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Referencias:

• Schack, V.R., Morth, J.P., Toustrup-Jensen, M.S., Anthonisen, A.N., Nissen, P., Andersen, J.P., Vilsen, B., Identification and function of a cytoplasmic K+ site of the Na+, K+-ATPase (2008) J. Biol. Chem., 283, pp. 27982-27990
• Shinoda, T., Ogawa, H., Cornelius, F., Toyoshima, C., Crystal structure of the sodium-potassium pump at 2.4 Å resolution (2009) Nature, 459, pp. 446-450
• Glynn, I.M., (1985) The Enzymes of Biological Membranes, pp. 35-114. , A.N. Martonosi, 2nd ed. Plenum Press New York
• Glynn, I.M., Annual review prize lecture "all hands to the sodium pump" (1993) J. Physiol. (Lond.), 462, pp. 1-30
• Skou, J.C., Esmann, M., The Na, K-ATPase (1992) J. Bioenerg. Biomembr., 24, pp. 249-261
• Garrahan, P.J., Glynn, I.M., Factors affecting the relative magnitudes of the sodium:potassium and sodium:sodium exchanges catalysed by the sodium pump (1967) J. Physiol., 192, pp. 189-216
• Fujita, M., Nagano, K., Mizuno, N., Tashima, Y., Nakao, T., Ouabain-sensitive Mg++-ATPase, K+-ATPase and Na+-ATPase activities accompanying a highly specific Na +-K+-ATPase preparation (1967) J. Biochem., 61, pp. 473-477
• Karlish, S.J., Glynn, I.M., An uncoupled efflux of sodium ions from human red cells, probably associated with Na-dependent ATPase activity (1974) Ann. N. Y. Acad. Sci., 242, pp. 461-470
• Plesner, L., Plesner, I.W., Kinetics of Na+-ATPase: Influence of Na+ and K + on substrate binding and hydrolysis (1985) Biochim. Biophys. Acta, 818, pp. 222-234
• Plesner, I.W., Plesner, L., Kinetics of (Na+ + K+)-ATPase: Analysis of the influence of Na+ and K+ by steady-state kinetics (1985) Biochim. Biophys. Acta, 818, pp. 235-250
• Polvani, C., Blostein, R., Protons as substitutes for sodium and potassium in the sodium pump reaction (1988) J. Biol. Chem., 263, pp. 16757-16763
• Lee, K.H., Blostein, R., Red cell sodium fluxes catalysed by the sodium pump in the absence of K+ and ADP (1980) Nature, 285, pp. 338-339
• Blostein, R., Proton-activated rubidium transport catalyzed by the sodium pump (1985) J. Biol. Chem., 260, pp. 829-833
• Hara, Y., Nakao, M., ATP-dependent proton uptake by proteoliposomes reconstituted with purified Na+, K+-ATPase (1986) J. Biol. Chem., 261, pp. 12655-12658
• Hara, Y., Yamada, J., Nakao, M., Proton transport catalyzed by the sodium pump Ouabain-sensitive ATPase activity and the phosphorylation of Na, K-ATPase in the absence of sodium ions (1986) J. Biochem., 99, pp. 531-539
• King, E.L., Altman, C., A schematic method of deriving the rate laws for enzyme-catalyzed reactions (1956) J. Phys. Chem., 60, pp. 1375-1378
• Wong, J.T., Hanes, C.S., Kinetic formulations for enzymic reactions involving two substrates (1962) Can. J. Biochem. Physiol., 40, pp. 763-804
• Cleland, W.W., Partition analysis and the concept of net rate constants as tools in enzyme kinetics (1975) Biochemistry, 14, pp. 3220-3224
• Cha, S., A simple method for derivation of rate equations for enzyme-catalyzed reactions under the rapid equilibrium assumption or combined assumptions of equilibrium and steady state (1968) J. Biol. Chem., 243, pp. 820-825
• Klodos, I., Esmann, M., Post, R.L., Large-scale preparation of sodium-potassium ATPase from kidney outer medulla (2002) Kidney Int., 62, pp. 2097-2100
• Schwarzbaum, P.J., Kaufman, S.B., Rossi, R.C., Garrahan, P.J., An unexpected effect of ATP on the ratio between activity and phosphoenzyme level of Na+/K+-ATPase in steady state (1995) Biochim. Biophys. Acta, 1233, pp. 33-40
• Rossi, R.C., Kaufman, S.B., González Lebrero, R.M., Nørby, J.G., Garrahan, P.J., An attachment for nondestructive, fast quenching of samples in rapid-mixing experiments (1999) Anal. Biochem., 270, pp. 276-285
• Burnham, K.P., Anderson, D.R., (2002) Model Selection and Multimodel Inference: A Practical Information-theoretic Approach, , Springer New York
• Kaufman, S.B., González-Lebrero, R.M., Schwarzbaum, P.J., Nørby, J.G., Garrahan, P.J., Rossi, R.C., Are the states that occlude rubidium obligatory intermediates of the Na+/K+-ATPase reaction? (1999) J. Biol. Chem., 274, pp. 20779-20790
• Poulsen, H., Khandelia, H., Morth, J.P., Bublitz, M., Mouritsen, O.G., Egebjerg, J., Nissen, P., Neurological disease mutations compromise a C-terminal ion pathway in the Na+/K+-ATPase (2010) Nature, 467, pp. 99-102
• Yu, H., Ratheal, I., Artigas, P., Roux, B., Protonation of key acidic residues is critical for the K +-selectivity of the Na/K pump (2011) Nat. Struct. Mol. Biol., 18, pp. 1159-1163
• Forbush, B., Rapid release of 42K and 86Rb from an occluded state of the Na, K-pump in the presence of ATP or ADP (1987) J. Biol. Chem., 262, pp. 11104-11115
• Rossi, R.C., Nørby, J.G., Kinetics of K+-stimulated dephosphorylation and simultaneous K+ occlusion by Na, K-ATPase, studied with the K+ congener Tl+. The possibility of differences between the first turnover and steady state (1993) J. Biol. Chem., 268, pp. 12579-12590
• Gonzalez-Lebrero, R.M., Kaufman, S.B., Garrahan, P.J., Rossi, R.C., The occlusion of Rb+ in the Na+/K +-ATPase II the effects of Rb+, Na+, Mg 2 +, or ATP on the equilibrium between free and occluded Rb + (2002) J. Biol. Chem., 277, pp. 5922-5928
• Peluffo, R.D., Rossi, R.C., Garrahan, P.J., Rega, A.F., Low affinity acceleration of the phosphorylation reaction of the Na, K-ATPase by ATP (1994) J. Biol. Chem., 269, pp. 1051-1056
• Mårdh, S., Zetterqvist, O., Phosphorylation and dephosphorylation reactions of bovine brain (Na +-K+)-stimulated ATP phosphohydrolase studied by a rapid mixing technique (1974) Biochim. Biophys. Acta, 350, pp. 473-483
• Schuurmans Stekhoven, F.M., Swarts, H.G., De Pont, J.J., Bonting, S.L., Na+-like effect of imidazole on the phosphorylation of (Na+ + K+)-ATPase (1985) Biochim. Biophys. Acta, 815, pp. 16-24
• Post, R.L., Hegyvary, C., Kume, S., Activation by adenosine triphosphate in the phosphorylation kinetics of sodium and potassium ion transport adenosine triphosphatase (1972) J. Biol. Chem., 247, pp. 6530-6540
• Beaugé, L., Breakdown of Na+/K+-exchanging ATPase phosphoenzymes formed from ATP and from inorganic phosphate during Na +-ATPase activity (2001) Eur. J. Biochem., 268, pp. 5627-5632
• Blostein, R., Sodium pump-catalyzed sodium-sodium exchange associated with ATP hydrolysis (1983) J. Biol. Chem., 258, pp. 7948-7953
• Segel, I.H., (1975) Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems, pp. 646-647. , Wiley-Interscience
• Heyse, S., Wuddel, I., Apell, H.J., Stürmer, W., Partial reactions of the Na, K-ATPase: Determination of rate constants (1994) J. Gen. Physiol., 104, pp. 197-240
• Pedemonte, C.H., Kinetic mechanism of inhibition of the Na+-pump and some of its partial reactions by external Na+ (Na+o) (1988) J. Theor. Biol., 134, pp. 165-182
• Plesner, I.W., Plesner, L., Nørby, J.G., Klodos, I., The steady-state kinetic mechanism of ATP hydrolysis catalyzed by membrane-bound (Na+ + K+)-ATPase from ox brain. III. A minimal model (1981) Biochim. Biophys. Acta, 643, pp. 483-494
• Plesner, L., Plesner, I.W., Ouabain-inhibited ATPase activity in the absence of Na+ and K+ (1985) The Sodium Pump, Proceedings of the 4th International Conference on the Na,K-ATPase, pp. 469-474. , I.M. Glynn, C. Ellory, The Company of Biologists Ltd
• Fedosova, N.U., Esmann, M., Nucleotide-binding kinetics of Na, K-ATPase: Cation dependence (2004) Biochemistry, 43, pp. 4212-4218

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