Associated Papers
Replacement of several single amino acid side chains exposed to the inside of the ATP-binding pocket induces different extents of affinity change in the high and low affinity ATP-binding sites of rat Na/K-ATPase.
Teramachi S et al.
The Journal of Biological Chemistry, 2002
Importance of Na,K-ATPase residue alpha 1-Arg544 in the segment Arg544-Asp567 for high-affinity binding of ATP, ADP, or MgATP.
Jacobsen MD et al.
Biochemistry, 2002
Structure-function relationships of Na(+), K(+), ATP, or Mg(2+) binding and energy transduction in Na,K-ATPase.
Jorgensen PL et al.
Biochimica Et Biophysica Acta, 2001
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