메뉴 건너뛰기




Volumn , Issue , 2008, Pages 57-90

Renal Ion-Translocating ATPases: The P-Type Family

Author keywords

[No Author keywords available]

Indexed keywords


EID: 84882891434     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-012088488-9.50006-1     Document Type: Chapter
Times cited : (2)

References (450)
  • 1
    • 0035873908 scopus 로고    scopus 로고
    • Catalytic function of nongastric H,K-ATPase expressed in Sf-21 insect cells
    • Adams G., Tillekeratne M., Yu C.L., Pestov N.B., Modyanov N.N. Catalytic function of nongastric H,K-ATPase expressed in Sf-21 insect cells. Biochemistry 2001, 40:5765-5776.
    • (2001) Biochemistry , vol.40 , pp. 5765-5776
    • Adams, G.1    Tillekeratne, M.2    Yu, C.L.3    Pestov, N.B.4    Modyanov, N.N.5
  • 2
    • 3242700773 scopus 로고    scopus 로고
    • +-ATPase alpha 3 gene ATP1A3 are associated with rapid-onset dystonia parkinsonism
    • +-ATPase alpha 3 gene ATP1A3 are associated with rapid-onset dystonia parkinsonism. Neuron 2004, 43:169-175.
    • (2004) Neuron , vol.43 , pp. 169-175
    • Agular, P.D.1    Sweadner, K.J.2    Penniston, J.T.3
  • 6
    • 0036720338 scopus 로고    scopus 로고
    • Generation and phenotypic analysis of CHIF knockout mice
    • Aizman R., Asher C., Fuzesi M., et al. Generation and phenotypic analysis of CHIF knockout mice. Am J Physiol Renal Physiol 2002, 283:F569-F577.
    • (2002) Am J Physiol Renal Physiol , vol.283
    • Aizman, R.1    Asher, C.2    Fuzesi, M.3
  • 7
    • 0000770960 scopus 로고
    • Biochemical aspects of active transport
    • Albers R.W. Biochemical aspects of active transport. Ann Rev Biochem 1967, 36:727-756.
    • (1967) Ann Rev Biochem , vol.36 , pp. 727-756
    • Albers, R.W.1
  • 9
    • 0024343117 scopus 로고
    • Electrogenic properties of the Na,K pump
    • Apell H-J. Electrogenic properties of the Na,K pump. J Membr Biol 1989, 110:103-114.
    • (1989) J Membr Biol , vol.110 , pp. 103-114
    • Apell, H.-J.1
  • 10
    • 0023201930 scopus 로고
    • +-ATPase activity in rat proximal convoluted tubule segments
    • +-ATPase activity in rat proximal convoluted tubule segments. Am J Physiol 1987, 252:F39-F45.
    • (1987) Am J Physiol , vol.252
    • Aperia, A.1    Bertorello, A.2    Seri, I.3
  • 12
    • 0029778862 scopus 로고    scopus 로고
    • Substitution of glutamic 779 with alanine in the Na,K-ATPase alpha sub-unit removes voltage dependence of ion transport
    • Argüello J.M., Peluffo R.D., Feng J.N., Lingrel J.B., Berlin J.R. Substitution of glutamic 779 with alanine in the Na,K-ATPase alpha sub-unit removes voltage dependence of ion transport. J Biol Chem 1996, 271:24610-24616.
    • (1996) J Biol Chem , vol.271 , pp. 24610-24616
    • Argüello, J.M.1    Peluffo, R.D.2    Feng, J.N.3    Lingrel, J.B.4    Berlin, J.R.5
  • 13
    • 0028148025 scopus 로고
    • Luminal acidification in K-replete OMCDi: contributions of H-K-ATPase and bafilomycin-A1-sensitive H-ATPase
    • Armitage F.E., Wingo C.S. Luminal acidification in K-replete OMCDi: contributions of H-K-ATPase and bafilomycin-A1-sensitive H-ATPase. Am J Physiol Renal Fluid Electrolyte Physiol 1994, 267:F450-F458.
    • (1994) Am J Physiol Renal Fluid Electrolyte Physiol , vol.267
    • Armitage, F.E.1    Wingo, C.S.2
  • 14
    • 0029166540 scopus 로고
    • Luminal acidification in K-replete OMCDi: inhibition of bicarbonate absorption by K removal and luminal Ba
    • Armitage F.E., Wingo C.S. Luminal acidification in K-replete OMCDi: inhibition of bicarbonate absorption by K removal and luminal Ba. Am J Physiol 1995, 269:F116-F124.
    • (1995) Am J Physiol , vol.269
    • Armitage, F.E.1    Wingo, C.S.2
  • 15
    • 0037458010 scopus 로고    scopus 로고
    • +-ligands modulate gating of palytoxin-induced ion channels
    • +-ligands modulate gating of palytoxin-induced ion channels. Proc Natl Acad Sci U S A 2003, 100:501-505.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 501-505
    • Artigas, P.1    Gadsby, D.C.2
  • 16
    • 1842736450 scopus 로고    scopus 로고
    • Large diameter of palytoxin-induced Na/K pump channels and modulation of palytoxin interaction by Na/K pump ligands
    • Artigas P., Gadsby D.C. Large diameter of palytoxin-induced Na/K pump channels and modulation of palytoxin interaction by Na/K pump ligands. J Gen Physiol 2004, 123:357-376.
    • (2004) J Gen Physiol , vol.123 , pp. 357-376
    • Artigas, P.1    Gadsby, D.C.2
  • 17
    • 0037155802 scopus 로고    scopus 로고
    • Differential regulation of renal Na,K-ATPase by splice variants of the gamma subunit
    • Arystarkhova E., Donnet C., Asinovski N.K., Sweadner K.J. Differential regulation of renal Na,K-ATPase by splice variants of the gamma subunit. J Biol Chem 2002, 277:10162-10172.
    • (2002) J Biol Chem , vol.277 , pp. 10162-10172
    • Arystarkhova, E.1    Donnet, C.2    Asinovski, N.K.3    Sweadner, K.J.4
  • 18
    • 0030884447 scopus 로고    scopus 로고
    • Tissue-specific expression of the Na,K-ATPase beta-3 subunit-the presence of beta-3 in lung and liver addresses the problem of the missing subunit
    • Arystarkhova E., Sweadner K.J. Tissue-specific expression of the Na,K-ATPase beta-3 subunit-the presence of beta-3 in lung and liver addresses the problem of the missing subunit. J Biol Chem 1997, 272:22405-22408.
    • (1997) J Biol Chem , vol.272 , pp. 22405-22408
    • Arystarkhova, E.1    Sweadner, K.J.2
  • 21
    • 0024380774 scopus 로고
    • Immunodetection of Na,K-ATPase alpha 3-isoform in renal and nerve tissues
    • Arystarkhova E.A., Lakhtina O.E., Modyanov N.N. Immunodetection of Na,K-ATPase alpha 3-isoform in renal and nerve tissues. FEBS Lett 1989, 250:545-548.
    • (1989) FEBS Lett , vol.250 , pp. 545-548
    • Arystarkhova, E.A.1    Lakhtina, O.E.2    Modyanov, N.N.3
  • 23
    • 0031964372 scopus 로고    scopus 로고
    • Evolution of substrate specificities in the P-type ATPase superfamily
    • Axelsen K.B., Palmgren M.G. Evolution of substrate specificities in the P-type ATPase superfamily. J Mol Evol 1998, 46:84-101.
    • (1998) J Mol Evol , vol.46 , pp. 84-101
    • Axelsen, K.B.1    Palmgren, M.G.2
  • 25
    • 0025326619 scopus 로고
    • Role of diacylglycerol in adrenergic-stimulated 86Rb uptake by proximal tubules
    • Baines A.D., Drangova R., Ho P. Role of diacylglycerol in adrenergic-stimulated 86Rb uptake by proximal tubules. Am J Physiol 1990, 258:F1133-F1138.
    • (1990) Am J Physiol , vol.258
    • Baines, A.D.1    Drangova, R.2    Ho, P.3
  • 26
    • 0028361579 scopus 로고
    • +-ATPase using in vitro translation
    • +-ATPase using in vitro translation. J Biol Chem 1994, 269:16909-16919.
    • (1994) J Biol Chem , vol.269 , pp. 16909-16919
    • Bamberg, K.1    Sachs, G.2
  • 27
    • 0038457938 scopus 로고    scopus 로고
    • Dopamine-mediated inhibition of renal Na,K-ATPase is reduced by insulin
    • Banday A.A., Asghar M., Hussain T., Lokhandwala M.F. Dopamine-mediated inhibition of renal Na,K-ATPase is reduced by insulin. Hypertension 2003, 41:1353-1358.
    • (2003) Hypertension , vol.41 , pp. 1353-1358
    • Banday, A.A.1    Asghar, M.2    Hussain, T.3    Lokhandwala, M.F.4
  • 28
    • 2442495047 scopus 로고    scopus 로고
    • Deletion of the Na/K-ATPase alpha 1-subunit gene (Atp1a1) does not prevent cavitation of the preimplantation mouse embryo
    • Barcroft L.C., Moseley A.E., Lingrel J.B., Watson A.J. Deletion of the Na/K-ATPase alpha 1-subunit gene (Atp1a1) does not prevent cavitation of the preimplantation mouse embryo. Mech Dev 2004, 121:417-426.
    • (2004) Mech Dev , vol.121 , pp. 417-426
    • Barcroft, L.C.1    Moseley, A.E.2    Lingrel, J.B.3    Watson, A.J.4
  • 29
    • 0027215335 scopus 로고
    • Are there several isoforms of Na,K-ATPase a subunit in the rabbit kidney
    • Barlet-Bas C., Arystarkhova E., Cheval L., et al. Are there several isoforms of Na,K-ATPase a subunit in the rabbit kidney. J Biol Chem 1993, 268:11512-11515.
    • (1993) J Biol Chem , vol.268 , pp. 11512-11515
    • Barlet-Bas, C.1    Arystarkhova, E.2    Cheval, L.3
  • 32
    • 0025274366 scopus 로고
    • Enhanced intracellular sodium concentration in kidney cells recruits a latent pool of Na-K-ATPase whose size is modulated by corticosteroids
    • Barlet-Bas C., Khadouri C., Marsy S., Doucet A. Enhanced intracellular sodium concentration in kidney cells recruits a latent pool of Na-K-ATPase whose size is modulated by corticosteroids. J Biol Chem 1990, 265:7799-7803.
    • (1990) J Biol Chem , vol.265 , pp. 7799-7803
    • Barlet-Bas, C.1    Khadouri, C.2    Marsy, S.3    Doucet, A.4
  • 34
    • 0029079008 scopus 로고
    • Colocalization of H-ATPase and H,K-ATPase immunoreactivity in the rat kidney
    • Bastani B. Colocalization of H-ATPase and H,K-ATPase immunoreactivity in the rat kidney. J Am Soc Nephrol 1995, 5:1476-1482.
    • (1995) J Am Soc Nephrol , vol.5 , pp. 1476-1482
    • Bastani, B.1
  • 35
    • 0023198508 scopus 로고
    • Insulin stimulates volume absorption in the rabbit proximal convoluted tubule
    • Baum M. Insulin stimulates volume absorption in the rabbit proximal convoluted tubule. J Clin Invest 1987, 79:1104-1109.
    • (1987) J Clin Invest , vol.79 , pp. 1104-1109
    • Baum, M.1
  • 36
    • 0031727550 scopus 로고    scopus 로고
    • Inhibition of proximal convoluted tubule transport by dopamine
    • Baum M., Quigley R. Inhibition of proximal convoluted tubule transport by dopamine. Kidney Int 1998, 54:1593-1600.
    • (1998) Kidney Int , vol.54 , pp. 1593-1600
    • Baum, M.1    Quigley, R.2
  • 38
    • 0028874093 scopus 로고
    • Dibutyryl cyclic adenosine monophosphate stimulates the sodium pump in rabbit renal cortical tubules
    • Beck J.S., Marsolais M., Nöel J., Breton S., Laprade R. Dibutyryl cyclic adenosine monophosphate stimulates the sodium pump in rabbit renal cortical tubules. Renal Physiol Biochem 1995, 18:21-26.
    • (1995) Renal Physiol Biochem , vol.18 , pp. 21-26
    • Beck, J.S.1    Marsolais, M.2    Nöel, J.3    Breton, S.4    Laprade, R.5
  • 39
    • 0029830036 scopus 로고    scopus 로고
    • Degradation and endoplasmic reticulum retention of unassembled alpha- and beta-subunits of Na,K-ATPase correlate with interaction of bip
    • Beggah A., Mathews P., Béguin P., Geering K. Degradation and endoplasmic reticulum retention of unassembled alpha- and beta-subunits of Na,K-ATPase correlate with interaction of bip. J Biol Chem 1996, 271:20895-20902.
    • (1996) J Biol Chem , vol.271 , pp. 20895-20902
    • Beggah, A.1    Mathews, P.2    Béguin, P.3    Geering, K.4
  • 40
    • 0027723277 scopus 로고
    • Hydrophobic C-terminal amino acids in the b-subunit are involved in the assembly with a-subunit of Na,K-ATPase
    • Beggah A.T., Béguin P., Jaunin P., Peitsch M.C., Geering K. Hydrophobic C-terminal amino acids in the b-subunit are involved in the assembly with a-subunit of Na,K-ATPase. Biochemistry 1993, 32:14117-14124.
    • (1993) Biochemistry , vol.32 , pp. 14117-14124
    • Beggah, A.T.1    Béguin, P.2    Jaunin, P.3    Peitsch, M.C.4    Geering, K.5
  • 41
    • 0030981919 scopus 로고    scopus 로고
    • Role of glycosylation and disulfide bond formation in the b subunit in the folding and functional expression of Na,K-ATPase
    • Beggah A.T., Jaunin P., Geering K. Role of glycosylation and disulfide bond formation in the b subunit in the folding and functional expression of Na,K-ATPase. J Biol Chem 1997, 272:10318-10326.
    • (1997) J Biol Chem , vol.272 , pp. 10318-10326
    • Beggah, A.T.1    Jaunin, P.2    Geering, K.3
  • 42
    • 0028033536 scopus 로고
    • Phosphorylation of the Na,K-ATPase a-subunit by protein kinase A and C in vitro and in intact cells. Identification of a novel motif for PKC-mediated phosphorylation
    • Béguin P., Beggah A.T., Chibalin A.V., et al. Phosphorylation of the Na,K-ATPase a-subunit by protein kinase A and C in vitro and in intact cells. Identification of a novel motif for PKC-mediated phosphorylation. J Biol Chem 1994, 269:24437-24445.
    • (1994) J Biol Chem , vol.269 , pp. 24437-24445
    • Béguin, P.1    Beggah, A.T.2    Chibalin, A.V.3
  • 43
    • 0035421235 scopus 로고    scopus 로고
    • CHIF, a member of the FXYD protein family, is a regulator of Na,K-ATPase distinct from the gamma-subunit
    • Béguin P., Crambert G., Guennoun S., et al. CHIF, a member of the FXYD protein family, is a regulator of Na,K-ATPase distinct from the gamma-subunit. EMBO J 2001, 20:3993-4002.
    • (2001) EMBO J , vol.20 , pp. 3993-4002
    • Béguin, P.1    Crambert, G.2    Guennoun, S.3
  • 44
    • 0036646065 scopus 로고    scopus 로고
    • FXYD7 is a brain-specific regulator of Na,K-ATPase alpha 1-beta isozymes
    • Béguin P., Crambert G., Monnet-Tschudi F., et al. FXYD7 is a brain-specific regulator of Na,K-ATPase alpha 1-beta isozymes. EMBO J 2002, 21:3264-3273.
    • (2002) EMBO J , vol.21 , pp. 3264-3273
    • Béguin, P.1    Crambert, G.2    Monnet-Tschudi, F.3
  • 45
    • 0029809317 scopus 로고    scopus 로고
    • A1 but not a2 or a3 isoforms of Na,K-ATPase are efficiently phosphorylated in a novel protein kinase C motif
    • Béguin P., Peitsch M.C., Geering K. a1 but not a2 or a3 isoforms of Na,K-ATPase are efficiently phosphorylated in a novel protein kinase C motif. Biochemistry 1996, 35:14098-14108.
    • (1996) Biochemistry , vol.35 , pp. 14098-14108
    • Béguin, P.1    Peitsch, M.C.2    Geering, K.3
  • 46
    • 0039438642 scopus 로고    scopus 로고
    • The g subunit is a specific component of the Na, K-ATPase and modulates its transport function
    • Béguin P., Wang X.Y., Firsov D., et al. The g subunit is a specific component of the Na, K-ATPase and modulates its transport function. EMBO J 1997, 16:4250-4260.
    • (1997) EMBO J , vol.16 , pp. 4250-4260
    • Béguin, P.1    Wang, X.Y.2    Firsov, D.3
  • 47
    • 0020144375 scopus 로고
    • Dopamine decreases fluid reabsorption in straight portions of rabbit proximal tubule
    • Belloreuss E., Higashi Y., Kaneda Y. Dopamine decreases fluid reabsorption in straight portions of rabbit proximal tubule. Am J Physiol 1982, 242:F634-F640.
    • (1982) Am J Physiol , vol.242
    • Belloreuss, E.1    Higashi, Y.2    Kaneda, Y.3
  • 48
    • 0030811629 scopus 로고    scopus 로고
    • + and pH and influences cell shape and adhesiveness
    • + and pH and influences cell shape and adhesiveness. J Biol Chem 1997, 272:20179-20184.
    • (1997) J Biol Chem , vol.272 , pp. 20179-20184
    • Belusa, R.1    Wang, Z.M.2    Matsubara, T.3
  • 49
    • 0032905866 scopus 로고    scopus 로고
    • Corticosteroid-dependent sodium transport in a novel immortalized mouse collecting duct principal cell line
    • Bens M., Vallet V., Cluzeaud F., et al. Corticosteroid-dependent sodium transport in a novel immortalized mouse collecting duct principal cell line. J Am Soc Nephrol 1999, 10:923-934.
    • (1999) J Am Soc Nephrol , vol.10 , pp. 923-934
    • Bens, M.1    Vallet, V.2    Cluzeaud, F.3
  • 50
    • 0030937107 scopus 로고    scopus 로고
    • Phorbol 12-myristate 13-acetate downregulates Na,K-ATPase independent of its protein kinase C site-decrease in basolateral cell surface area
    • Beron J., Forster I., Béguin P., Geering K., Verrey F. Phorbol 12-myristate 13-acetate downregulates Na,K-ATPase independent of its protein kinase C site-decrease in basolateral cell surface area. Mol Biol Cell 1997, 8:387-398.
    • (1997) Mol Biol Cell , vol.8 , pp. 387-398
    • Beron, J.1    Forster, I.2    Béguin, P.3    Geering, K.4    Verrey, F.5
  • 51
    • 0028924230 scopus 로고
    • Aldosterone modulates sodium kinetics of Na,K-ATPase containing an alpha-1 subunit in A6 kidney cell epithelia
    • Beron J., Mastroberardino L., Spillmann A., Verrey F. Aldosterone modulates sodium kinetics of Na,K-ATPase containing an alpha-1 subunit in A6 kidney cell epithelia. Mol Biol Cell 1995, 6:261-271.
    • (1995) Mol Biol Cell , vol.6 , pp. 261-271
    • Beron, J.1    Mastroberardino, L.2    Spillmann, A.3    Verrey, F.4
  • 52
    • 0024557969 scopus 로고
    • +-ATPase activity in kidney proximal tubules: involvement of GTP binding proteins
    • +-ATPase activity in kidney proximal tubules: involvement of GTP binding proteins. Am J Physiol 1989, 256:F57-F62.
    • (1989) Am J Physiol , vol.256
    • Bertorello, A.1    Aperia, A.2
  • 54
    • 0024498475 scopus 로고
    • +-ATPase is an effector protein for protein kinase C in renal proximal tubule cells
    • +-ATPase is an effector protein for protein kinase C in renal proximal tubule cells. Am J Physiol 1989, 256:F370-F373.
    • (1989) Am J Physiol , vol.256
    • Bertorello, A.1    Aperia, A.2
  • 55
    • 0023876939 scopus 로고
    • Proximal tubule Na+-K+-ATPase activitis inhibited during high-salt diet: evidence for DA-mediated effect
    • Bertorello A., Hokfelt T., Goldstein M., Aperia A. Proximal tubule Na+-K+-ATPase activitis inhibited during high-salt diet: evidence for DA-mediated effect. Am J Physiol 1988, 254:F795-F801.
    • (1988) Am J Physiol , vol.254
    • Bertorello, A.1    Hokfelt, T.2    Goldstein, M.3    Aperia, A.4
  • 57
    • 0030930189 scopus 로고    scopus 로고
    • Sites of reaction of the gastric H,K-ATPase with extracytoplasmic thiol reagents
    • Besancon M., Simon A., Sachs G., Shin J.M. Sites of reaction of the gastric H,K-ATPase with extracytoplasmic thiol reagents. J Biol Chem 1997, 272:22438-22446.
    • (1997) J Biol Chem , vol.272 , pp. 22438-22446
    • Besancon, M.1    Simon, A.2    Sachs, G.3    Shin, J.M.4
  • 58
    • 0028168363 scopus 로고
    • The a-subunit of the Na,K-ATPase has catalytic activity independent of the b-subunit
    • Blanco G., DeTomaso A.W., Koster J., Xie Z.J., Mercer R.W. The a-subunit of the Na,K-ATPase has catalytic activity independent of the b-subunit. J Biol Chem 1994, 269:23420-23425.
    • (1994) J Biol Chem , vol.269 , pp. 23420-23425
    • Blanco, G.1    DeTomaso, A.W.2    Koster, J.3    Xie, Z.J.4    Mercer, R.W.5
  • 59
    • 0027450805 scopus 로고
    • Functional expression of the a2 and a3 isoforms of th Na,K-ATPase in baculovirus-infected insect cells
    • Blanco G., Xie Z.J., Mercer R.W. Functional expression of the a2 and a3 isoforms of th Na,K-ATPase in baculovirus-infected insect cells. Proc Natl Acad Sci U S A 1993, 90:1824-1828.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 1824-1828
    • Blanco, G.1    Xie, Z.J.2    Mercer, R.W.3
  • 60
    • 0029947132 scopus 로고    scopus 로고
    • Endogenous ouabain-role in the pathogenesis of hypertension
    • Blaustein M.P. Endogenous ouabain-role in the pathogenesis of hypertension. Kidney Int 1996, 49:1748-1753.
    • (1996) Kidney Int , vol.49 , pp. 1748-1753
    • Blaustein, M.P.1
  • 61
    • 0025990187 scopus 로고
    • Pathogenesis of essential hypertension: a link between dietary salt and high blood pressure
    • Blaustein M.P., Hamlyn J.M. Pathogenesis of essential hypertension: a link between dietary salt and high blood pressure. Hypertension 1991, 18(Suppl 3):III184-III195.
    • (1991) Hypertension , vol.18 , Issue.SUPPL.3 , pp. 3184-3195
    • Blaustein, M.P.1    Hamlyn, J.M.2
  • 62
    • 0021112658 scopus 로고
    • The influence of cytoplasmic sodium concentration on the stoichiometry of the sodium pump
    • Blostein R. The influence of cytoplasmic sodium concentration on the stoichiometry of the sodium pump. J Biol Chem 1983, 258:12228-12232.
    • (1983) J Biol Chem , vol.258 , pp. 12228-12232
    • Blostein, R.1
  • 63
    • 0030610588 scopus 로고    scopus 로고
    • Evidence that ser(775) in the alpha subunit of Na,K-ATPase is a residue in the cation binding pocket
    • Blostein R., Wilczynska A., Karlish S.J.D., Argüello J.M., Lingrel J.B. Evidence that ser(775) in the alpha subunit of Na,K-ATPase is a residue in the cation binding pocket. J Biol Chem 1997, 272:24987-24993.
    • (1997) J Biol Chem , vol.272 , pp. 24987-24993
    • Blostein, R.1    Wilczynska, A.2    Karlish, S.J.D.3    Argüello, J.M.4    Lingrel, J.B.5
  • 64
    • 0035290265 scopus 로고    scopus 로고
    • Coordinate control of Na,K-ATPase mRNA expression by aldosterone, vasopressin and cell sodium delivery in the cortical collecting duct
    • Blot-Chabaud M., Djelidi S., Courtois-Coutry N., et al. Coordinate control of Na,K-ATPase mRNA expression by aldosterone, vasopressin and cell sodium delivery in the cortical collecting duct. Cell Mol Biol 2001, 47:247-253.
    • (2001) Cell Mol Biol , vol.47 , pp. 247-253
    • Blot-Chabaud, M.1    Djelidi, S.2    Courtois-Coutry, N.3
  • 69
    • 0032962733 scopus 로고    scopus 로고
    • Acute regulation by corticosteroids of channel-inducing factor gene messenger ribonucleic acid in the distal colon
    • Brennan F.E., Fuller P.J. Acute regulation by corticosteroids of channel-inducing factor gene messenger ribonucleic acid in the distal colon. Endocrinology 1999, 140:1213-1218.
    • (1999) Endocrinology , vol.140 , pp. 1213-1218
    • Brennan, F.E.1    Fuller, P.J.2
  • 72
    • 0031954657 scopus 로고    scopus 로고
    • +-ATPase in the rat outer medullary collecting duct during potassium depletion
    • +-ATPase in the rat outer medullary collecting duct during potassium depletion. J Am Soc Nephrol 1998, 9:538-550.
    • (1998) J Am Soc Nephrol , vol.9 , pp. 538-550
    • Buffin-Meyer, B.1    Verbavatz, J.M.2    Cheval, L.3
  • 75
    • 0027452091 scopus 로고
    • The Wilson disease gene is a putative copper transporting P-type ATPase similar to the Menkes gene
    • Bull P.C., Thomas G.R., Rommens J.M., Forbes J.R., Cox D.W. The Wilson disease gene is a putative copper transporting P-type ATPase similar to the Menkes gene. Nat Genet 1993, 5:327-337.
    • (1993) Nat Genet , vol.5 , pp. 327-337
    • Bull, P.C.1    Thomas, G.R.2    Rommens, J.M.3    Forbes, J.R.4    Cox, D.W.5
  • 76
    • 0038143257 scopus 로고    scopus 로고
    • Electrogenicity of Na,K- and H,K-ATPase activity and presence of a positively charged amino acid in the fifth transmembrane segment
    • Burnay M., Crambert G., Kharoubi-Hess S., Geering K., Horisberger J-D. Electrogenicity of Na,K- and H,K-ATPase activity and presence of a positively charged amino acid in the fifth transmembrane segment. J Biol Chem 2003, 278:19237-19244.
    • (2003) J Biol Chem , vol.278 , pp. 19237-19244
    • Burnay, M.1    Crambert, G.2    Kharoubi-Hess, S.3    Geering, K.4    Horisberger, J.-D.5
  • 77
    • 0035195428 scopus 로고    scopus 로고
    • The Bufo marinus bladder H,K-ATPase carries out electroneutral ion transport
    • Burnay M., Geering K., Horisberger J.-D. The Bufo marinus bladder H,K-ATPase carries out electroneutral ion transport. Am J Physiol 2001, 281:F869-F874.
    • (2001) Am J Physiol , vol.281
    • Burnay, M.1    Geering, K.2    Horisberger, J.-D.3
  • 80
    • 0029100527 scopus 로고
    • In situ hybridization of H-KATPase beta-subunit mRNA in rat and rabbit kidney
    • Campbell-Thompson M.L., Verlander J.W., Curran K.A., et al. In situ hybridization of H-KATPase beta-subunit mRNA in rat and rabbit kidney. Am J Physiol 1995, 269:F345-F354.
    • (1995) Am J Physiol , vol.269
    • Campbell-Thompson, M.L.1    Verlander, J.W.2    Curran, K.A.3
  • 81
    • 0026568206 scopus 로고
    • Mutation of a cysteine in the first transmembrane segment of Na-K-ATPase a subunit confers ouabain resistance
    • Canessa C.M., Horisberger J.-D., Louvard D., Rossier B.C. Mutation of a cysteine in the first transmembrane segment of Na-K-ATPase a subunit confers ouabain resistance. EMBO J 1992, 11:1681-1687.
    • (1992) EMBO J , vol.11 , pp. 1681-1687
    • Canessa, C.M.1    Horisberger, J.-D.2    Louvard, D.3    Rossier, B.C.4
  • 83
    • 0035818494 scopus 로고    scopus 로고
    • The expression of the gamma subunit of Na-K-ATPase is regulated by osmolality via C-terminal Jun kinase and phosphatidylinositol 3-kinase-dependent mechanisms
    • Capasso J.M., Rivard C., Berl T. The expression of the gamma subunit of Na-K-ATPase is regulated by osmolality via C-terminal Jun kinase and phosphatidylinositol 3-kinase-dependent mechanisms. Proc Natl Acad Sci U S A 2001, 98:13414-13419.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 13414-13419
    • Capasso, J.M.1    Rivard, C.2    Berl, T.3
  • 84
    • 11144292696 scopus 로고    scopus 로고
    • Synthesis of the Na-K-ATPase gamma-subunit is regulated at both the transcriptional and translational levels in IMCD3 cells
    • Capasso J.M., Rivard C.J., Berl T. Synthesis of the Na-K-ATPase gamma-subunit is regulated at both the transcriptional and translational levels in IMCD3 cells. Am J Physiol Renal Physiol 2005, 288:F76-F81.
    • (2005) Am J Physiol Renal Physiol , vol.288
    • Capasso, J.M.1    Rivard, C.J.2    Berl, T.3
  • 85
    • 0037975649 scopus 로고    scopus 로고
    • Chloride, not sodium, stimulates expression of the gamma subunit of Na/K-ATPase and activates JNK in response to hypertonicity in mouse IMCD3 cells
    • Capasso J.M., Rivard C.J., Enomoto L.M., Berl T. Chloride, not sodium, stimulates expression of the gamma subunit of Na/K-ATPase and activates JNK in response to hypertonicity in mouse IMCD3 cells. Proc Natl Acad Sci U S A 2003, 100:6428-6433.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 6428-6433
    • Capasso, J.M.1    Rivard, C.J.2    Enomoto, L.M.3    Berl, T.4
  • 86
    • 24644481485 scopus 로고    scopus 로고
    • +-ATPase gene mutations linked to familial hemiplegic migraine
    • +-ATPase gene mutations linked to familial hemiplegic migraine. Neuromol Med 2005, 6:105-116.
    • (2005) Neuromol Med , vol.6 , pp. 105-116
    • Capendeguy, O.1    Horisberger, J.-D.2
  • 87
    • 0029848868 scopus 로고    scopus 로고
    • Cellular localization and regulation of CHIF in kidney and colon
    • Capurro C., Coutry N., Bonvalet J.P., et al. Cellular localization and regulation of CHIF in kidney and colon. Am J Physiol Cell Physiol 1996, 40:C753-C762.
    • (1996) Am J Physiol Cell Physiol , vol.40
    • Capurro, C.1    Coutry, N.2    Bonvalet, J.P.3
  • 88
    • 0028113894 scopus 로고
    • Biogenesis: plasma membrane calcium ATPase-15 years of work on the purified enzyme
    • Carafoli E. Biogenesis: plasma membrane calcium ATPase-15 years of work on the purified enzyme. FASEB J 1994, 8:993-1002.
    • (1994) FASEB J , vol.8 , pp. 993-1002
    • Carafoli, E.1
  • 91
    • 0030569288 scopus 로고    scopus 로고
    • +-ATPase alpha-subunit phosphorylation by a cAMP-dependent signalling pathway in intact cells from rat kidney cortex
    • +-ATPase alpha-subunit phosphorylation by a cAMP-dependent signalling pathway in intact cells from rat kidney cortex. FEBS Lett 1996, 396:309-314.
    • (1996) FEBS Lett , vol.396 , pp. 309-314
    • Carranza, M.L.1    Féraille, E.2    Kiroytcheva, M.3    Rousselot, M.4    Favre, H.5
  • 92
    • 0030754545 scopus 로고    scopus 로고
    • The complete inventory of the yeast saccharomyces cerevisiae P-type transport ATPases
    • Catty P., Dexaerde A.D., Goffeau A. The complete inventory of the yeast saccharomyces cerevisiae P-type transport ATPases. FEBS Lett 1997, 409:325-332.
    • (1997) FEBS Lett , vol.409 , pp. 325-332
    • Catty, P.1    Dexaerde, A.D.2    Goffeau, A.3
  • 93
  • 94
    • 0006262658 scopus 로고
    • +-ATPase subunits along the rat nephron by polymerase chain reaction
    • Steinkopff, Darmstadt, E. Bamberg, W. Schoner (Eds.)
    • +-ATPase subunits along the rat nephron by polymerase chain reaction. The Sodium Pump 1994, 704-709. Steinkopff, Darmstadt. E. Bamberg, W. Schoner (Eds.).
    • (1994) The Sodium Pump , pp. 704-709
    • Cheval, L.1    Barlet-Bas, C.2    Doucet, A.3
  • 95
    • 0025041280 scopus 로고
    • Measurement of Na-K-ATPase-mediated rubidium influx in single segments of rat nephron
    • Cheval L., Doucet A. Measurement of Na-K-ATPase-mediated rubidium influx in single segments of rat nephron. Am J Physiol Renal Fluid Electrolyte Physiol 1990, 259:F111-F121.
    • (1990) Am J Physiol Renal Fluid Electrolyte Physiol , vol.259
    • Cheval, L.1    Doucet, A.2
  • 96
    • 0031021581 scopus 로고    scopus 로고
    • Re-evaluation of the expression of the gastric H,K-atpase alpha subunit along the rat nephron
    • Cheval L., Elalouf J.M., Doucet A. Re-evaluation of the expression of the gastric H,K-atpase alpha subunit along the rat nephron. Pflügers Arch 1997, 433:539-541.
    • (1997) Pflügers Arch , vol.433 , pp. 539-541
    • Cheval, L.1    Elalouf, J.M.2    Doucet, A.3
  • 98
    • 0033593228 scopus 로고    scopus 로고
    • +-ATPase is initiated by phosphorylation of ser-18 in the rat alpha subunit and is responsible for the decreased activity in epithelial cells
    • +-ATPase is initiated by phosphorylation of ser-18 in the rat alpha subunit and is responsible for the decreased activity in epithelial cells. J Biol Chem 1999, 274:1920-1927.
    • (1999) J Biol Chem , vol.274 , pp. 1920-1927
    • Chibalin, A.V.1    Ogimoto, G.2    Pedemonte, C.H.3
  • 103
    • 0020489227 scopus 로고
    • +)- ATPase proteolipid labeled with a photoaffinity derivative of ouabain
    • +)- ATPase proteolipid labeled with a photoaffinity derivative of ouabain. Biochim Biophys Acta 1982, 686:7-12.
    • (1982) Biochim Biophys Acta , vol.686 , pp. 7-12
    • Collins, J.H.1    Forbush, B.2    Lane, L.K.3
  • 104
    • 0030977127 scopus 로고    scopus 로고
    • Subunit interactions in the Na,K-ATPase explored with the yeast two-hybrid system
    • Colonna T.E., Huynh L., Fambrough D.M. Subunit interactions in the Na,K-ATPase explored with the yeast two-hybrid system. J Biol Chem 1997, 272:12366-12372.
    • (1997) J Biol Chem , vol.272 , pp. 12366-12372
    • Colonna, T.E.1    Huynh, L.2    Fambrough, D.M.3
  • 108
    • 0030797573 scopus 로고    scopus 로고
    • A tyrosine-based signal targets H/K-atpase to a regulated compartment and is required for the cessation of gastric acid secretion
    • Courtois-Coutry N., Roush D., Rajendran V., et al. A tyrosine-based signal targets H/K-atpase to a regulated compartment and is required for the cessation of gastric acid secretion. Cell 1997, 90:501-510.
    • (1997) Cell , vol.90 , pp. 501-510
    • Courtois-Coutry, N.1    Roush, D.2    Rajendran, V.3
  • 111
    • 0037188308 scopus 로고    scopus 로고
    • Bm, a structural member of the X,K-ATPase beta subunit family, resides in the ER and does not associate with any known X,K-ATPase alpha subunit
    • Crambert G., Béguin P., Pestov N.B., Modyanov N.N., Geering K. bm, a structural member of the X,K-ATPase beta subunit family, resides in the ER and does not associate with any known X,K-ATPase alpha subunit. Biochemistry 2002, 41:6723-6733.
    • (2002) Biochemistry , vol.41 , pp. 6723-6733
    • Crambert, G.1    Béguin, P.2    Pestov, N.B.3    Modyanov, N.N.4    Geering, K.5
  • 112
    • 0037143722 scopus 로고    scopus 로고
    • Phospholemman (FXYD1) associates with Na,K-ATPase and regulates its transport properties
    • Crambert G., Fuzesi M., Garty H., Karlish S.J.D., Geering K. Phospholemman (FXYD1) associates with Na,K-ATPase and regulates its transport properties. Proc Natl Acad Sci U S A 2002, 99:11476-11481.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 11476-11481
    • Crambert, G.1    Fuzesi, M.2    Garty, H.3    Karlish, S.J.D.4    Geering, K.5
  • 113
    • 0037458166 scopus 로고    scopus 로고
    • FXYD proteins: new tissue-specific regulators of the ubiquitous Na,K-ATPase
    • Crambert G., Geering K. FXYD proteins: new tissue-specific regulators of the ubiquitous Na,K-ATPase. Sci STKE 2003, (66):RE1.
    • (2003) Sci STKE , Issue.66
    • Crambert, G.1    Geering, K.2
  • 114
    • 0034695680 scopus 로고    scopus 로고
    • Transport and pharmacological properties of nine different human Na,K-ATPase isozymes
    • Crambert G., Hasler U., Beggah A.T., et al. Transport and pharmacological properties of nine different human Na,K-ATPase isozymes. J Biol Chem 2000, 275:1976-1986.
    • (2000) J Biol Chem , vol.275 , pp. 1976-1986
    • Crambert, G.1    Hasler, U.2    Beggah, A.T.3
  • 116
    • 18244401341 scopus 로고    scopus 로고
    • FXYD3 (Mat-8), a new regulator of Na,K-ATPase
    • Crambert G., Li C.M., Claeys D., Geering K. FXYD3 (Mat-8), a new regulator of Na,K-ATPase. Mol Biol Cell 2005, 16:2363-2371.
    • (2005) Mol Biol Cell , vol.16 , pp. 2363-2371
    • Crambert, G.1    Li, C.M.2    Claeys, D.3    Geering, K.4
  • 117
    • 3142682294 scopus 로고    scopus 로고
    • FXYD7, mapping of functional sites involved in endoplasmic reticulum export, association with and regulation of Na,K-ATPase
    • Crambert G., Li C.M., Swee L.K., Geering K. FXYD7, mapping of functional sites involved in endoplasmic reticulum export, association with and regulation of Na,K-ATPase. J Biol Chem 2004, 279:30888-30895.
    • (2004) J Biol Chem , vol.279 , pp. 30888-30895
    • Crambert, G.1    Li, C.M.2    Swee, L.K.3    Geering, K.4
  • 118
    • 1642579506 scopus 로고    scopus 로고
    • New molecular determinants controlling the accessibility of ouabain to its binding site in human Na,K-ATPase alpha isoforms
    • Crambert G., Schaer D., Roy S., Geering K. New molecular determinants controlling the accessibility of ouabain to its binding site in human Na,K-ATPase alpha isoforms. Mol Pharmacol 2004, 65:335-341.
    • (2004) Mol Pharmacol , vol.65 , pp. 335-341
    • Crambert, G.1    Schaer, D.2    Roy, S.3    Geering, K.4
  • 119
    • 0026766656 scopus 로고
    • +-ATPase and mRNA expression in distal colon, kidney, and uterus
    • +-ATPase and mRNA expression in distal colon, kidney, and uterus. J Biol Chem 1992, 267:13740-13748.
    • (1992) J Biol Chem , vol.267 , pp. 13740-13748
    • Crowson, M.S.1    Shull, G.E.2
  • 120
    • 0037312922 scopus 로고    scopus 로고
    • + pump alpha 2 subunit associated with familial hemiplegic migraine type 2
    • + pump alpha 2 subunit associated with familial hemiplegic migraine type 2. Nat Genet 2003, 33:192-196.
    • (2003) Nat Genet , vol.33 , pp. 192-196
    • De, F.M.1    Marconi, R.2    Silvestri, L.3
  • 121
    • 0343570013 scopus 로고    scopus 로고
    • +-ATPase activity is correlated with urinary sodium excretion in rat nephrotic syndromes
    • +-ATPase activity is correlated with urinary sodium excretion in rat nephrotic syndromes. J Am Soc Nephrol 2000, 11:604-615.
    • (2000) J Am Soc Nephrol , vol.11 , pp. 604-615
    • Deschenes, G.1    Doucet, A.2
  • 122
    • 0034752561 scopus 로고    scopus 로고
    • Increased synthesis and AVP unresponsiveness of Na,K-ATPase in collecting duct from nephrotic rats
    • Deschenes G., Gonin S., Zolty E., et al. Increased synthesis and AVP unresponsiveness of Na,K-ATPase in collecting duct from nephrotic rats. J Am Soc Nephrol 2001, 12:2241-2252.
    • (2001) J Am Soc Nephrol , vol.12 , pp. 2241-2252
    • Deschenes, G.1    Gonin, S.2    Zolty, E.3
  • 123
    • 0035126825 scopus 로고    scopus 로고
    • Collecting duct is a site of sodium retention in PAN nephrosis: a rationale for amiloride therapy
    • Deschenes G., Wittner M., Di Stefano A., Jounier S., Doucet A. Collecting duct is a site of sodium retention in PAN nephrosis: a rationale for amiloride therapy. J Am Soc Nephrol 2001, 12:598-601.
    • (2001) J Am Soc Nephrol , vol.12 , pp. 598-601
    • Deschenes, G.1    Wittner, M.2    Di, S.A.3    Jounier, S.4    Doucet, A.5
  • 124
    • 23344445947 scopus 로고    scopus 로고
    • Phospholemman-phosphorylation mediates the b-adrenergic effects on Na/K pump function in cardiac myocytes
    • Despa S., Bossuyt J., Han F., et al. Phospholemman-phosphorylation mediates the b-adrenergic effects on Na/K pump function in cardiac myocytes. Circ Res 2005, 97:252-259.
    • (2005) Circ Res , vol.97 , pp. 252-259
    • Despa, S.1    Bossuyt, J.2    Han, F.3
  • 125
    • 0027509004 scopus 로고
    • Expression, targeting, and assembly of functional Na,K-ATPase polypeptides in baculovirus -infected insect cells
    • DeTomaso A.W., Jian Xie Z., Liu G., Mercer R.W. Expression, targeting, and assembly of functional Na,K-ATPase polypeptides in baculovirus -infected insect cells. J Biol Chem 1993, 268:1470-1478.
    • (1993) J Biol Chem , vol.268 , pp. 1470-1478
    • DeTomaso, A.W.1    Jian, X.Z.2    Liu, G.3    Mercer, R.W.4
  • 126
    • 32444445051 scopus 로고    scopus 로고
    • Molecular identification of Sch28080-sensitive K-ATPase activities in the mouse kidney
    • Dherbecourt O., Cheval L., Bloch-Faure M., Meneton P., Doucet A. Molecular identification of Sch28080-sensitive K-ATPase activities in the mouse kidney. Pflügers Arch 2006, 451(6):769-775.
    • (2006) Pflügers Arch , vol.451 , Issue.6 , pp. 769-775
    • Dherbecourt, O.1    Cheval, L.2    Bloch-Faure, M.3    Meneton, P.4    Doucet, A.5
  • 127
    • 0034863197 scopus 로고    scopus 로고
    • Basolateral translocation by vasopressin of the aldosterone-induced pool of latent Na-K-ATPases is accompanied by alpha 1 subunit dephosphorylation: Study in a new aldosterone-sensitive rat cortical collecting duct cell line
    • Djelidi S., Beggah A., Courtois-Coutry N., et al. Basolateral translocation by vasopressin of the aldosterone-induced pool of latent Na-K-ATPases is accompanied by alpha 1 subunit dephosphorylation: Study in a new aldosterone-sensitive rat cortical collecting duct cell line. J Am Soc Nephrol 2001, 12:1805-1818.
    • (2001) J Am Soc Nephrol , vol.12 , pp. 1805-1818
    • Djelidi, S.1    Beggah, A.2    Courtois-Coutry, N.3
  • 128
    • 0031438982 scopus 로고    scopus 로고
    • Transcriptional regulation of sodium transport by vasopressin in renal cells
    • Djelidi S., Fay M., Cluzeaud F., et al. Transcriptional regulation of sodium transport by vasopressin in renal cells. J Biol Chem 1997, 272:32919-32924.
    • (1997) J Biol Chem , vol.272 , pp. 32919-32924
    • Djelidi, S.1    Fay, M.2    Cluzeaud, F.3
  • 129
    • 0037053399 scopus 로고    scopus 로고
    • +-ATPase alphasubunit is essential for AP-2 binding and clathrin-dependent endocytosis
    • +-ATPase alphasubunit is essential for AP-2 binding and clathrin-dependent endocytosis. J Biol Chem 2002, 277:17108-17111.
    • (2002) J Biol Chem , vol.277 , pp. 17108-17111
    • Done, S.C.1    Leibiger, I.B.2    Efendiev, R.3
  • 130
    • 12344315651 scopus 로고    scopus 로고
    • The alpha(2)-isoform of Na-K-ATPase mediates ouabain-induced hypertension in mice and increased vascular contractility in vitro
    • Dostanic I., Paul R.J., Lorenz J.N., et al. The alpha(2)-isoform of Na-K-ATPase mediates ouabain-induced hypertension in mice and increased vascular contractility in vitro. Am J Physiol Heart Circ Physiol 2005, 288:H477-H485.
    • (2005) Am J Physiol Heart Circ Physiol , vol.288
    • Dostanic, I.1    Paul, R.J.2    Lorenz, J.N.3
  • 131
    • 0022620365 scopus 로고
    • Evidence for differences in the sensitivity to ouabain of Na-K-ATPase along the nephrons of rabbit kidney
    • Doucet A., Barlet-Bas C. Evidence for differences in the sensitivity to ouabain of Na-K-ATPase along the nephrons of rabbit kidney. J Biol Chem 1986, 261:993-995.
    • (1986) J Biol Chem , vol.261 , pp. 993-995
    • Doucet, A.1    Barlet-Bas, C.2
  • 132
    • 0019614751 scopus 로고
    • Short-term effect of aldosterone on Na-K-ATPase in single nephron segments
    • Doucet A., Katz A.I. Short-term effect of aldosterone on Na-K-ATPase in single nephron segments. Am J Physiol 1981, 241:F273-F278.
    • (1981) Am J Physiol , vol.241
    • Doucet, A.1    Katz, A.I.2
  • 133
    • 0023554066 scopus 로고
    • Characterization of K-ATPase activity in distal nephron: stimulation by potassium depletion
    • Doucet A., Marsy S. Characterization of K-ATPase activity in distal nephron: stimulation by potassium depletion. Am J Physiol 1987, 253:F418-F423.
    • (1987) Am J Physiol , vol.253
    • Doucet, A.1    Marsy, S.2
  • 139
    • 18144428731 scopus 로고    scopus 로고
    • +-ATPase alpha(1)-subunit phosphorylation signal into binding and activation of phosphoinositide 3-kinase during endocytosis
    • +-ATPase alpha(1)-subunit phosphorylation signal into binding and activation of phosphoinositide 3-kinase during endocytosis. J Biol Chem 2005, 280:16272-16277.
    • (2005) J Biol Chem , vol.280 , pp. 16272-16277
    • Efendiev, R.1    Chen, Z.P.2    Krmar, R.T.3
  • 141
    • 0027272056 scopus 로고
    • Regulation of collecting tubule adenosine triphosphatases by aldosterone and potassium
    • Eiam-Ong S., Kurtzman N.A., Sabatini S. Regulation of collecting tubule adenosine triphosphatases by aldosterone and potassium. J Clin Invest 1993, 91:2385-2392.
    • (1993) J Clin Invest , vol.91 , pp. 2385-2392
    • Eiam-Ong, S.1    Kurtzman, N.A.2    Sabatini, S.3
  • 142
    • 0028131421 scopus 로고
    • Effect of respiratory acidosis and respiratory alkalosis on renal transport enzymes
    • Eiam-Ong S., Laski M.E., Kurtzman N.A., Sabatini S. Effect of respiratory acidosis and respiratory alkalosis on renal transport enzymes. Am J Physiol 1994, 267:F390-F399.
    • (1994) Am J Physiol , vol.267
    • Eiam-Ong, S.1    Laski, M.E.2    Kurtzman, N.A.3    Sabatini, S.4
  • 143
    • 17544387513 scopus 로고
    • Changes in tubular basolateral membrane markers after chronic treatment
    • El Mernissi G., Charbades D., Doucet A., et al. Changes in tubular basolateral membrane markers after chronic treatment. Am J Physiol 1983, 245:F100-F109.
    • (1983) Am J Physiol , vol.245
    • El, M.G.1    Charbades, D.2    Doucet, A.3
  • 144
    • 0021054534 scopus 로고
    • Short-term effect of aldosterone on renal sodium transport and tubular Na-K-ATPase in the rat
    • El Mernissi G., Doucet A. Short-term effect of aldosterone on renal sodium transport and tubular Na-K-ATPase in the rat. Pflügers Arch 1983, 399:139-146.
    • (1983) Pflügers Arch , vol.399 , pp. 139-146
    • El, M.G.1    Doucet, A.2
  • 145
    • 17444440121 scopus 로고
    • Quantification of (3H)ouabain binding and turnover of Na-KATPase along the rabbit nephron
    • El Mernissi G., Doucet A. Quantification of (3H)ouabain binding and turnover of Na-KATPase along the rabbit nephron. Am J Physiol 1984, 247:F158-F167.
    • (1984) Am J Physiol , vol.247
    • El, M.G.1    Doucet, A.2
  • 146
    • 0021485839 scopus 로고
    • Stimulation of Na-K-ATPase in the rat collecting tubule by two diuretics: furosemide and amiloride
    • El Mernissi G., Doucet A. Stimulation of Na-K-ATPase in the rat collecting tubule by two diuretics: furosemide and amiloride. Am J Physiol 1984, 247:F485-F490.
    • (1984) Am J Physiol , vol.247
    • El, M.G.1    Doucet, A.2
  • 147
    • 0021019634 scopus 로고
    • Short-term effects of aldosterone and dexamethasone on Na- K-ATPase along the rabbit nephron
    • El Mernissi G., Doucet A. Short-term effects of aldosterone and dexamethasone on Na- K-ATPase along the rabbit nephron. Pflügers Arch 1983, 399:147-151.
    • (1983) Pflügers Arch , vol.399 , pp. 147-151
    • El, M.G.1    Doucet, A.2
  • 148
    • 0031050337 scopus 로고    scopus 로고
    • Expression of the beta-isoforms of Na,K-ATPase in the renal cortex of rats
    • Eleno N., DiezPanero L.M., Rodriguez-Lopez A., et al. Expression of the beta-isoforms of Na,K-ATPase in the renal cortex of rats. Exp Nephrol 1997, 5:82-87.
    • (1997) Exp Nephrol , vol.5 , pp. 82-87
    • Eleno, N.1    DiezPanero, L.M.2    Rodriguez-Lopez, A.3
  • 149
    • 0027231230 scopus 로고
    • Modification of lysine 501 in Na,K-ATPase reveals coupling between cation occupancy and changes in the ATP binding domain
    • Ellis-Davies G.C.R., Kaplan J.H. Modification of lysine 501 in Na,K-ATPase reveals coupling between cation occupancy and changes in the ATP binding domain. J Biol Chem 1993, 268:11622-11627.
    • (1993) J Biol Chem , vol.268 , pp. 11622-11627
    • Ellis-Davies, G.C.R.1    Kaplan, J.H.2
  • 151
    • 0030920317 scopus 로고    scopus 로고
    • Noncoordinate regulation of epithelial Na channel and Na pump subunit mRNAs in kidney and colon by aldosterone
    • Escoubet B., Coureau C., Bonvalet J.P., Farman N. Noncoordinate regulation of epithelial Na channel and Na pump subunit mRNAs in kidney and colon by aldosterone. Am J Physiol Cell Physiol 1997, 41:C1482-C1491.
    • (1997) Am J Physiol Cell Physiol , vol.41
    • Escoubet, B.1    Coureau, C.2    Bonvalet, J.P.3    Farman, N.4
  • 153
    • 0021173423 scopus 로고
    • The amino acid sequence of a fluorescein- labeled peptide from the active site of (Na, K)-ATPase
    • Farley R.A., Tran C.M., Carilli C.T., Hawke D., Shively J.E. The amino acid sequence of a fluorescein- labeled peptide from the active site of (Na, K)-ATPase. J Biol Chem 1984, 259:9532-9535.
    • (1984) J Biol Chem , vol.259 , pp. 9532-9535
    • Farley, R.A.1    Tran, C.M.2    Carilli, C.T.3    Hawke, D.4    Shively, J.E.5
  • 156
    • 0038578683 scopus 로고    scopus 로고
    • Cell-specific expression of three members of the FXYD family along the renal tubule
    • Farman N., Fay M., Cluzeaud F. Cell-specific expression of three members of the FXYD family along the renal tubule. Ann N Y Acad Sci 2003, 986:428-436.
    • (2003) Ann N Y Acad Sci , vol.986 , pp. 428-436
    • Farman, N.1    Fay, M.2    Cluzeaud, F.3
  • 157
    • 0032828651 scopus 로고    scopus 로고
    • Intrarenal distribution of the colonic H,K-ATPase mRNA in rabbit
    • Fejes-Tóth G., Naray F.T., Velazquez H., et al. Intrarenal distribution of the colonic H,K-ATPase mRNA in rabbit. Kidney Int 1999, 56:1029-1036.
    • (1999) Kidney Int , vol.56 , pp. 1029-1036
    • Fejes-Tóth, G.1    Naray, F.T.2    Velazquez, H.3
  • 158
    • 0034890089 scopus 로고    scopus 로고
    • Immunohistochemical localization of colonic H-KATPase to the apical membrane of connectingtubule cells
    • Fejes-Tóth G., Naray-Fejes-Toth A. Immunohistochemical localization of colonic H-KATPase to the apical membrane of connectingtubule cells. Am J Physiol Renal Physiol 2001, 281:F318-F325.
    • (2001) Am J Physiol Renal Physiol , vol.281
    • Fejes-Tóth, G.1    Naray-Fejes-Toth, A.2
  • 160
    • 0027275069 scopus 로고
    • Identification of a functional thyroid hormone response element in the upstream flanking region of the human Na, K-ATPase b1 gene
    • Feng J., Orlowski J., Lingrel J.B. Identification of a functional thyroid hormone response element in the upstream flanking region of the human Na, K-ATPase b1 gene. Nucleic Acids Res 1993, 21:2619-2626.
    • (1993) Nucleic Acids Res , vol.21 , pp. 2619-2626
    • Feng, J.1    Orlowski, J.2    Lingrel, J.B.3
  • 161
    • 0029022454 scopus 로고
    • Functional consequences of substitutions of the carboxyl residue glutamate 779 of the Na,K-ATPase
    • Feng J.N., Lingrel J.B. Functional consequences of substitutions of the carboxyl residue glutamate 779 of the Na,K-ATPase. Cell Mol Biol Res 1995, 41:29-37.
    • (1995) Cell Mol Biol Res , vol.41 , pp. 29-37
    • Feng, J.N.1    Lingrel, J.B.2
  • 163
    • 9844223081 scopus 로고
    • Insulin stimulates Na, K-ATPase through tyrosine phosphorylation of its a subunit in rat cortical collecting tubules
    • Féraille E., Carranza M.L., Rousselot M., Caverzasio J., Favre H. Insulin stimulates Na, K-ATPase through tyrosine phosphorylation of its a subunit in rat cortical collecting tubules. J Am Soc Nephrol 1995, 6:336.
    • (1995) J Am Soc Nephrol , vol.6 , pp. 336
    • Féraille, E.1    Carranza, M.L.2    Rousselot, M.3    Caverzasio, J.4    Favre, H.5
  • 164
    • 0027981732 scopus 로고
    • Insulin enhances sodium sensitivity of Na-K-ATPase in isolated rat proximal convoluted tubule
    • Féraille E., Carranza M.L., Rousselot M., Favre H. Insulin enhances sodium sensitivity of Na-K-ATPase in isolated rat proximal convoluted tubule. Am J Physiol 1994, 267:F55-F62.
    • (1994) Am J Physiol , vol.267
    • Féraille, E.1    Carranza, M.L.2    Rousselot, M.3    Favre, H.4
  • 166
    • 0026653060 scopus 로고
    • Sites of antinatriuretic action of insulin along rat nephron
    • Féraille E., Marsy S., Cheval L., et al. Sites of antinatriuretic action of insulin along rat nephron. Am J Physiol 1992, 263:F175-F179.
    • (1992) Am J Physiol , vol.263
    • Féraille, E.1    Marsy, S.2    Cheval, L.3
  • 167
    • 0027245489 scopus 로고
    • Mechanism of enhanced Na-K-ATPase activity in cortical collecting duct from rats with nephrotic syndrome
    • Féraille E., Vogt B., Rousselot M., et al. Mechanism of enhanced Na-K-ATPase activity in cortical collecting duct from rats with nephrotic syndrome. J Clin Invest 1993, 91:1295-1300.
    • (1993) J Clin Invest , vol.91 , pp. 1295-1300
    • Féraille, E.1    Vogt, B.2    Rousselot, M.3
  • 170
    • 4043050179 scopus 로고    scopus 로고
    • Organ hypertrophic signaling within caveolae membrane subdomains triggered by ouabain and antagonized by PST 2238
    • Ferrandi M., Molinari I., Barassi P., et al. Organ hypertrophic signaling within caveolae membrane subdomains triggered by ouabain and antagonized by PST 2238. J Biol Chem 2004, 279:33306-33314.
    • (2004) J Biol Chem , vol.279 , pp. 33306-33314
    • Ferrandi, M.1    Molinari, I.2    Barassi, P.3
  • 171
    • 0030798864 scopus 로고    scopus 로고
    • Phosphorylation of Na,K-atpase by protein kinase C at ser(18) occurs in intact cells but does not result in direct inhibition of ATP hydrolysis
    • Feschenko M.S., Sweadner K.J. Phosphorylation of Na,K-atpase by protein kinase C at ser(18) occurs in intact cells but does not result in direct inhibition of ATP hydrolysis. J Biol Chem 1997, 272:17726-17733.
    • (1997) J Biol Chem , vol.272 , pp. 17726-17733
    • Feschenko, M.S.1    Sweadner, K.J.2
  • 172
    • 0029850427 scopus 로고    scopus 로고
    • +-ATPase derived from beta-galactosidase fusion proteins expressed in yeast
    • +-ATPase derived from beta-galactosidase fusion proteins expressed in yeast. J Biol Chem 1996, 271:29312-29320.
    • (1996) J Biol Chem , vol.271 , pp. 29312-29320
    • Fiedler, B.1    Scheiner-Bobis, G.2
  • 173
  • 174
    • 0001546554 scopus 로고
    • Cardiotonic steroid binding to Na,K-ATPase
    • Forbush B3. Cardiotonic steroid binding to Na,K-ATPase. Curr Top Membr Transport 1983, 19:167-201.
    • (1983) Curr Top Membr Transport , vol.19 , pp. 167-201
    • Forbush, B.1
  • 175
    • 0017893008 scopus 로고
    • Characterization of a new photoaffinity derivative of ouabain: labeling of the large polypeptide and of a proteolipid component of the Na, K-ATPase
    • Forbush B3., Kaplan J.H., Hoffman J.F. Characterization of a new photoaffinity derivative of ouabain: labeling of the large polypeptide and of a proteolipid component of the Na, K-ATPase. Biochemistry 1978, 17:3667-3676.
    • (1978) Biochemistry , vol.17 , pp. 3667-3676
    • Forbush, B.1    Kaplan, J.H.2    Hoffman, J.F.3
  • 177
    • 0037376604 scopus 로고    scopus 로고
    • Cardiac ischemia causes inhibition of the Na/K ATPase by a labile cytosolic compound whose production is linked to oxidant stress
    • Fuller W., Parmar V., Eaton P., Bell J.R., Shattock M.J. Cardiac ischemia causes inhibition of the Na/K ATPase by a labile cytosolic compound whose production is linked to oxidant stress. Cardiovasc Res 2003, 57:1044-1051.
    • (2003) Cardiovasc Res , vol.57 , pp. 1044-1051
    • Fuller, W.1    Parmar, V.2    Eaton, P.3    Bell, J.R.4    Shattock, M.J.5
  • 178
    • 0019581781 scopus 로고
    • Mineralocorticoid effects on Na-K-ATPase in individual nephron segments
    • Garg L.C., Knepper M.A., Burg M.B. Mineralocorticoid effects on Na-K-ATPase in individual nephron segments. Am J Physiol 1981, 240:F536-F544.
    • (1981) Am J Physiol , vol.240
    • Garg, L.C.1    Knepper, M.A.2    Burg, M.B.3
  • 179
    • 0023936434 scopus 로고
    • Ouabain-insensitive K-adenosine triphosphatase in distal nephron segments of the rabbit
    • Garg L.C., Narang N. Ouabain-insensitive K-adenosine triphosphatase in distal nephron segments of the rabbit. J Clin Invest 1988, 81:1024-1028.
    • (1988) J Clin Invest , vol.81 , pp. 1024-1028
    • Garg, L.C.1    Narang, N.2
  • 180
    • 0022049212 scopus 로고
    • Glucocorticoid effects on Na-K ATPase in rabbit nephron segments
    • Garg L.C., Narang N., Wingo C.S. Glucocorticoid effects on Na-K ATPase in rabbit nephron segments. Am J Physiol 1985, 248:F487-F491.
    • (1985) Am J Physiol , vol.248
    • Garg, L.C.1    Narang, N.2    Wingo, C.S.3
  • 181
    • 0036783541 scopus 로고    scopus 로고
    • A functional interaction between CHIF and Na-K-ATPase: implication for regulation by FXYD proteins
    • Garty H., Lindzen M., Scanzano R., et al. A functional interaction between CHIF and Na-K-ATPase: implication for regulation by FXYD proteins. Am J Physiol Renal Physiol 2002, 283:F607-F615.
    • (2002) Am J Physiol Renal Physiol , vol.283
    • Garty, H.1    Lindzen, M.2    Scanzano, R.3
  • 182
    • 0034773778 scopus 로고    scopus 로고
    • The functional role of beta subunits in oligomeric P-type ATPases
    • Geering K. The functional role of beta subunits in oligomeric P-type ATPases. J Bioenerg Biomembr 2001, 33:425-438.
    • (2001) J Bioenerg Biomembr , vol.33 , pp. 425-438
    • Geering, K.1
  • 185
    • 0025817601 scopus 로고
    • The functional role of the b-subunit in the maturation and intracellular transport of Na,K-ATPase
    • Geering K. The functional role of the b-subunit in the maturation and intracellular transport of Na,K-ATPase. FEBS Lett 1991, 285:189-193.
    • (1991) FEBS Lett , vol.285 , pp. 189-193
    • Geering, K.1
  • 186
    • 0029905492 scopus 로고    scopus 로고
    • Oligomerization and maturation of Na,K-ATPase- functional interaction of the cytoplasmic NH2 terminus of the beta subunit with the alpha subunit
    • Geering K., Beggah A., Good P., et al. Oligomerization and maturation of Na,K-ATPase- functional interaction of the cytoplasmic NH2 terminus of the beta subunit with the alpha subunit. J Cell Biol 1996, 133:1193-1204.
    • (1996) J Cell Biol , vol.133 , pp. 1193-1204
    • Geering, K.1    Beggah, A.2    Good, P.3
  • 187
    • 0034680338 scopus 로고    scopus 로고
    • Intersubunit interactions in human X,K-ATPases: role of membrane domains M9 and M10 in the assembly process and association efficiency of human, nongastric H,K-ATPase alpha subunits (ATP1al1) with known beta subunits
    • Geering K., Crambert G., Yu C.L., et al. Intersubunit interactions in human X,K-ATPases: role of membrane domains M9 and M10 in the assembly process and association efficiency of human, nongastric H,K-ATPase alpha subunits (ATP1al1) with known beta subunits. Biochemistry 2000, 39:12688-12698.
    • (2000) Biochemistry , vol.39 , pp. 12688-12698
    • Geering, K.1    Crambert, G.2    Yu, C.L.3
  • 189
    • 0027474170 scopus 로고
    • Na,K-ATPase in several tissues of the rat: tissue-specific expression of subunit mRNAs and enzyme activity
    • Gick G.G., Hatala M.A., Chon D., Ismail-Beigi F. Na,K-ATPase in several tissues of the rat: tissue-specific expression of subunit mRNAs and enzyme activity. J Membr Biol 1993, 131:229-236.
    • (1993) J Membr Biol , vol.131 , pp. 229-236
    • Gick, G.G.1    Hatala, M.A.2    Chon, D.3    Ismail-Beigi, F.4
  • 191
    • 0025293107 scopus 로고
    • Thyroidal enhancement of rat myocardial Na,KATPase: preferential expression of a2 activity and mRNA abundance
    • Gick G.G., Melikian J., Ismail-Beigi F. Thyroidal enhancement of rat myocardial Na,KATPase: preferential expression of a2 activity and mRNA abundance. J Membr Biol 1990, 115:273-282.
    • (1990) J Membr Biol , vol.115 , pp. 273-282
    • Gick, G.G.1    Melikian, J.2    Ismail-Beigi, F.3
  • 192
    • 9444286543 scopus 로고
    • Renal potassium transport
    • Springer Verlag, Berlin, G. Giebisch, D.C. Tosteson, H.H. Ussing (Eds.)
    • Giebisch G. Renal potassium transport. Membrane Transport in Biology 1979, Volume IV A:215-298. Springer Verlag, Berlin. G. Giebisch, D.C. Tosteson, H.H. Ussing (Eds.).
    • (1979) Membrane Transport in Biology , vol.IV A , pp. 215-298
    • Giebisch, G.1
  • 194
    • 0025138388 scopus 로고
    • The adhesion molecule on glia (AMOG) is a homologue of the b subunit of the Na,K-ATPase
    • Gloor S., Antonicek H., Sweadner K.J., et al. The adhesion molecule on glia (AMOG) is a homologue of the b subunit of the Na,K-ATPase. J Cell Biol 1990, 110:165-174.
    • (1990) J Cell Biol , vol.110 , pp. 165-174
    • Gloor, S.1    Antonicek, H.2    Sweadner, K.J.3
  • 195
    • 0027566787 scopus 로고
    • All hands to the sodium pump
    • Glynn I.M. All hands to the sodium pump. J Physiol (London) 1993, 462:1-30.
    • (1993) J Physiol (London) , vol.462 , pp. 1-30
    • Glynn, I.M.1
  • 196
    • 1442303517 scopus 로고    scopus 로고
    • Kidney and colon electrolyte transport in CHIF knockout mice
    • Goldschmidt I., Grahammer F., Warth R., et al. Kidney and colon electrolyte transport in CHIF knockout mice. Cell Physiol Biochem 2004, 14:113-120.
    • (2004) Cell Physiol Biochem , vol.14 , pp. 113-120
    • Goldschmidt, I.1    Grahammer, F.2    Warth, R.3
  • 197
    • 0028982165 scopus 로고
    • Topology of the alpha-subunit of Na,K-ATPase based on proteolysis-lability of the topological organization
    • Goldshleger R., Tal D.M., Karlish S.J.D. Topology of the alpha-subunit of Na,K-ATPase based on proteolysis-lability of the topological organization. Biochemistry 1995, 34:8668-8679.
    • (1995) Biochemistry , vol.34 , pp. 8668-8679
    • Goldshleger, R.1    Tal, D.M.2    Karlish, S.J.D.3
  • 199
    • 0035149523 scopus 로고    scopus 로고
    • Cyclic AMP increases cell surface expression of functional Na,K-ATPase units in mammalian cortical collecting duct principal cells
    • Gonin S., Deschenes G., Roger F., et al. Cyclic AMP increases cell surface expression of functional Na,K-ATPase units in mammalian cortical collecting duct principal cells. Mol Biol Cell 2001, 12:255-264.
    • (2001) Mol Biol Cell , vol.12 , pp. 255-264
    • Gonin, S.1    Deschenes, G.2    Roger, F.3
  • 202
    • 0028346360 scopus 로고
    • Cloning and characterization of the entire cDNA encoded by ATP1AL1-a member of the human Na,K/H,K-ATPase gene family
    • Grishin A.V., Sverdlov V.E., Kostina M.B., Modyanov N.N. Cloning and characterization of the entire cDNA encoded by ATP1AL1-a member of the human Na,K/H,K-ATPase gene family. FEBS Lett 1994, 349:144-150.
    • (1994) FEBS Lett , vol.349 , pp. 144-150
    • Grishin, A.V.1    Sverdlov, V.E.2    Kostina, M.B.3    Modyanov, N.N.4
  • 203
    • 0037181169 scopus 로고    scopus 로고
    • Cysteine-scanning mutagenesis study of the sixth transmembrane segment of the Na,K-ATPase a subunit
    • Guennoun S., Horisberger J.-D. Cysteine-scanning mutagenesis study of the sixth transmembrane segment of the Na,K-ATPase a subunit. FEBS Lett 2002, 513:277-281.
    • (2002) FEBS Lett , vol.513 , pp. 277-281
    • Guennoun, S.1    Horisberger, J.-D.2
  • 204
    • 0034730856 scopus 로고    scopus 로고
    • Structure of the 5th transmembrane segment of the Na,K-ATPase a subunit: a cysteine-scanning mutagenesis study
    • Guennoun S., Horisberger J-D. Structure of the 5th transmembrane segment of the Na,K-ATPase a subunit: a cysteine-scanning mutagenesis study. FEBS Lett 2000, 482:144-148.
    • (2000) FEBS Lett , vol.482 , pp. 144-148
    • Guennoun, S.1    Horisberger, J.-D.2
  • 206
    • 0024470756 scopus 로고
    • +-ATPase
    • +-ATPase. Toxicon 1989, 27:1171-1187.
    • (1989) Toxicon , vol.27 , pp. 1171-1187
    • Habermann, E.1
  • 207
    • 0025821399 scopus 로고
    • Identification and characterization of a ouabainlike compound from human plasma
    • Hamlyn J.M., Blaustein M.P., Bova S., et al. Identification and characterization of a ouabainlike compound from human plasma. Proc Natl Acad Sci U S A 1991, 88:6259-6263.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 6259-6263
    • Hamlyn, J.M.1    Blaustein, M.P.2    Bova, S.3
  • 208
    • 0027077508 scopus 로고
    • Ouabain, digitalis-like factors and hypertension
    • Hamlyn J.M., Manunta P. Ouabain, digitalis-like factors and hypertension. J Hypertens 1992, 10(Suppl 7):S99-S111.
    • (1992) J Hypertens , vol.10 , Issue.SUPPL.7
    • Hamlyn, J.M.1    Manunta, P.2
  • 209
    • 0026745559 scopus 로고
    • Heterogeneity of Na,K-ATPase from kidney
    • Hansen O. Heterogeneity of Na,K-ATPase from kidney. Acta Physiol Scand 1992, 146:229-234.
    • (1992) Acta Physiol Scand , vol.146 , pp. 229-234
    • Hansen, O.1
  • 211
    • 0038579601 scopus 로고    scopus 로고
    • Renal Na,K-ATPase structure from cryo-electron microscopy of two-dimensional crystals
    • Hebert H., Purhonen P., Thomsen K., Vorum H., Maunsbach A.B. Renal Na,K-ATPase structure from cryo-electron microscopy of two-dimensional crystals. Ann N Y Acad Sci 2003, 986:9-16.
    • (2003) Ann N Y Acad Sci , vol.986 , pp. 9-16
    • Hebert, H.1    Purhonen, P.2    Thomsen, K.3    Vorum, H.4    Maunsbach, A.B.5
  • 213
    • 0028888879 scopus 로고
    • Gastric acid secretion
    • Hersey S.J., Sachs G. Gastric acid secretion. Physiol Rev 1995, 75:155-189.
    • (1995) Physiol Rev , vol.75 , pp. 155-189
    • Hersey, S.J.1    Sachs, G.2
  • 214
    • 0038442766 scopus 로고    scopus 로고
    • ATP-induced conformational changes of the nucleotide-binding domain of Na,K-ATPase
    • Hilge M., Siegal G., Vuister G.W., et al. ATP-induced conformational changes of the nucleotide-binding domain of Na,K-ATPase. Nat Struct Biol 2003, 10:468-474.
    • (2003) Nat Struct Biol , vol.10 , pp. 468-474
    • Hilge, M.1    Siegal, G.2    Vuister, G.W.3
  • 215
    • 0030910142 scopus 로고    scopus 로고
    • ATP compartmentation in human erythrocytes
    • Hoffman J.F. ATP compartmentation in human erythrocytes. Curr Opin Hematol 1997, 4:112-115.
    • (1997) Curr Opin Hematol , vol.4 , pp. 112-115
    • Hoffman, J.F.1
  • 216
    • 10444275509 scopus 로고    scopus 로고
    • Recent insights into the structure and mechanism of the sodium pump
    • Horisberger J.-D. Recent insights into the structure and mechanism of the sodium pump. Physiology 2004, 19:377-387.
    • (2004) Physiology , vol.19 , pp. 377-387
    • Horisberger, J.-D.1
  • 218
    • 0026014462 scopus 로고
    • Coexpression of a1 with putative b3 subunits results in functional Na-K-pumps in Xenopus oocyte
    • Horisberger J.-D., Jaunin P., Good P.J., Rossier B.C., Geering K. Coexpression of a1 with putative b3 subunits results in functional Na-K-pumps in Xenopus oocyte. Proc Natl Acad Sci U S A 1991, 88:8397-8400.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 8397-8400
    • Horisberger, J.-D.1    Jaunin, P.2    Good, P.J.3    Rossier, B.C.4    Geering, K.5
  • 219
    • 0037088857 scopus 로고    scopus 로고
    • Functional differences between a subunit isoforms of the rat Na,K-ATPase expressed in Xenopus oocytes
    • Horisberger J.-D., Kharoubi-Hess S. Functional differences between a subunit isoforms of the rat Na,K-ATPase expressed in Xenopus oocytes. J Physiol (London) 2002, 539:669-680.
    • (2002) J Physiol (London) , vol.539 , pp. 669-680
    • Horisberger, J.-D.1    Kharoubi-Hess, S.2
  • 220
    • 0025183069 scopus 로고
    • Differential regulation of Na, K-ATPase alpha 1, alpha 2, and beta subunit mRNA and protein levels by thyroid hormone
    • Horowitz B., Hensley C.B., Quintero M., et al. Differential regulation of Na, K-ATPase alpha 1, alpha 2, and beta subunit mRNA and protein levels by thyroid hormone. J Biol Chem 1990, 265:14308-14314.
    • (1990) J Biol Chem , vol.265 , pp. 14308-14314
    • Horowitz, B.1    Hensley, C.B.2    Quintero, M.3
  • 222
    • 0020686646 scopus 로고
    • Role for intrarenal mechanisms in the impaired salt excretion of experimental nephrotic syndrome
    • Ichikawa I., Rennke H.G., Hoyer J.R., et al. Role for intrarenal mechanisms in the impaired salt excretion of experimental nephrotic syndrome. J Clin Invest 1983, 71:91-103.
    • (1983) J Clin Invest , vol.71 , pp. 91-103
    • Ichikawa, I.1    Rennke, H.G.2    Hoyer, J.R.3
  • 224
    • 0030909776 scopus 로고    scopus 로고
    • Developmental changes of fetal rat lung Na-K-ATPase after maternal treatment with dexamethasone
    • Ingbar D.H., Duvick S., Savick S.K., et al. Developmental changes of fetal rat lung Na-K-ATPase after maternal treatment with dexamethasone. Am J Physiol Lung Cell Mol Physiol 1997, 16:L665-L672.
    • (1997) Am J Physiol Lung Cell Mol Physiol , vol.16
    • Ingbar, D.H.1    Duvick, S.2    Savick, S.K.3
  • 225
    • 0027444602 scopus 로고
    • A putative H,K-ATPase is selectively expressed in surface epithelial cells of rat distal colon
    • Jaisser F., Coutry N., Farman N., Binder H.J., Rossier B.C. A putative H,K-ATPase is selectively expressed in surface epithelial cells of rat distal colon. Am J Physiol 1993, 265:C1080-C1089.
    • (1993) Am J Physiol , vol.265
    • Jaisser, F.1    Coutry, N.2    Farman, N.3    Binder, H.J.4    Rossier, B.C.5
  • 228
    • 0027759874 scopus 로고
    • Primary sequence and functional expression of a novel b subunit of the P-ATPase gene family
    • Jaisser F., Horisberger J.-D., Rossier B.C. Primary sequence and functional expression of a novel b subunit of the P-ATPase gene family. Pflügers Arch 1993, 425:446-452.
    • (1993) Pflügers Arch , vol.425 , pp. 446-452
    • Jaisser, F.1    Horisberger, J.-D.2    Rossier, B.C.3
  • 230
    • 0032997363 scopus 로고    scopus 로고
    • Identification of a specific role for the Na,K-ATPase alpha 2 isoform as a regulator of calcium in the heart
    • James P.F., Grupp I.L., Grupp G., et al. Identification of a specific role for the Na,K-ATPase alpha 2 isoform as a regulator of calcium in the heart. Mol Cell 1999, 3:555-563.
    • (1999) Mol Cell , vol.3 , pp. 555-563
    • James, P.F.1    Grupp, I.L.2    Grupp, G.3
  • 231
    • 0027749257 scopus 로고
    • Role of the transmembrane and extracytoplasmic domain of b-subunits in subunit assembly, intracellular transport and functional expression of Na,K-pumps
    • Jaunin P., Jaisser F., Beggah A.T., et al. Role of the transmembrane and extracytoplasmic domain of b-subunits in subunit assembly, intracellular transport and functional expression of Na,K-pumps. J Cell Biol 1993, 123:1751-1759.
    • (1993) J Cell Biol , vol.123 , pp. 1751-1759
    • Jaunin, P.1    Jaisser, F.2    Beggah, A.T.3
  • 232
    • 0026014141 scopus 로고
    • Comparison of the substrate dependence properties of the rat Na, K-ATPase a1, a2, and a3 isoforms expressed in HeLa cells
    • Jewell E.A., Lingrel J.B. Comparison of the substrate dependence properties of the rat Na, K-ATPase a1, a2, and a3 isoforms expressed in HeLa cells. J Biol Chem 1991, 266:16925-16930.
    • (1991) J Biol Chem , vol.266 , pp. 16925-16930
    • Jewell, E.A.1    Lingrel, J.B.2
  • 233
    • 0027728991 scopus 로고
    • Site-directed mutagenesis of the Na,K-ATPase: consequences of substitutions of negatively-charged amino acids localized in the transmembrane domains
    • Jewell-Motz E.A., Lingrel J.B. Site-directed mutagenesis of the Na,K-ATPase: consequences of substitutions of negatively-charged amino acids localized in the transmembrane domains. Biochemistry 1993, 32:13523-13530.
    • (1993) Biochemistry , vol.32 , pp. 13523-13530
    • Jewell-Motz, E.A.1    Lingrel, J.B.2
  • 234
    • 20144383961 scopus 로고    scopus 로고
    • Hypertrophy, increased ejection fraction, and reduced Na-K-ATPase activity in phospholemman-deficient mice
    • Jia L.G., Donnet C., Bogaev R.C., et al. Hypertrophy, increased ejection fraction, and reduced Na-K-ATPase activity in phospholemman-deficient mice. Am J Physiol Heart Circ Physiol 2005, 288:H1982-H1988.
    • (2005) Am J Physiol Heart Circ Physiol , vol.288
    • Jia, L.G.1    Donnet, C.2    Bogaev, R.C.3
  • 236
    • 0019303902 scopus 로고
    • Sodium and potassium ion pump in kidney tubules
    • Jorgensen P.L. Sodium and potassium ion pump in kidney tubules. Physiol Rev 1980, 60:864-917.
    • (1980) Physiol Rev , vol.60 , pp. 864-917
    • Jorgensen, P.L.1
  • 237
    • 0026478846 scopus 로고
    • Regulation of Na,K-ATPase gene expression by thyroid hormone in rat cardiocytes
    • Kamitani T., Ikeda U., Muto S., et al. Regulation of Na,K-ATPase gene expression by thyroid hormone in rat cardiocytes. Circ Res 1992, 71:1457-1464.
    • (1992) Circ Res , vol.71 , pp. 1457-1464
    • Kamitani, T.1    Ikeda, U.2    Muto, S.3
  • 238
    • 0027339323 scopus 로고
    • 831 of the a chain of Na/K-ATPase at the cytoplasmic surface. Implication for topological models
    • 831 of the a chain of Na/K-ATPase at the cytoplasmic surface. Implication for topological models. J Biol Chem 1993, 268:3471-3478.
    • (1993) J Biol Chem , vol.268 , pp. 3471-3478
    • Karlish, S.J.D.1    Goldshleger, R.2    Jorgensen, P.L.3
  • 239
    • 0025367761 scopus 로고
    • A 19-kDa C-terminal tryptic fragment of the a chain of Na/K-ATPase is essential for occlusion and transport of cations
    • Karlish S.J.D., Goldshleger R., Stein W.D. A 19-kDa C-terminal tryptic fragment of the a chain of Na/K-ATPase is essential for occlusion and transport of cations. Proc Natl Acad Sci U S A 1990, 87:4566-4570.
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 4566-4570
    • Karlish, S.J.D.1    Goldshleger, R.2    Stein, W.D.3
  • 240
    • 0022399724 scopus 로고
    • Monoclonal antibody to Na-K-ATPase: immunocytochemical localization along nephron segments
    • Kashgarian M., Biemesderfer D., Caplan M., Forbush B. Monoclonal antibody to Na-K-ATPase: immunocytochemical localization along nephron segments. Kidney Int 1985, 28:899-913.
    • (1985) Kidney Int , vol.28 , pp. 899-913
    • Kashgarian, M.1    Biemesderfer, D.2    Caplan, M.3    Forbush, B.4
  • 241
    • 0018507998 scopus 로고
    • Na-K-ATPase activity along the rabbit, rat, and mouse nephron
    • Katz A.I., Doucet A., Morel F. Na-K-ATPase activity along the rabbit, rat, and mouse nephron. Am J Physiol 1979, 237:114-120.
    • (1979) Am J Physiol , vol.237 , pp. 114-120
    • Katz, A.I.1    Doucet, A.2    Morel, F.3
  • 242
    • 0014189489 scopus 로고
    • The role of sodium-potassium-activated adenosine triphosphatase in the reabsorption of sodium by the kidney
    • Katz A.I., Epstein F.H. The role of sodium-potassium-activated adenosine triphosphatase in the reabsorption of sodium by the kidney. J Clin Invest 1967, 46:1999-2011.
    • (1967) J Clin Invest , vol.46 , pp. 1999-2011
    • Katz, A.I.1    Epstein, F.H.2
  • 243
    • 0038730346 scopus 로고    scopus 로고
    • Proton translocation driven by ATP hydrolysis in V-ATPases
    • Kawasaki-Nishi S., Nishi T., Forgac M. Proton translocation driven by ATP hydrolysis in V-ATPases. FEBS Lett 2003, 545:76-85.
    • (2003) FEBS Lett , vol.545 , pp. 76-85
    • Kawasaki-Nishi, S.1    Nishi, T.2    Forgac, M.3
  • 244
    • 2342418859 scopus 로고    scopus 로고
    • +-ATPase in response to parathyroid hormone requires ERK-dependent phosphorylation of Ser-11 within the alpha(1)-subunit
    • +-ATPase in response to parathyroid hormone requires ERK-dependent phosphorylation of Ser-11 within the alpha(1)-subunit. J Biol Chem 2004, 279:17418-17427.
    • (2004) J Biol Chem , vol.279 , pp. 17418-17427
    • Khundmiri, S.J.1    Bertorello, A.M.2    Delamere, N.A.3    Lederer, E.D.4
  • 245
    • 1942535177 scopus 로고    scopus 로고
    • Increased expression and apical targeting of renal ENaC subunits in puromycin aminonucleoside-induced nephrotic syndrome in rats
    • Kim S.W., Wang W.D., Nielsen J., et al. Increased expression and apical targeting of renal ENaC subunits in puromycin aminonucleoside-induced nephrotic syndrome in rats. Am J Physiol Renal Physiol 2004, 286:F922-F935.
    • (2004) Am J Physiol Renal Physiol , vol.286
    • Kim, S.W.1    Wang, W.D.2    Nielsen, J.3
  • 248
    • 0027291366 scopus 로고
    • Functional expression of gastric H, K-ATPase using the baculovirus expression system
    • Klaassen C.H.W., Van Uem T.J.F., De Moel M.P., et al. Functional expression of gastric H, K-ATPase using the baculovirus expression system. FEBS Lett 1993, 329:277-282.
    • (1993) FEBS Lett , vol.329 , pp. 277-282
    • Klaassen, C.H.W.1    Van, U.T.J.F.2    De, M.M.P.3
  • 252
    • 0030799007 scopus 로고    scopus 로고
    • Effect of hypokalemia on the abundance of HK alpha 1 and HK alpha 2 protein in the rat kidney
    • Kraut J.A., Hiura J., Besancon M., et al. Effect of hypokalemia on the abundance of HK alpha 1 and HK alpha 2 protein in the rat kidney. Am J Physiol 1997, 272:F744-F750.
    • (1997) Am J Physiol , vol.272
    • Kraut, J.A.1    Hiura, J.2    Besancon, M.3
  • 255
    • 0029658484 scopus 로고    scopus 로고
    • Asp(804) and asp(808) in the transmembrane domain of the Na,K-ATPase alpha subunit are cation coordinating residues
    • Kuntzweiler T.A., Argüello J.M., Lingrel J.B. Asp(804) and asp(808) in the transmembrane domain of the Na,K-ATPase alpha subunit are cation coordinating residues. J Biol Chem 1996, 271:29682-29687.
    • (1996) J Biol Chem , vol.271 , pp. 29682-29687
    • Kuntzweiler, T.A.1    Argüello, J.M.2    Lingrel, J.B.3
  • 257
    • 0030763913 scopus 로고    scopus 로고
    • Regulation of a c-Jun amino-terminal kinase/stress-activated protein kinase cascade by a sodium-dependent signal transduction pathway
    • Kuroki D.W., Minden A., Sanchez I., Wattenberg E.V. Regulation of a c-Jun amino-terminal kinase/stress-activated protein kinase cascade by a sodium-dependent signal transduction pathway. J Biol Chem 1997, 272:23905-23911.
    • (1997) J Biol Chem , vol.272 , pp. 23905-23911
    • Kuroki, D.W.1    Minden, A.2    Sanchez, I.3    Wattenberg, E.V.4
  • 258
    • 0034674066 scopus 로고    scopus 로고
    • A new variant of the gamma subunit of renal Na,KATPase- identification by mass spectrometry, antibody binding, and expression in cultured cells
    • Kuster B., Shainskaya A., Pu H.X., et al. A new variant of the gamma subunit of renal Na,KATPase- identification by mass spectrometry, antibody binding, and expression in cultured cells. J Biol Chem 2000, 275:18441-18446.
    • (2000) J Biol Chem , vol.275 , pp. 18441-18446
    • Kuster, B.1    Shainskaya, A.2    Pu, H.X.3
  • 263
    • 0037166283 scopus 로고    scopus 로고
    • Protein kinase A- independent activation of ERK and H,K-ATPase by cAMP in native kidney cells-role of Epac I
    • Laroche-Joubert N., Marsy S., Michelet S., Imbert-Teboul M., Doucet A. Protein kinase A- independent activation of ERK and H,K-ATPase by cAMP in native kidney cells-role of Epac I. J Biol Chem 2002, 277:18598-18604.
    • (2002) J Biol Chem , vol.277 , pp. 18598-18604
    • Laroche-Joubert, N.1    Marsy, S.2    Michelet, S.3    Imbert-Teboul, M.4    Doucet, A.5
  • 264
    • 0018799006 scopus 로고
    • A channel mechanism for electrogenic ion pumps
    • Läuger P. A channel mechanism for electrogenic ion pumps. Biochim Biophys Acta 1979, 552:143-161.
    • (1979) Biochim Biophys Acta , vol.552 , pp. 143-161
    • Läuger, P.1
  • 265
    • 0028786344 scopus 로고
    • Functional expression and segmental localization of rat colonic K-adenosine triphosphatase
    • Lee J.S., Rajendran V.M., Mann A.S., Kashgarian M., Binder H.J. Functional expression and segmental localization of rat colonic K-adenosine triphosphatase. J Clin Invest 1995, 96:2002-2008.
    • (1995) J Clin Invest , vol.96 , pp. 2002-2008
    • Lee, J.S.1    Rajendran, V.M.2    Mann, A.S.3    Kashgarian, M.4    Binder, H.J.5
  • 266
    • 0027320842 scopus 로고
    • Dietary sodium stimulates ouabainlike activity in adrenalectomized spontaneously hypertensive rats
    • Leenen F.H.H., Harmsen E., Yu H., Yuan B. Dietary sodium stimulates ouabainlike activity in adrenalectomized spontaneously hypertensive rats. Am J Physiol Heart Circ Physiol 1993, 265:H421-H424.
    • (1993) Am J Physiol Heart Circ Physiol , vol.265
    • Leenen, F.H.H.1    Harmsen, E.2    Yu, H.3    Yuan, B.4
  • 267
    • 0028289934 scopus 로고
    • 26 amino acids of an extracellular domain of the Na,K-ATPase a-subunit are sufficient for assembly with the Na,K-ATPase b-subunit
    • Lemas M.V., Hamrick M., Takeyasu K., Fambrough D.M. 26 amino acids of an extracellular domain of the Na,K-ATPase a-subunit are sufficient for assembly with the Na,K-ATPase b-subunit. J Biol Chem 1994, 269:8255-8259.
    • (1994) J Biol Chem , vol.269 , pp. 8255-8259
    • Lemas, M.V.1    Hamrick, M.2    Takeyasu, K.3    Fambrough, D.M.4
  • 268
    • 0028352750 scopus 로고
    • Assembly of Na,K-ATPase asubunit isoforms with Na,K-ATPase b-subunit isoforms and H,K-ATPase b-subunit
    • Lemas M.V., Yu H.-Y., Takeyasu K., Kone B., Fambrough D.M. Assembly of Na,K-ATPase asubunit isoforms with Na,K-ATPase b-subunit isoforms and H,K-ATPase b-subunit. J Biol Chem 1994, 269:18651-18655.
    • (1994) J Biol Chem , vol.269 , pp. 18651-18655
    • Lemas, M.V.1    Yu, H.-Y.2    Takeyasu, K.3    Kone, B.4    Fambrough, D.M.5
  • 271
    • 0026636168 scopus 로고
    • Na,K-ATPase: Isoform structure, function, and expression
    • Lingrel J.B. Na,K-ATPase: Isoform structure, function, and expression. J Bioenerg Biomembr 1992, 24:263-270.
    • (1992) J Bioenerg Biomembr , vol.24 , pp. 263-270
    • Lingrel, J.B.1
  • 273
    • 0027953639 scopus 로고
    • Structure-function studies of the Na,K-ATPase
    • Lingrel J.B., Van Huysse J., O'Brien W., et al. Structure-function studies of the Na,K-ATPase. Kidney Int Suppl 1994, 44:S32-S39.
    • (1994) Kidney Int Suppl , vol.44
    • Lingrel, J.B.1    Van, H.J.2    O'Brien, W.3
  • 274
    • 0029781307 scopus 로고    scopus 로고
    • Na-k-ATPase isoform (alpha3, alpha2, alpha1) abundance in rat kidney estimated by competitive rt-PCR and ouabain binding
    • Lucking K., Nielsen J.M., Pedersen P.A., Jorgensen P.L. Na-k-ATPase isoform (alpha3, alpha2, alpha1) abundance in rat kidney estimated by competitive rt-PCR and ouabain binding. Am J Physiol Renal Fluid Electrolyte Physiol 1996, 40:F253-F260.
    • (1996) Am J Physiol Renal Fluid Electrolyte Physiol , vol.40
    • Lucking, K.1    Nielsen, J.M.2    Pedersen, P.A.3    Jorgensen, P.L.4
  • 275
    • 0026576613 scopus 로고
    • Rat adrenal cortex is a source of a circulating ouabainlike compound
    • Ludens J.H., Clark M.A., Robinson F.G., DuCharme D.W. Rat adrenal cortex is a source of a circulating ouabainlike compound. Hypertension 1992, 19:721-724.
    • (1992) Hypertension , vol.19 , pp. 721-724
    • Ludens, J.H.1    Clark, M.A.2    Robinson, F.G.3    DuCharme, D.W.4
  • 276
    • 84882921905 scopus 로고    scopus 로고
    • The multifaceted role of the N-terminal domain in regulation of the Wilson's disease protein (WNDP), a human copper-transporting ATPase
    • Lutsenko S., Tsivkovskii R., Walker J.M., Cooper M.J. The multifaceted role of the N-terminal domain in regulation of the Wilson's disease protein (WNDP), a human copper-transporting ATPase. FASEB J 2002, 16:A462.
    • (2002) FASEB J , vol.16
    • Lutsenko, S.1    Tsivkovskii, R.2    Walker, J.M.3    Cooper, M.J.4
  • 278
    • 0038464639 scopus 로고    scopus 로고
    • Phospholamban: a crucial regulator of cardiac contractility
    • Maclennan D.H., Kranias E.G. Phospholamban: a crucial regulator of cardiac contractility. Nature Rev Mol Cell Biol 2003, 4:566-577.
    • (2003) Nature Rev Mol Cell Biol , vol.4 , pp. 566-577
    • Maclennan, D.H.1    Kranias, E.G.2
  • 284
    • 0024521531 scopus 로고
    • Identification of a putative isoform of the Na,K-ATPase b subunit. Primary structure and tissue-specific expression
    • Martin-Vasallo P., Dackowski W., Emanuel J.R., Levenson R. Identification of a putative isoform of the Na,K-ATPase b subunit. Primary structure and tissue-specific expression. J Biol Chem 1989, 264:4613-4618.
    • (1989) J Biol Chem , vol.264 , pp. 4613-4618
    • Martin-Vasallo, P.1    Dackowski, W.2    Emanuel, J.R.3    Levenson, R.4
  • 286
    • 0025305262 scopus 로고
    • The sodium pump needs its b subunit
    • McDonough A.A., Geering K., Farley R.A. The sodium pump needs its b subunit. FASEB J 1990, 4:1598-1605.
    • (1990) FASEB J , vol.4 , pp. 1598-1605
    • McDonough, A.A.1    Geering, K.2    Farley, R.A.3
  • 287
    • 0028119627 scopus 로고
    • +-ATPase a- and b-subunits along rat nephron: isoform specificity and response to hypokalemia
    • +-ATPase a- and b-subunits along rat nephron: isoform specificity and response to hypokalemia. Am J Physiol Cell Physiol 1994, 267:C901-C908.
    • (1994) Am J Physiol Cell Physiol , vol.267
    • McDonough, A.A.1    Magyar, C.E.2    Komatsu, Y.3
  • 290
    • 0027281005 scopus 로고
    • Molecular cloning and immunological characterization of the gamma polypeptide, a small protein associated with the Na,K-ATPase
    • Mercer R.W., Biemesderfer D., Bliss D.P., Collins J.H., Forbush B3. Molecular cloning and immunological characterization of the gamma polypeptide, a small protein associated with the Na,K-ATPase. J Cell Biol 1993, 121:579-586.
    • (1993) J Cell Biol , vol.121 , pp. 579-586
    • Mercer, R.W.1    Biemesderfer, D.2    Bliss, D.P.3    Collins, J.H.4    Forbush, B.5
  • 291
    • 10944229752 scopus 로고    scopus 로고
    • ERK1/2 controls Na,K-ATPase activity and transepithelial sodium transport in the principal cell of the cortical collecting duct of the mouse kidney
    • Michlig S., Mercier A., Doucet A., et al. ERK1/2 controls Na,K-ATPase activity and transepithelial sodium transport in the principal cell of the cortical collecting duct of the mouse kidney. J Biol Chem 2004, 279:51002-51012.
    • (2004) J Biol Chem , vol.279 , pp. 51002-51012
    • Michlig, S.1    Mercier, A.2    Doucet, A.3
  • 292
    • 0030805996 scopus 로고    scopus 로고
    • Intracellular pH regulation in the rabbit cortical collecting duct a-type intercalated cell
    • Milton A.E., Weiner I.D. Intracellular pH regulation in the rabbit cortical collecting duct a-type intercalated cell. Am J Physiol Renal Fluid Electrolyte Physiol 1997, 42:F340-F347.
    • (1997) Am J Physiol Renal Fluid Electrolyte Physiol , vol.42
    • Milton, A.E.1    Weiner, I.D.2
  • 295
    • 0029940235 scopus 로고    scopus 로고
    • Structural organization, ion transport, and energy transduction of ATPases
    • Moller J.V., Juul B., Lemaire M. Structural organization, ion transport, and energy transduction of ATPases. Biochim Biophys Acta 1996, 1286:1-51.
    • (1996) Biochim Biophys Acta , vol.1286 , pp. 1-51
    • Moller, J.V.1    Juul, B.2    Lemaire, M.3
  • 297
    • 0022521184 scopus 로고
    • Hormonal control of kidney functions at the cell level
    • Morel F., Doucet A. Hormonal control of kidney functions at the cell level. Physiol Rev 1986, 66:377-468.
    • (1986) Physiol Rev , vol.66 , pp. 377-468
    • Morel, F.1    Doucet, A.2
  • 298
    • 0028952569 scopus 로고
    • Mat-8, a novel phospholemman-like protein expressed in human breast-tumors, induces a chloride conductance in Xenopus oocytes
    • Morrison B.W., Moorman J.R., Kowdley G.C., et al. Mat-8, a novel phospholemman-like protein expressed in human breast-tumors, induces a chloride conductance in Xenopus oocytes. J Biol Chem 1995, 270:2176-2182.
    • (1995) J Biol Chem , vol.270 , pp. 2176-2182
    • Morrison, B.W.1    Moorman, J.R.2    Kowdley, G.C.3
  • 299
    • 20644462617 scopus 로고    scopus 로고
    • Genetic profiling reveals global changes in multiple biological pathways in the hearts of Na,K-ATPase alpha 1 isoform haplo-insufficient mice
    • Moseley A.E., Huddleson J.P., Bohanan C.S., et al. Genetic profiling reveals global changes in multiple biological pathways in the hearts of Na,K-ATPase alpha 1 isoform haplo-insufficient mice. Cell Physiol Biochem 2005, 15:145-158.
    • (2005) Cell Physiol Biochem , vol.15 , pp. 145-158
    • Moseley, A.E.1    Huddleson, J.P.2    Bohanan, C.S.3
  • 300
    • 0037687290 scopus 로고    scopus 로고
    • The Na,K-ATPase alpha 2 isoform is expressed in neurons, and its absence disrupts neuronal activity in newborn mice
    • Moseley A.E., Lieske S.P., Wetzel R.K., et al. The Na,K-ATPase alpha 2 isoform is expressed in neurons, and its absence disrupts neuronal activity in newborn mice. J Biol Chem 2003, 278:5317-5324.
    • (2003) J Biol Chem , vol.278 , pp. 5317-5324
    • Moseley, A.E.1    Lieske, S.P.2    Wetzel, R.K.3
  • 301
    • 0022362904 scopus 로고
    • Modulation of renal sodiumpotassium-adenosine triphosphatase by aldosterone
    • Mujais S.K., Chekai A., Jones W.J., Hayslett J.P., Katz A.I. Modulation of renal sodiumpotassium-adenosine triphosphatase by aldosterone. J Clin Invest 1985, 76:170-176.
    • (1985) J Clin Invest , vol.76 , pp. 170-176
    • Mujais, S.K.1    Chekai, A.2    Jones, W.J.3    Hayslett, J.P.4    Katz, A.I.5
  • 302
    • 0021362422 scopus 로고
    • Regulation of renal Na-K-ATPase in the rat.Role of the natural mineralo- and gluco-corticoid hormones
    • Mujais S.K., Chekal M.A., Jones W.J., Hayslett J.P., Katz A.I. Regulation of renal Na-K-ATPase in the rat.Role of the natural mineralo- and gluco-corticoid hormones. J Clin Invest 1984, 73:13-19.
    • (1984) J Clin Invest , vol.73 , pp. 13-19
    • Mujais, S.K.1    Chekal, M.A.2    Jones, W.J.3    Hayslett, J.P.4    Katz, A.I.5
  • 303
    • 0021185702 scopus 로고
    • Relationship between adrenal steroids and renal Na-K-ATPase
    • Mujais S.K., Chekal M.A., Lee S.-M., Katz A.I. Relationship between adrenal steroids and renal Na-K-ATPase. Pflügers Arch 1984, 402:48-51.
    • (1984) Pflügers Arch , vol.402 , pp. 48-51
    • Mujais, S.K.1    Chekal, M.A.2    Lee, S.-M.3    Katz, A.I.4
  • 304
    • 0026176015 scopus 로고
    • Effects of apical vs basolateral palytoxin on LLC-PK1 renal epithelia
    • Mullin J.M., Snock K.V., McGinn M.T. Effects of apical vs basolateral palytoxin on LLC-PK1 renal epithelia. Am J Physiol Cell Physiol 1991, 260:C1201-C1211.
    • (1991) Am J Physiol Cell Physiol , vol.260
    • Mullin, J.M.1    Snock, K.V.2    McGinn, M.T.3
  • 305
    • 16844381593 scopus 로고    scopus 로고
    • Inhibitor and ion binding sites on the gastric H,K-ATPase
    • Munson K., Garcia R., Sachs G. Inhibitor and ion binding sites on the gastric H,K-ATPase. Biochemistry 2005, 44:5267-5284.
    • (2005) Biochemistry , vol.44 , pp. 5267-5284
    • Munson, K.1    Garcia, R.2    Sachs, G.3
  • 307
    • 0022471974 scopus 로고
    • Voltage dependence of the Na translocation by the Na/K pump
    • Nakao M., Gadsby D.C. Voltage dependence of the Na translocation by the Na/K pump. Nature 1986, 323:628-630.
    • (1986) Nature , vol.323 , pp. 628-630
    • Nakao, M.1    Gadsby, D.C.2
  • 310
    • 0021809938 scopus 로고
    • Sodium-dependent modulation of the renal Na-K-ATPase: influence of mineralocorticoids on the cortical collecting duct
    • O'Neil R.G., Hayhurst R.A. Sodium-dependent modulation of the renal Na-K-ATPase: influence of mineralocorticoids on the cortical collecting duct. J Membr Biol 1986, 85:169-179.
    • (1986) J Membr Biol , vol.85 , pp. 169-179
    • O'Neil, R.G.1    Hayhurst, R.A.2
  • 312
  • 314
    • 0029768938 scopus 로고    scopus 로고
    • Regulation of Na-K-ATPase activity in the proximal tubule-role of the protein kinase c pathway and of eicosanoids
    • Ominato M., Satoh T., Katz A.I. Regulation of Na-K-ATPase activity in the proximal tubule-role of the protein kinase c pathway and of eicosanoids. J Membr Biol 1996, 152:235-243.
    • (1996) J Membr Biol , vol.152 , pp. 235-243
    • Ominato, M.1    Satoh, T.2    Katz, A.I.3
  • 316
    • 0025215465 scopus 로고
    • Thyroid and glucocorticoid hormones regulate the expression of multiple Na,K-ATPase genes in cultured neonatal rat cardiac myocytes
    • Orlowski J., Lingrel J.B. Thyroid and glucocorticoid hormones regulate the expression of multiple Na,K-ATPase genes in cultured neonatal rat cardiac myocytes. J Biol Chem 1990, 265:3462-3470.
    • (1990) J Biol Chem , vol.265 , pp. 3462-3470
    • Orlowski, J.1    Lingrel, J.B.2
  • 318
    • 12144251755 scopus 로고    scopus 로고
    • Interactions between cardiac glycosides and sodium/potassium-ATPase: three-dimensional structure-activity relationship models for ligand binding to the E-2-P-i form of the enzyme versus activity inhibition
    • Paula S., Tabet M.R., Ball W.J. Interactions between cardiac glycosides and sodium/potassium-ATPase: three-dimensional structure-activity relationship models for ligand binding to the E-2-P-i form of the enzyme versus activity inhibition. Biochemistry 2005, 44:498-510.
    • (2005) Biochemistry , vol.44 , pp. 498-510
    • Paula, S.1    Tabet, M.R.2    Ball, W.J.3
  • 321
    • 0030456587 scopus 로고    scopus 로고
    • Consequences of mutations to the phosphorylation site of the alpha-subunit of Na,K-atpase for ATP binding and E(1)-E(2) conformational equilibrium
    • Pedersen P.A., Rasmussen J.H., Jorgensen P.L. Consequences of mutations to the phosphorylation site of the alpha-subunit of Na,K-atpase for ATP binding and E(1)-E(2) conformational equilibrium. Biochemistry 1996, 35:16085-16093.
    • (1996) Biochemistry , vol.35 , pp. 16085-16093
    • Pedersen, P.A.1    Rasmussen, J.H.2    Jorgensen, P.L.3
  • 323
    • 0026630558 scopus 로고
    • Low affinity superphosphorylation of the Na,K-ATPase by ATP
    • Peluffo R.D., Garrahan P.J., Rega A.F. Low affinity superphosphorylation of the Na,K-ATPase by ATP. J Biol Chem 1992, 267:6596-6601.
    • (1992) J Biol Chem , vol.267 , pp. 6596-6601
    • Peluffo, R.D.1    Garrahan, P.J.2    Rega, A.F.3
  • 324
    • 0030908069 scopus 로고    scopus 로고
    • Isoforms of Na,K-ATPase alpha and beta subunits in the rat cerebellum and in granule cell cultures
    • Peng L., Martin-Vasallo P., Sweadner K.J. Isoforms of Na,K-ATPase alpha and beta subunits in the rat cerebellum and in granule cell cultures. J Neurosci 1997, 17:3488-3502.
    • (1997) J Neurosci , vol.17 , pp. 3488-3502
    • Peng, L.1    Martin-Vasallo, P.2    Sweadner, K.J.3
  • 325
    • 2442432400 scopus 로고    scopus 로고
    • Identification of the beta-subunit for nongastric H-K-ATPase in rat anterior prostate
    • Pestov N.B., Korneenko T.V., Radkov R., et al. Identification of the beta-subunit for nongastric H-K-ATPase in rat anterior prostate. Am J Physiol Cell Physiol 2004, 286:C1229-C1237.
    • (2004) Am J Physiol Cell Physiol , vol.286
    • Pestov, N.B.1    Korneenko, T.V.2    Radkov, R.3
  • 327
    • 0019790965 scopus 로고
    • Secondary effect of aldosterone on Na-K-ATPase activity in the rabbit cortical collecting tubule
    • Petty K.J., Kokko J.P., Marver D. Secondary effect of aldosterone on Na-K-ATPase activity in the rabbit cortical collecting tubule. J Clin Invest 1981, 68:1514-1521.
    • (1981) J Clin Invest , vol.68 , pp. 1514-1521
    • Petty, K.J.1    Kokko, J.P.2    Marver, D.3
  • 328
    • 15044353413 scopus 로고    scopus 로고
    • The gamma-subunit of Na-K-ATPase is incorporated into plasma membranes of mouse IMCD3 cells in response to hypertonicity
    • Pihakaski-Maunsbach K., Tokonabe S., Vorum H., et al. The gamma-subunit of Na-K-ATPase is incorporated into plasma membranes of mouse IMCD3 cells in response to hypertonicity. Am J Physiol Renal Physiol 2005, 288:F650-F657.
    • (2005) Am J Physiol Renal Physiol , vol.288
    • Pihakaski-Maunsbach, K.1    Tokonabe, S.2    Vorum, H.3
  • 329
    • 0037564507 scopus 로고    scopus 로고
    • Immunocytochemical localization of Na,K-ATPase gamma subunit and CHIF in inner medulla of rat kidney
    • Pihakaski-Maunsbach K., Vorum H., Locke E.M., et al. Immunocytochemical localization of Na,K-ATPase gamma subunit and CHIF in inner medulla of rat kidney. Ann N Y Acad Sci 2003, 986:401-409.
    • (2003) Ann N Y Acad Sci , vol.986 , pp. 401-409
    • Pihakaski-Maunsbach, K.1    Vorum, H.2    Locke, E.M.3
  • 330
    • 0023796964 scopus 로고
    • Protons as substitutes for sodium and potassium in the sodium pump reaction
    • Polvani C., Blostein R. Protons as substitutes for sodium and potassium in the sodium pump reaction. J Biol Chem 1988, 263:16757-16763.
    • (1988) J Biol Chem , vol.263 , pp. 16757-16763
    • Polvani, C.1    Blostein, R.2
  • 331
    • 0015523849 scopus 로고
    • Activation by adenosine triphosphate in the phosphorylation kinetics of sodium and potassium ion transport adenosine triphosphatase
    • Post R.L., Hegyvary C., Kume S. Activation by adenosine triphosphate in the phosphorylation kinetics of sodium and potassium ion transport adenosine triphosphatase. J Biol Chem 1972, 247:6530-6540.
    • (1972) J Biol Chem , vol.247 , pp. 6530-6540
    • Post, R.L.1    Hegyvary, C.2    Kume, S.3
  • 332
    • 0025211402 scopus 로고
    • Structure-function studies of Na,K-ATPase. Site-directed mutagenesis of the border residues from the H1-H2 extracellular domain of the a subunit
    • Price E.M., Rice D.A., Lingrel J.B. Structure-function studies of Na,K-ATPase. Site-directed mutagenesis of the border residues from the H1-H2 extracellular domain of the a subunit. J Biol Chem 1990, 265:6638-6641.
    • (1990) J Biol Chem , vol.265 , pp. 6638-6641
    • Price, E.M.1    Rice, D.A.2    Lingrel, J.B.3
  • 333
    • 0035827529 scopus 로고    scopus 로고
    • Functional role and immunocytochemical localization of the gamma(a) and gamma(b) forms of the Na,K-ATPase gamma subunit
    • Pu H.X., Cluzeaud F., Goldshleger R., et al. Functional role and immunocytochemical localization of the gamma(a) and gamma(b) forms of the Na,K-ATPase gamma subunit. J Biol Chem 2001, 276:20370-20378.
    • (2001) J Biol Chem , vol.276 , pp. 20370-20378
    • Pu, H.X.1    Cluzeaud, F.2    Goldshleger, R.3
  • 334
    • 0037036441 scopus 로고    scopus 로고
    • Distinct regulatory effects of the Na,K-ATPase gamma subunit
    • Pu H.X., Scanzano R., Blostein R. Distinct regulatory effects of the Na,K-ATPase gamma subunit. J Biol Chem 2002, 277:20270-20276.
    • (2002) J Biol Chem , vol.277 , pp. 20270-20276
    • Pu, H.X.1    Scanzano, R.2    Blostein, R.3
  • 336
    • 0025321011 scopus 로고
    • The mechanism and structure of the gastric H,K-ATPase
    • Rabon E.C., Reuben M.A. The mechanism and structure of the gastric H,K-ATPase. Annu Rev Physiol 1990, 52:321-344.
    • (1990) Annu Rev Physiol , vol.52 , pp. 321-344
    • Rabon, E.C.1    Reuben, M.A.2
  • 338
    • 0021431441 scopus 로고
    • +-ATPase: differential sensitivities along the nephron
    • +-ATPase: differential sensitivities along the nephron. Am J Physiol 1984, 246:F656-F662.
    • (1984) Am J Physiol , vol.246
    • Rayson, B.M.1    Lowther, S.O.2
  • 339
    • 0030070890 scopus 로고    scopus 로고
    • + influx into yeast cells expressing the mammalian sodium pump is due to the formation of a channel within the enzyme
    • + influx into yeast cells expressing the mammalian sodium pump is due to the formation of a channel within the enzyme. Mol Pharmacol 1996, 49:49-57.
    • (1996) Mol Pharmacol , vol.49 , pp. 49-57
    • Redondo, J.1    Fiedler, B.2    Scheiner-Bobis, G.3
  • 340
    • 0023278664 scopus 로고
    • Toxic effects of herbal teas
    • Ridker P.M. Toxic effects of herbal teas. Arch Environ Health 1987, 42:133-136.
    • (1987) Arch Environ Health , vol.42 , pp. 133-136
    • Ridker, P.M.1
  • 343
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali A., Blundell T.L. Comparative protein modelling by satisfaction of spatial restraints. J Mol Biol 1993, 234:779-815.
    • (1993) J Mol Biol , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 344
    • 0028084172 scopus 로고
    • Role of protein kinase C in insulin activation of the Na-K pump in cultured skeletal muscle
    • Sampson S.R., Brodie C., Alboim S.V. Role of protein kinase C in insulin activation of the Na-K pump in cultured skeletal muscle. Am J Physiol Cell Physiol 1994, 266:C751-C758.
    • (1994) Am J Physiol Cell Physiol , vol.266
    • Sampson, S.R.1    Brodie, C.2    Alboim, S.V.3
  • 345
    • 0032987164 scopus 로고    scopus 로고
    • Colonic H-K-ATPase b-subunit: identification in apical membranes and regulation by dietary K depletion
    • Sangan P., Kolla S.S., Rajendran V.M., Kashgarian M., Binder H.J. Colonic H-K-ATPase b-subunit: identification in apical membranes and regulation by dietary K depletion. Am J Physiol Cell Physiol 1999, 45:C350-C360.
    • (1999) Am J Physiol Cell Physiol , vol.45
    • Sangan, P.1    Kolla, S.S.2    Rajendran, V.M.3    Kashgarian, M.4    Binder, H.J.5
  • 347
    • 0030948553 scopus 로고    scopus 로고
    • Regulation of colonic H-K-ATPase in large intestine and kidney by dietary Na-depletion and dietary K depletion
    • Sangan P.C., Rajendran V.M., Mann A.S., Kashgarian M., Binder H.J. Regulation of colonic H-K-ATPase in large intestine and kidney by dietary Na-depletion and dietary K depletion. Am J Physiol Cell Physiol 1997, 41:C685-C696.
    • (1997) Am J Physiol Cell Physiol , vol.41
    • Sangan, P.C.1    Rajendran, V.M.2    Mann, A.S.3    Kashgarian, M.4    Binder, H.J.5
  • 348
    • 0027504676 scopus 로고
    • Different mechanism of renal Na,K-ATPase regulation by protein kinases in proximal and distal nephron
    • Satoh T., Cohen H.T., Katz A.I. Different mechanism of renal Na,K-ATPase regulation by protein kinases in proximal and distal nephron. Am J Physiol 1993, 265:F399-F405.
    • (1993) Am J Physiol , vol.265
    • Satoh, T.1    Cohen, H.T.2    Katz, A.I.3
  • 350
    • 0028016092 scopus 로고
    • Subunit requirements for expression of functional sodium pumps in yeast cells
    • Scheiner-Bobis G., Farley R.A. Subunit requirements for expression of functional sodium pumps in yeast cells. Biochim Biophys Acta 1994, 1193:226-234.
    • (1994) Biochim Biophys Acta , vol.1193 , pp. 226-234
    • Scheiner-Bobis, G.1    Farley, R.A.2
  • 352
    • 0031029915 scopus 로고    scopus 로고
    • Isoform-specific interactions of Na,K-ATPase subunits are mediated via extracellular domains and carbohydrates
    • Schmalzing G., Ruhl K., Gloor S.M. Isoform-specific interactions of Na,K-ATPase subunits are mediated via extracellular domains and carbohydrates. Proc Natl Acad Sci U S A 1997, 94:1136-1141.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 1136-1141
    • Schmalzing, G.1    Ruhl, K.2    Gloor, S.M.3
  • 353
    • 0014463549 scopus 로고
    • +)-stimulated adenosintriphosphatase in the rat nephron
    • +)-stimulated adenosintriphosphatase in the rat nephron. Pflügers Arch 1969, 306:219-226.
    • (1969) Pflügers Arch , vol.306 , pp. 219-226
    • Schmidt, U.1    Dubach, U.C.2
  • 354
    • 0027389899 scopus 로고
    • Substitution of transmembrane residues with hydrogen-bonding potential in the a subunit of Na,K-ATPase reveals alterations in ouabain sensitivity
    • Schultheis P.J., Lingrel J.B. Substitution of transmembrane residues with hydrogen-bonding potential in the a subunit of Na,K-ATPase reveals alterations in ouabain sensitivity. Biochemistry 1993, 32:544-550.
    • (1993) Biochemistry , vol.32 , pp. 544-550
    • Schultheis, P.J.1    Lingrel, J.B.2
  • 355
    • 0016302392 scopus 로고
    • Target-cell polarity and membrane phosphorylation in relation to mechanism of action of antidiuretic-hormone
    • Schwartz I.L., Shlatz L.J., Kinnesaf E., Kinne R. Target-cell polarity and membrane phosphorylation in relation to mechanism of action of antidiuretic-hormone. Proc Natl Acad Sci U S A 1974, 71:2595-2599.
    • (1974) Proc Natl Acad Sci U S A , vol.71 , pp. 2595-2599
    • Schwartz, I.L.1    Shlatz, L.J.2    Kinnesaf, E.3    Kinne, R.4
  • 357
    • 0036453581 scopus 로고    scopus 로고
    • +,K(+)ATPase by the serum and glucocorticoid-dependent kinase sgk1
    • +,K(+)ATPase by the serum and glucocorticoid-dependent kinase sgk1. Pflügers Arch 2002, 444:426-431.
    • (2002) Pflügers Arch , vol.444 , pp. 426-431
    • Setiawan, I.1    Henke, G.2    Feng, Y.X.3
  • 358
    • 0028264177 scopus 로고
    • Evidence that the cation occlusion domain of Na/K-ATPase consists of a complex of membrane-spanning segments. Analysis of limit membrane-embedded tryptic fragments
    • Shainskaya A., Karlish S.J.D. Evidence that the cation occlusion domain of Na/K-ATPase consists of a complex of membrane-spanning segments. Analysis of limit membrane-embedded tryptic fragments. J Biol Chem 1994, 269:10780-10789.
    • (1994) J Biol Chem , vol.269 , pp. 10780-10789
    • Shainskaya, A.1    Karlish, S.J.D.2
  • 360
    • 2142763787 scopus 로고    scopus 로고
    • + pump alpha 2-isoform specifically couples to contractility in vascular smooth muscle: evidence from gene-targeted neonatal mice
    • + pump alpha 2-isoform specifically couples to contractility in vascular smooth muscle: evidence from gene-targeted neonatal mice. Am J Physiol Cell Physiol 2004, 286:C813-C820.
    • (2004) Am J Physiol Cell Physiol , vol.286
    • Shelly, D.A.1    He, S.W.2    Moseley, A.3
  • 362
    • 0028246635 scopus 로고
    • Identification of a region of the H,K-ATPase a subunit associated with the b subunit
    • Shin J.M., Sachs G. Identification of a region of the H,K-ATPase a subunit associated with the b subunit. J Biol Chem 1994, 269:8642-8646.
    • (1994) J Biol Chem , vol.269 , pp. 8642-8646
    • Shin, J.M.1    Sachs, G.2
  • 365
    • 0024339819 scopus 로고
    • Antisera specific for the a1, a2, a3, and b subunits of the Na, K-ATPase: differential expression of a and b subunits in rat tissue membranes
    • Shyjian A.W., Levenson R. Antisera specific for the a1, a2, a3, and b subunits of the Na, K-ATPase: differential expression of a and b subunits in rat tissue membranes. Biochemistry 1989, 28:4531-4535.
    • (1989) Biochemistry , vol.28 , pp. 4531-4535
    • Shyjian, A.W.1    Levenson, R.2
  • 367
    • 0027474515 scopus 로고
    • Functional identification of H-K-ATPase in intercalated cells of cortical collecting tubule
    • Silver R.B., Frindt G. Functional identification of H-K-ATPase in intercalated cells of cortical collecting tubule. Am J Physiol Renal Fluid Electrolyte Physiol 1993, 264:F259-F266.
    • (1993) Am J Physiol Renal Fluid Electrolyte Physiol , vol.264
    • Silver, R.B.1    Frindt, G.2
  • 368
    • 0029867508 scopus 로고    scopus 로고
    • Stimulation of apical H-K-ATPase in intercalated cells of cortical collecting duct with chronic metabolic acidosis
    • Silver R.B., Mennitt P., Satlin L.M. Stimulation of apical H-K-ATPase in intercalated cells of cortical collecting duct with chronic metabolic acidosis. Am J Physiol Renal Fluid Electrolyte Physiol 1996, 39:F539-F547.
    • (1996) Am J Physiol Renal Fluid Electrolyte Physiol , vol.39
    • Silver, R.B.1    Mennitt, P.2    Satlin, L.M.3
  • 369
    • 0030574276 scopus 로고    scopus 로고
    • Bacterial resistances to toxic metal ions-a review
    • Silver S. Bacterial resistances to toxic metal ions-a review. Gene 1996, 179:9-19.
    • (1996) Gene , vol.179 , pp. 9-19
    • Silver, S.1
  • 371
    • 0001409028 scopus 로고
    • The influence of some cations on an adenosinetriphosphatase from peripheral nerves
    • Skou J.C. The influence of some cations on an adenosinetriphosphatase from peripheral nerves. Biochim Biophys Acta 1957, 23:394-401.
    • (1957) Biochim Biophys Acta , vol.23 , pp. 394-401
    • Skou, J.C.1
  • 373
    • 0026548232 scopus 로고
    • Three-dimensional structure of Na, K-ATPase determined from membrane crystals induced by cobalt-tetrammine-ATP
    • Skriver E., Kavéus U., Hebert H., Maunsbach A.B. Three-dimensional structure of Na, K-ATPase determined from membrane crystals induced by cobalt-tetrammine-ATP. J Struct Biol 1992, 108:176-185.
    • (1992) J Struct Biol , vol.108 , pp. 176-185
    • Skriver, E.1    Kavéus, U.2    Hebert, H.3    Maunsbach, A.B.4
  • 374
  • 375
    • 0023829545 scopus 로고
    • Digitalis: mechanisms of action and clinicaluse
    • Smith T.W. Digitalis: mechanisms of action and clinicaluse. N Engl J Med 1988, 318:358-365.
    • (1988) N Engl J Med , vol.318 , pp. 358-365
    • Smith, T.W.1
  • 376
    • 2942668632 scopus 로고    scopus 로고
    • Phosphoryl transfer and calcium ion occlusion in the calcium pump
    • Sorensen T.LM., Moller J.V., Nissen P. Phosphoryl transfer and calcium ion occlusion in the calcium pump. Science 2004, 304:1672-1675.
    • (2004) Science , vol.304 , pp. 1672-1675
    • Sorensen, T.L.M.1    Moller, J.V.2    Nissen, P.3
  • 377
    • 0034647744 scopus 로고    scopus 로고
    • Stomachs of mice lacking the gastric H,K-ATPase alpha-subunit have achlorhydria, abnormal parietal cells, and ciliated metaplasia
    • Spicer Z., Miller M.L., Andringa A., et al. Stomachs of mice lacking the gastric H,K-ATPase alpha-subunit have achlorhydria, abnormal parietal cells, and ciliated metaplasia. J Biol Chem 2000, 275:21555-21565.
    • (2000) J Biol Chem , vol.275 , pp. 21555-21565
    • Spicer, Z.1    Miller, M.L.2    Andringa, A.3
  • 379
    • 0030990390 scopus 로고    scopus 로고
    • Na,K-ATPase subunit isoforms in human reticulocytes-evidence from reverse transcription-pcr for the presence of alpha-1, alpha-3, beta-2, beta-3, and gamma
    • Stengelin M.K., Hoffman J.F. Na,K-ATPase subunit isoforms in human reticulocytes-evidence from reverse transcription-pcr for the presence of alpha-1, alpha-3, beta-2, beta-3, and gamma. Proc Natl Acad Sci U S A 1997, 94:5943-5948.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 5943-5948
    • Stengelin, M.K.1    Hoffman, J.F.2
  • 381
    • 0035861678 scopus 로고    scopus 로고
    • Short-term effect of aldosterone on Na,K-ATPase cell surface expression in kidney collecting duct cells
    • Summa V., Mordasini D., Roger F., et al. Short-term effect of aldosterone on Na,K-ATPase cell surface expression in kidney collecting duct cells. J Biol Chem 2001, 276::47087-47093.
    • (2001) J Biol Chem , pp. 47087-47093
    • Summa, V.1    Mordasini, D.2    Roger, F.3
  • 382
    • 0027058504 scopus 로고
    • Overlapping and diverse distribution of Na-K ATPase isozymes in neurons and glia
    • (Suppl)
    • Sweadner K.J. Overlapping and diverse distribution of Na-K ATPase isozymes in neurons and glia. Can J Physiol Pharmacol 1992, 70:S255-S259. (Suppl).
    • (1992) Can J Physiol Pharmacol , vol.70
    • Sweadner, K.J.1
  • 383
    • 0022251551 scopus 로고
    • Enzymatic properties of separated isozymes of Na,K-ATPase
    • Sweadner K.J. Enzymatic properties of separated isozymes of Na,K-ATPase. J Biol Chem 1985, 260:11508-11513.
    • (1985) J Biol Chem , vol.260 , pp. 11508-11513
    • Sweadner, K.J.1
  • 385
    • 0035875154 scopus 로고    scopus 로고
    • 2+- ATPase of the sarcoplasmic reticulum
    • 2+- ATPase of the sarcoplasmic reticulum. Biochem J 2001, 356:685-704.
    • (2001) Biochem J , vol.356 , pp. 685-704
    • Sweadner, K.J.1    Donnet, C.2
  • 386
    • 0034662757 scopus 로고    scopus 로고
    • The FXYD gene family of small ion transport regulators or channels: cDNA sequence, protein signature sequence, and expression
    • Sweadner K.J., Rael E. The FXYD gene family of small ion transport regulators or channels: cDNA sequence, protein signature sequence, and expression. Genomics 2000, 68:41-56.
    • (2000) Genomics , vol.68 , pp. 41-56
    • Sweadner, K.J.1    Rael, E.2
  • 387
    • 0029992825 scopus 로고    scopus 로고
    • A subfamily of P-type ATPases with aminophospholipid transporting activity
    • Tang X.J., Halleck M.S., Schlegel R.A., Williamson P. A subfamily of P-type ATPases with aminophospholipid transporting activity. Science 1996, 272:1495-1497.
    • (1996) Science , vol.272 , pp. 1495-1497
    • Tang, X.J.1    Halleck, M.S.2    Schlegel, R.A.3    Williamson, P.4
  • 388
    • 0024502870 scopus 로고
    • +-ATPase activities in renal tubule segments of rat inner medulla
    • +-ATPase activities in renal tubule segments of rat inner medulla. Am J Physiol 1989, 256:F218-F223.
    • (1989) Am J Physiol , vol.256
    • Terada, Y.1    Knepper, M.A.2
  • 389
    • 0031434245 scopus 로고    scopus 로고
    • Tissue-specific distribution and modulatory role of the gamma subunit of the Na,K-ATPase
    • Therien A.G., Goldshleger R., Karlish S.J.D., Blostein R. Tissue-specific distribution and modulatory role of the gamma subunit of the Na,K-ATPase. J Biol Chem 1997, 272:32628-32634.
    • (1997) J Biol Chem , vol.272 , pp. 32628-32634
    • Therien, A.G.1    Goldshleger, R.2    Karlish, S.J.D.3    Blostein, R.4
  • 390
    • 0033617311 scopus 로고    scopus 로고
    • Expression and functional role of the g subunit of the Na,K-ATPase in mammalian cells
    • Therien A.G., Karlish S.J.D., Blostein R. Expression and functional role of the g subunit of the Na,K-ATPase in mammalian cells. J Biol Chem 1999, 274:12252-12256.
    • (1999) J Biol Chem , vol.274 , pp. 12252-12256
    • Therien, A.G.1    Karlish, S.J.D.2    Blostein, R.3
  • 391
    • 0029911740 scopus 로고    scopus 로고
    • Tissue-specific versus isoform-specific differences in cation activation kinetics of the Na,K-ATPase
    • Therien A.G., Nestor N.B., Ball W.J., Blostein R. Tissue-specific versus isoform-specific differences in cation activation kinetics of the Na,K-ATPase. J Biol Chem 1996, 271:7104-7112.
    • (1996) J Biol Chem , vol.271 , pp. 7104-7112
    • Therien, A.G.1    Nestor, N.B.2    Ball, W.J.3    Blostein, R.4
  • 392
    • 16944363867 scopus 로고    scopus 로고
    • Skeletal muscle Na,K-ATPase alpha and beta subunit protein levels respond to hypokalemic challenge with isoform and muscle type specificity
    • Thompson C.B,, McDonough A.A. Skeletal muscle Na,K-ATPase alpha and beta subunit protein levels respond to hypokalemic challenge with isoform and muscle type specificity. J Biol Chem 1996, 271:32653-32658.
    • (1996) J Biol Chem , vol.271 , pp. 32653-32658
    • Thompson, C.B.1    McDonough, A.A.2
  • 393
    • 3943055518 scopus 로고    scopus 로고
    • 2+-ATPase of the sacroplasmic reticulum
    • 2+-ATPase of the sacroplasmic reticulum. Annu Rev Biochem 2004, 73:269-292.
    • (2004) Annu Rev Biochem , vol.73 , pp. 269-292
    • Toyoshima, C.1    Inesi, G.2
  • 394
    • 3242888769 scopus 로고    scopus 로고
    • Crystal structure of the calcium pump with a bound ATP analogue
    • Toyoshima C., Mizutani T. Crystal structure of the calcium pump with a bound ATP analogue. Nature 2004, 430:529-535.
    • (2004) Nature , vol.430 , pp. 529-535
    • Toyoshima, C.1    Mizutani, T.2
  • 395
    • 0034621834 scopus 로고    scopus 로고
    • Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 A resolution
    • Toyoshima C., Nakasako M., Nomura H., Ogawa H. Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 A resolution. Nature 2000, 405:647-655.
    • (2000) Nature , vol.405 , pp. 647-655
    • Toyoshima, C.1    Nakasako, M.2    Nomura, H.3    Ogawa, H.4
  • 396
    • 0037043709 scopus 로고    scopus 로고
    • Structural changes in the calcium pump accompanying the dissociation of calcium
    • Toyoshima C., Nomura H. Structural changes in the calcium pump accompanying the dissociation of calcium. Nature 2002, 418:605-611.
    • (2002) Nature , vol.418 , pp. 605-611
    • Toyoshima, C.1    Nomura, H.2
  • 397
    • 9244232176 scopus 로고    scopus 로고
    • Lumenal gating mechanism revealed in calcium pump crystal structures with phosphate analogues
    • Toyoshima C., Nomura H., Tsuda T. Lumenal gating mechanism revealed in calcium pump crystal structures with phosphate analogues. Nature 2004, 432:361-368.
    • (2004) Nature , vol.432 , pp. 361-368
    • Toyoshima, C.1    Nomura, H.2    Tsuda, T.3
  • 398
    • 0028356961 scopus 로고
    • Photochemical labeling and inhibition of Na,K-ATPase by 2-azido-ATP. Identification of an amino acid located within the ATP binding site
    • Tran C.M., Huston E.E., Farley R.A. Photochemical labeling and inhibition of Na,K-ATPase by 2-azido-ATP. Identification of an amino acid located within the ATP binding site. J Biol Chem 1994, 269:6558-6565.
    • (1994) J Biol Chem , vol.269 , pp. 6558-6565
    • Tran, C.M.1    Huston, E.E.2    Farley, R.A.3
  • 400
    • 0027169925 scopus 로고
    • Physicochemical characterization of a ouabain isomer isolated from bovine hypothalamus
    • Tymiak A.A., Norman J.A., Bolgar M., et al. Physicochemical characterization of a ouabain isomer isolated from bovine hypothalamus. Proc Natl Acad Sci U S A 1993, 90:8189-8193.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 8189-8193
    • Tymiak, A.A.1    Norman, J.A.2    Bolgar, M.3
  • 401
    • 0027518959 scopus 로고
    • Site-directed mutagenesis of a predicted cation binding site of Na,K-ATPase
    • Van Huysse J.W., Jewell E.A., Lingrel J.B.. Site-directed mutagenesis of a predicted cation binding site of Na,K-ATPase. Biochemistry 1993, 32:819-826.
    • (1993) Biochemistry , vol.32 , pp. 819-826
    • Van, H.J.W.1    Jewell, E.A.2    Lingrel, J.B..3
  • 403
    • 0026594969 scopus 로고
    • + pumps in Xenopus oocytes by membrane potential and stimulation of protein kinases
    • + pumps in Xenopus oocytes by membrane potential and stimulation of protein kinases. J Membr Biol 1992, 125:119-132.
    • (1992) J Membr Biol , vol.125 , pp. 119-132
    • Vasilets, L.A.1    Schwarz, W.2
  • 405
    • 0024433097 scopus 로고
    • Aldosterone induces a rapid increase in the rate of Na,K-ATPase gene transcription in cultured kidney cells
    • Verrey F., Kraehenbühl J.-P., Rossier B.C. Aldosterone induces a rapid increase in the rate of Na,K-ATPase gene transcription in cultured kidney cells. Mol Endocrinol 1989, 3:1369-1376.
    • (1989) Mol Endocrinol , vol.3 , pp. 1369-1376
    • Verrey, F.1    Kraehenbühl, J.-P.2    Rossier, B.C.3
  • 407
    • 0027772018 scopus 로고
    • +-ATPase is not an essential residue for active transport of sodium and potassium ions
    • +-ATPase is not an essential residue for active transport of sodium and potassium ions. Biochemistry 1993, 32:13340-13349.
    • (1993) Biochemistry , vol.32 , pp. 13340-13349
    • Vilsen, B.1
  • 408
    • 0027340285 scopus 로고
    • +-activated ATP hydrolysis with normal turnover number
    • +-activated ATP hydrolysis with normal turnover number. FEBS Lett 1993, 333:44-50.
    • (1993) FEBS Lett , vol.333 , pp. 44-50
    • Vilsen, B.1
  • 409
    • 0028988432 scopus 로고
    • +-ATPase displays low cation affinity and catalyzes ATP hydrolysis at a high rate in the absence of potassium
    • +-ATPase displays low cation affinity and catalyzes ATP hydrolysis at a high rate in the absence of potassium. Biochemistry 1995, 34:1455-1463.
    • (1995) Biochemistry , vol.34 , pp. 1455-1463
    • Vilsen, B.1
  • 411
    • 0038107524 scopus 로고    scopus 로고
    • + controls cell surface expression of Na,K-ATPase via a cAMP-independent PKA pathway in mammalian kidney collecting duct cells
    • + controls cell surface expression of Na,K-ATPase via a cAMP-independent PKA pathway in mammalian kidney collecting duct cells. Mol Biol Cell 2003, 14:2677-2688.
    • (2003) Mol Biol Cell , vol.14 , pp. 2677-2688
    • Vinciguerra, M.1    Deschenes, G.2    Hasler, U.3
  • 412
    • 33644801924 scopus 로고    scopus 로고
    • Cytokines and sodium induce protein kinase A-dependent cell-surface Na,K-ATPase recruitment via dissociation of NF-kB/IkB/protein kinase A catalytic subunit complex in collecting duct principal cells
    • Vinciguerra M., Hasler U., Mordasini D., et al. Cytokines and sodium induce protein kinase A-dependent cell-surface Na,K-ATPase recruitment via dissociation of NF-kB/IkB/protein kinase A catalytic subunit complex in collecting duct principal cells. J Am Soc Nephrol 2005, 16:2576-2585.
    • (2005) J Am Soc Nephrol , vol.16 , pp. 2576-2585
    • Vinciguerra, M.1    Hasler, U.2    Mordasini, D.3
  • 413
    • 0025803091 scopus 로고
    • +-Atpase activity and hormones in single nephron segments from nephrotic rats
    • +-Atpase activity and hormones in single nephron segments from nephrotic rats. Clin Sci 1991, 80:599-604.
    • (1991) Clin Sci , vol.80 , pp. 599-604
    • Vogt, B.1    Favre, H.2
  • 414
    • 0027446365 scopus 로고
    • Isolation of a candidate gene for Menkes disease and evidence that it encodes a copper-transporting ATPase
    • Vulpe C., Levinson B., Whitney S., Packman S., Gitschier J. Isolation of a candidate gene for Menkes disease and evidence that it encodes a copper-transporting ATPase. Nat Genet 1993, 3:7-13.
    • (1993) Nat Genet , vol.3 , pp. 7-13
    • Vulpe, C.1    Levinson, B.2    Whitney, S.3    Packman, S.4    Gitschier, J.5
  • 416
    • 0031752940 scopus 로고    scopus 로고
    • + restriction upregulates total and Sch-28080- sensitive bicarbonate absorption in rat tIMCD
    • + restriction upregulates total and Sch-28080- sensitive bicarbonate absorption in rat tIMCD. Am J Physiol Renal Physiol 1998, 275:F543-F549.
    • (1998) Am J Physiol Renal Physiol , vol.275
    • Wall, S.M.1    Mehta, P.2    DuBose, T.D.3
  • 418
    • 0023215971 scopus 로고
    • +-ATPase and acid secretion by SCH 28080, a substituted pyridyl(1,2a)imidazole
    • +-ATPase and acid secretion by SCH 28080, a substituted pyridyl(1,2a)imidazole. J Biol Chem 1987, 262:2077-2084.
    • (1987) J Biol Chem , vol.262 , pp. 2077-2084
    • Wallmark, B.1    Briving, C.2    Fryklund, J.3
  • 420
    • 0030748308 scopus 로고    scopus 로고
    • Palytoxin effects through interaction with the Na,K-ATPase in Xenopus oocyte
    • Wang X., Horisberger J-D. Palytoxin effects through interaction with the Na,K-ATPase in Xenopus oocyte. FEBS Lett 1997, 409:391-395.
    • (1997) FEBS Lett , vol.409 , pp. 391-395
    • Wang, X.1    Horisberger, J.-D.2
  • 422
    • 33745374903 scopus 로고    scopus 로고
    • Potassium depletion and acid-base transporters in rat kidney: differential effect of hypophysectomy
    • Wang Z., Baird N., Shumaker H., Soleimani M. Potassium depletion and acid-base transporters in rat kidney: differential effect of hypophysectomy. Am J Physiol 1997, 272:F736-F743.
    • (1997) Am J Physiol , vol.272
    • Wang, Z.1    Baird, N.2    Shumaker, H.3    Soleimani, M.4
  • 423
    • 0027254430 scopus 로고
    • Solubilized ab Na,K-ATPase remains protomeric during turnover yet shows apparent negative cooperativity toward ATP
    • Ward D.G., Cavieres J.D. Solubilized ab Na,K-ATPase remains protomeric during turnover yet shows apparent negative cooperativity toward ATP. Proc Natl Acad Sci U S A 1993, 90:5332-5336.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 5332-5336
    • Ward, D.G.1    Cavieres, J.D.2
  • 426
    • 4744368156 scopus 로고    scopus 로고
    • Stress-induced expression of the gamma subunit (FXYD2) modulates Na,K-ATPase activity and cell growth
    • Wetzel R.K., Pascoa J.L., Arystarkhova E. Stress-induced expression of the gamma subunit (FXYD2) modulates Na,K-ATPase activity and cell growth. J Biol Chem 2004, 279:41750-41757.
    • (2004) J Biol Chem , vol.279 , pp. 41750-41757
    • Wetzel, R.K.1    Pascoa, J.L.2    Arystarkhova, E.3
  • 427
    • 0034836615 scopus 로고    scopus 로고
    • Immunocytochemical localization of Na-K-ATPase alpha- and gamma-subunits in rat kidney
    • Wetzel R.K., Sweadner K.J. Immunocytochemical localization of Na-K-ATPase alpha- and gamma-subunits in rat kidney. Am J Physiol Renal Physiol 2001, 281:F531-F545.
    • (2001) Am J Physiol Renal Physiol , vol.281
    • Wetzel, R.K.1    Sweadner, K.J.2
  • 428
    • 0038819028 scopus 로고    scopus 로고
    • Phospholemman expression in extraglomer ular mesangium and afferent arteriole of the juxtaglomerular apparatus
    • Wetzel R.K., Sweadner K.J. Phospholemman expression in extraglomer ular mesangium and afferent arteriole of the juxtaglomerular apparatus. Am J Physiol Renal Physiol 2003, 285:F121-F129.
    • (2003) Am J Physiol Renal Physiol , vol.285
    • Wetzel, R.K.1    Sweadner, K.J.2
  • 429
    • 0033883799 scopus 로고    scopus 로고
    • Apical plasma membrane mispolarization of NaKATPase in polycystic kidney disease epithelia is associated with aberrant expression of the beta 2 isoform
    • Wilson P.D., Devuyst O., Li X.H,, et al. Apical plasma membrane mispolarization of NaKATPase in polycystic kidney disease epithelia is associated with aberrant expression of the beta 2 isoform. Am J Pathol 2000, 156:253-268.
    • (2000) Am J Pathol , vol.156 , pp. 253-268
    • Wilson, P.D.1    Devuyst, O.2    Li, X.H.3
  • 430
    • 0026465110 scopus 로고
    • Rubidium absorption and proton secretion by rabbit outer medullary collecting duct via H-K-ATPase
    • Wingo C.S., Armitage F.E. Rubidium absorption and proton secretion by rabbit outer medullary collecting duct via H-K-ATPase. Am J Physiol Renal Fluid Electrolyte Physiol 1992, 263:F849-F857.
    • (1992) Am J Physiol Renal Fluid Electrolyte Physiol , vol.263
    • Wingo, C.S.1    Armitage, F.E.2
  • 431
    • 0025009959 scopus 로고
    • H-K-ATPase immunoreactivity in cortical and outer medullary collecting duct
    • Wingo C.S., Madsen K.M., Smolka A., Tisher C.C. H-K-ATPase immunoreactivity in cortical and outer medullary collecting duct. Kidney Int 1990, 38:985-990.
    • (1990) Kidney Int , vol.38 , pp. 985-990
    • Wingo, C.S.1    Madsen, K.M.2    Smolka, A.3    Tisher, C.C.4
  • 432
    • 0024356509 scopus 로고
    • Active proton secretion and potassium absorption in the rabbit outer medullary collecting duct. Functional evidence for proton-potassium-activated adenosine triphosphatase
    • Wingo C.S., Straub S.G. Active proton secretion and potassium absorption in the rabbit outer medullary collecting duct. Functional evidence for proton-potassium-activated adenosine triphosphatase. J Clin Invest 1989, 84:361-365.
    • (1989) J Clin Invest , vol.84 , pp. 361-365
    • Wingo, C.S.1    Straub, S.G.2
  • 434
    • 0032924856 scopus 로고    scopus 로고
    • Characterization of the fourth alpha isoform of the Na,K-ATPase
    • Woo A.L., James P.F., Lingrel J.B., et al. Characterization of the fourth alpha isoform of the Na,K-ATPase. J Membr Biol 1999, 169:39-44.
    • (1999) J Membr Biol , vol.169 , pp. 39-44
    • Woo, A.L.1    James, P.F.2    Lingrel, J.B.3
  • 437
    • 0026389786 scopus 로고
    • Sodium-calcium exchange and phototransduction in retinal photoreceptors
    • Yau K.W., Nakatani K., Tamura T. Sodium-calcium exchange and phototransduction in retinal photoreceptors. Ann N Y Acad Sci 1991, 639:275-284.
    • (1991) Ann N Y Acad Sci , vol.639 , pp. 275-284
    • Yau, K.W.1    Nakatani, K.2    Tamura, T.3
  • 438
    • 0022374116 scopus 로고
    • Rheogenic sodium-bicarbonate cotransport in the peritubular cell membrane of rat renal proximal tubule
    • Yoshitomi K., Burckhardt B.C., Fromter E. Rheogenic sodium-bicarbonate cotransport in the peritubular cell membrane of rat renal proximal tubule. Pflügers Arch 1985, 405:360-366.
    • (1985) Pflügers Arch , vol.405 , pp. 360-366
    • Yoshitomi, K.1    Burckhardt, B.C.2    Fromter, E.3
  • 439
    • 0027993705 scopus 로고
    • Inhibition by ouabain of palytoxin-induced catecholamine secretion and calcium influx into cultured bovine adrenal chromaffin cells
    • Yoshizumi M., Ishimura Y., Masuda Y., et al. Inhibition by ouabain of palytoxin-induced catecholamine secretion and calcium influx into cultured bovine adrenal chromaffin cells. Biochem Pharmacol 1994, 48:1047-1049.
    • (1994) Biochem Pharmacol , vol.48 , pp. 1047-1049
    • Yoshizumi, M.1    Ishimura, Y.2    Masuda, Y.3
  • 442
    • 0030746385 scopus 로고    scopus 로고
    • Sodium kinetics of Na,K-ATPase a isoforms in intact transfected Hela cells
    • Zahler R., Zhang Z.T., Manor M., Boron W.F. Sodium kinetics of Na,K-ATPase a isoforms in intact transfected Hela cells. J Gen Physiol 1997, 110:201-213.
    • (1997) J Gen Physiol , vol.110 , pp. 201-213
    • Zahler, R.1    Zhang, Z.T.2    Manor, M.3    Boron, W.F.4
  • 443
    • 2442680179 scopus 로고    scopus 로고
    • SGK1 increases Na,K-ATP cell-surface expression and function in Xenopus laevis oocytes
    • Zecevic M., Heitzmann D., Camargo S.M.R., Verrey F. SGK1 increases Na,K-ATP cell-surface expression and function in Xenopus laevis oocytes. Pflügers Arch 2004, 448:29-35.
    • (2004) Pflügers Arch , vol.448 , pp. 29-35
    • Zecevic, M.1    Heitzmann, D.2    Camargo, S.M.R.3    Verrey, F.4
  • 444
    • 0029860263 scopus 로고    scopus 로고
    • Flux coupling in a neuronal glutamate transporter
    • Zerangue N., Kavanaugh M.P. Flux coupling in a neuronal glutamate transporter. Nature 1996, 383:634-637.
    • (1996) Nature , vol.383 , pp. 634-637
    • Zerangue, N.1    Kavanaugh, M.P.2
  • 446
    • 0029147014 scopus 로고
    • Na,K-ATPase inhibitors from bovine hypothalamus and human plasma are different from ouabain-nanogram scale CD structural analysis
    • Zhao N., Lo L.C., Berova N., et al. Na,K-ATPase inhibitors from bovine hypothalamus and human plasma are different from ouabain-nanogram scale CD structural analysis. Biochemistry 1995, 34:9893-9896.
    • (1995) Biochemistry , vol.34 , pp. 9893-9896
    • Zhao, N.1    Lo, L.C.2    Berova, N.3
  • 448
    • 0027086836 scopus 로고
    • Mechanisms of rubidium permeation by rabbit cortical collecting duct during potassium restriction
    • Zhou X., Wingo C.S. Mechanisms of rubidium permeation by rabbit cortical collecting duct during potassium restriction. Am J Physiol Renal Fluid Electrolyte Physiol 1992, 263:F1134-F1141.
    • (1992) Am J Physiol Renal Fluid Electrolyte Physiol , vol.263
    • Zhou, X.1    Wingo, C.S.2
  • 450
    • 0034884703 scopus 로고    scopus 로고
    • Increased CO2 stimulates K/Rb reabsorption mediated by H-K-ATPase in CCD of potassium-restricted rabbit
    • Zhou X.M., Nakamura S., Xia S.L., Wingo C.S. Increased CO2 stimulates K/Rb reabsorption mediated by H-K-ATPase in CCD of potassium-restricted rabbit. Am J Physiol Renal Physiol 2001, 281:F366-F373.
    • (2001) Am J Physiol Renal Physiol , vol.281
    • Zhou, X.M.1    Nakamura, S.2    Xia, S.L.3    Wingo, C.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.