMR Data;Angewandte Chemie International Edition;2011-06-10
2. The Conformation of ATP within the Na,K-ATPase Nucleotide Site: A Statistically Constrained Analysis of REDOR Solid-State NMR Data;Angewandte Chemie;2011-06-10
3. Capillary Endothelial Na+, K+, ATPase Transporter Homeostasis and a New Theory for Migraine Pathophysiology;Headache: The Journal of Head and Face Pain;2010-03
4. ATP-binding Modes and Functionally Important Interdomain Bonds of Sarcoplasmic Reticulum Ca2+-ATPase Revealed by Mutation of Glycine 438, Glutamate 439, and Arginine 678;Journal of Biological Chemistry;2007-07
5. Modulatory and catalytic modes of ATP binding by the calcium pump;The EMBO Journal;2006-05-18
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