Distance determinations at the active site of kidney (Na+ + K+ )-ATPase by Mn(II) ion electron paramagnetic resonance
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(80)80244-4/fullpdf
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1. Role of magnesium ions in the conformational change reported by fluorescein 5'-isothiocyanate modification of sodium-potassium-ATPase;Biochemistry;1993-06-15
2. ATP dependence of Na(+)-K+ pump of cold-sensitive and cold-tolerant mammalian red blood cells.;The Journal of Physiology;1992-10-01
3. Effects of ouabain on the rotational dynamics of renal sodium-potassium ATPase studied by saturation-transfer EPR;Biochemistry;1992-02
4. Polarized infrared absorption of Na+/K+-ATPase studied by attenuated total reflection spectroscopy;Biochimica et Biophysica Acta (BBA) - Biomembranes;1989-09
5. Nuclear Overhauser effect studies of the conformation of Co(NH3)4ATP bound to kidney sodium-potassium ATPase;Biochemistry;1989-05-30
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