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Volumn 143, Issue 4, 2014, Pages 449-464

Route, mechanism, and implications of proton import during Na++/K+ exchange by native Na++/K+-ATPase pumps

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); ATP1A1 PROTEIN, XENOPUS; PROTON PUMP; XENOPUS PROTEIN;

EID: 84897054891     PISSN: 00221295     EISSN: 15407748     Source Type: Journal    
DOI: 10.1085/jgp.201311148     Document Type: Article
Times cited : (62)

References (87)
  • 1
    • 78449241100 scopus 로고    scopus 로고
    • + ATPase blockade on cortical layer V neurons
    • + ATPase blockade on cortical layer V neurons. J. Physiol. 588:4401-4414. http://dx.doi.org/10.1113/jphysiol.2010.191858
    • (2010) J. Physiol. , vol.588 , pp. 4401-4414
    • Anderson, T.R.1    Huguenard, J.R.2    Prince, D.A.3
  • 2
    • 0037458010 scopus 로고    scopus 로고
    • +-pump ligands modulate gating of palytoxin-induced ion channels
    • +-pump ligands modulate gating of palytoxin-induced ion channels. Proc. Natl. Acad. Sci. USA. 100:501-505. http://dx.doi.org/10.1073/pnas.0135849100
    • (2003) Proc. Natl. Acad. Sci. USA. , vol.100 , pp. 501-505
    • Artigas, P.1    Gadsby, D.C.2
  • 3
    • 33747584895 scopus 로고    scopus 로고
    • Ouabain affinity determining residues lie close to the Na/K pump ion pathway
    • Artigas, P., and D.C. Gadsby. 2006. Ouabain affinity determining residues lie close to the Na/K pump ion pathway. Proc. Natl. Acad. Sci. USA. 103:12613-12618. http://dx.doi.org/10.1073/pnas.0602720103
    • (2006) Proc. Natl. Acad. Sci. USA. , vol.103 , pp. 12613-12618
    • Artigas, P.1    Gadsby, D.C.2
  • 5
    • 0034636796 scopus 로고    scopus 로고
    • Proton translocation by cytochrome c oxidase can take place without the conserved glutamic acid in subunit I.
    • Backgren, C., G. Hummer, M. Wikström, and A. Puustinen. 2000. Proton translocation by cytochrome c oxidase can take place without the conserved glutamic acid in subunit I. Biochemistry. 39:7863-7867. http://dx.doi.org/10.1021/bi000806b
    • (2000) Biochemistry , vol.39 , pp. 7863-7867
    • Backgren, C.1    Hummer, G.2    Wikström, M.3    Puustinen, A.4
  • 7
    • 0344608880 scopus 로고    scopus 로고
    • + regulation in cardiac myocytes.
    • + regulation in cardiac myocytes. Cardiovasc. Res. 57:897-912. http://dx.doi.org/10.1016/S0008-6363(02)00656-9
    • (2003) Cardiovasc. Res. , vol.57 , pp. 897-912
    • Bers, D.M.1    Barry, W.H.2    Despa, S.3
  • 8
    • 84890209378 scopus 로고    scopus 로고
    • The gating charge should not be estimated by fitting a two-state model to a Q-V curve.
    • Bezanilla, F., and C.A. Villalba-Galea. 2013. The gating charge should not be estimated by fitting a two-state model to a Q-V curve. J. Gen. Physiol. 142:575-578. http://dx.doi.org/10.1085/jgp.201311056
    • (2013) J. Gen. Physiol. , vol.142 , pp. 575-578
    • Bezanilla, F.1    Villalba-Galea, C.A.2
  • 9
    • 0025356602 scopus 로고
    • Comparison of intracellular pH transients in single ventricular myocytes and isolated ventricular muscle of guinea-pig
    • Bountra, C., T. Powell, and R.D. Vaughan-Jones. 1990. Comparison of intracellular pH transients in single ventricular myocytes and isolated ventricular muscle of guinea-pig. J. Physiol. 424:343-365.
    • (1990) J. Physiol. , vol.424 , pp. 343-365
    • Bountra, C.1    Powell, T.2    Vaughan-Jones, R.D.3
  • 10
    • 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., G. Crambert, S. Kharoubi-Hess, K. Geering, and J.-D. Horisberger. 2003. 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. 278:19237-19244. http://dx.doi.org/10.1074/jbc. M300946200
    • (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
  • 12
    • 0026568206 scopus 로고
    • Mutation of a cysteine in the first transmembrane segment of Na, K-ATPase α subunit confers ouabain resistance
    • Canessa, C.M., J.-D. Horisberger, D. Louvard, and B.C. Rossier. 1992. Mutation of a cysteine in the first transmembrane segment of Na, K-ATPase α subunit confers ouabain resistance. EMBO J. 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
  • 13
    • 84855489518 scopus 로고    scopus 로고
    • Estimating the voltage-dependent free energy change of ion channels using the median voltage for activation.
    • Chowdhury, S., and B. Chanda. 2012. Estimating the voltage-dependent free energy change of ion channels using the median voltage for activation. J. Gen. Physiol. 139:3-17. http://dx.doi.org/10.1085/jgp.201110722
    • (2012) J. Gen. Physiol. , vol.139 , pp. 3-17
    • Chowdhury, S.1    Chanda, B.2
  • 14
    • 84874782025 scopus 로고    scopus 로고
    • A structural view on the functional importance of the sugar moiety and steroid hydroxyls of cardiotonic steroids in binding to Na, K-ATPase
    • Cornelius, F., R. Kanai, and C. Toyoshima. 2013. A structural view on the functional importance of the sugar moiety and steroid hydroxyls of cardiotonic steroids in binding to Na, K-ATPase. J. Biol. Chem. 288:6602-6616. http://dx.doi.org/10.1074/jbc. M112.442137
    • (2013) J. Biol. Chem. , vol.288 , pp. 6602-6616
    • Cornelius, F.1    Kanai, R.2    Toyoshima, C.3
  • 15
    • 0023858834 scopus 로고
    • Voltage dependence of the Na-K pump.
    • De Weer, P., D.C. Gadsby, and R.F. Rakowski. 1988. Voltage dependence of the Na-K pump. Annu. Rev. Physiol. 50:225-241. http://dx.doi.org/10.1146/annurev.physiol.50.1.225
    • (1988) Annu. Rev. Physiol. , vol.50 , pp. 225-241
    • De Weer, P.1    Gadsby, D.C.2    Rakowski, R.F.3
  • 16
    • 0035004423 scopus 로고    scopus 로고
    • Voltage dependence of the apparent affinity for external Na+ of the backwardrunning sodium pump.
    • De Weer, P., D.C. Gadsby, and R.F. Rakowski. 2001. Voltage dependence of the apparent affinity for external Na+ of the backwardrunning sodium pump. J. Gen. Physiol. 117:315-328. http://dx.doi.org/10.1085/jgp.117.4.315
    • (2001) J. Gen. Physiol. , vol.117 , pp. 315-328
    • De Weer, P.1    Gadsby, D.C.2    Rakowski, R.F.3
  • 17
    • 0037379781 scopus 로고    scopus 로고
    • Voltage-gated proton channels and other proton transfer pathways
    • DeCoursey, T.E. 2003. Voltage-gated proton channels and other proton transfer pathways. Physiol. Rev. 83:475-579.
    • (2003) Physiol. Rev. , vol.83 , pp. 475-579
    • DeCoursey, T.E.1
  • 20
    • 0029076899 scopus 로고
    • An excitatory amino-acid transporter with properties of a ligand-gated chloride channel
    • Fairman, W.A., R.J. Vandenberg, J.L. Arriza, M.P. Kavanaugh, and S.G. Amara. 1995. An excitatory amino-acid transporter with properties of a ligand-gated chloride channel. Nature. 375:599-603. http://dx.doi.org/10.1038/375599a0
    • (1995) Nature , vol.375 , pp. 599-603
    • Fairman, W.A.1    Vandenberg, R.J.2    Arriza, J.L.3    Kavanaugh, M.P.4    Amara, S.G.5
  • 21
    • 0023655684 scopus 로고
    • Rapid release of 42K and 86Rb from an occluded state of the Na, K-pump in the presence of ATP or ADP.
    • Forbush, B., III. 1987a. Rapid release of 42K and 86Rb from an occluded state of the Na, K-pump in the presence of ATP or ADP. J. Biol. Chem. 262:11104-11115.
    • (1987) J. Biol. Chem. , vol.262 , pp. 11104-11115
    • Forbush III, B.1
  • 22
    • 0023655701 scopus 로고
    • Rapid release of 42K or 86Rb from two distinct transport sites on the Na, K-pump in the presence of Pi or vanadate.
    • Forbush, B., III. 1987b. Rapid release of 42K or 86Rb from two distinct transport sites on the Na, K-pump in the presence of Pi or vanadate. J. Biol. Chem. 262:11116-11127.
    • (1987) J. Biol. Chem. , vol.262 , pp. 11116-11127
    • Forbush III, B.1
  • 23
    • 0004073280 scopus 로고
    • +- ATPase in regulating ATP-dependent endosome acidification.
    • +- ATPase in regulating ATP-dependent endosome acidification. Proc. Natl. Acad. Sci. USA. 86:539-543. http://dx.doi.org/10.1073/pnas.86.2.539
    • (1989) Proc. Natl. Acad. Sci. USA. , vol.86 , pp. 539-543
    • Fuchs, R.1    Schmid, S.2    Mellman, I.3
  • 24
    • 67349185408 scopus 로고    scopus 로고
    • Ion channels versus ion pumps: the principal difference, in principle.
    • Gadsby, D.C. 2009. Ion channels versus ion pumps: the principal difference, in principle. Nat. Rev. Mol. Cell Biol. 10:344-352. http://dx.doi.org/10.1038/nrm2668
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 344-352
    • Gadsby, D.C.1
  • 25
    • 0027905015 scopus 로고
    • Extracellular access to the Na, K pump: Pathway similar to ion channel
    • Gadsby, D.C., R.F. Rakowski, and P. De Weer. 1993. Extracellular access to the Na, K pump: Pathway similar to ion channel. Science. 260:100-103. http://dx.doi.org/10.1126/science.7682009
    • (1993) Science. , vol.260 , pp. 100-103
    • Gadsby, D.C.1    Rakowski, R.F.2    De Weer, P.3
  • 27
    • 0014123484 scopus 로고
    • The stoicheiometry of the sodium pump.
    • Garrahan, P.J., and I.M. Glynn. 1967a. The stoicheiometry of the sodium pump. J. Physiol. 192:217-235.
    • (1967) J. Physiol. , vol.192 , pp. 217-235
    • Garrahan, P.J.1    Glynn, I.M.2
  • 28
    • 0014124020 scopus 로고
    • The incorporation of inorganic phosphate into adenosine triphosphate by reversal of the sodium pump.
    • Garrahan, P.J., and I.M. Glynn. 1967b. The incorporation of inorganic phosphate into adenosine triphosphate by reversal of the sodium pump. J. Physiol. 192:237-256.
    • (1967) J. Physiol. , vol.192 , pp. 237-256
    • Garrahan, P.J.1    Glynn, I.M.2
  • 29
    • 0028465482 scopus 로고
    • 31P-MRS measurements of extracellular pH of tumors using 3-aminopropylphosphonate
    • Gillies, R.J., Z. Liu, and Z. Bhujwalla. 1994. 31P-MRS measurements of extracellular pH of tumors using 3-aminopropylphosphonate. Am. J. Physiol. 267:C195-C203.
    • (1994) Am. J. Physiol. , vol.267
    • Gillies, R.J.1    Liu, Z.2    Bhujwalla, Z.3
  • 30
    • 0025633348 scopus 로고
    • A nervous system-specific isotype of the ? subunit of Na+, K+-ATPase expressed during early development of Xenopus laevis.
    • Good, P.J., K. Richter, and I.B. Dawid. 1990. A nervous system-specific isotype of the ? subunit of Na+, K+-ATPase expressed during early development of Xenopus laevis. Proc. Natl. Acad. Sci. USA. 87:9088-9092. http://dx.doi.org/10.1073/pnas.87.23.9088
    • (1990) Proc. Natl. Acad. Sci. USA. , vol.87 , pp. 9088-9092
    • Good, P.J.1    Richter, K.2    Dawid, I.B.3
  • 31
    • 0028058903 scopus 로고
    • Partial reactions of the Na, K-ATPase: Determination of rate constants.
    • Heyse, S., I. Wuddel, H.-J. Apell, and W. Stürmer. 1994. Partial reactions of the Na, K-ATPase: Determination of rate constants. J. Gen. Physiol. 104:197-240. http://dx.doi.org/10.1085/jgp.104.2.197
    • (1994) J. Gen. Physiol. , vol.104 , pp. 197-240
    • Heyse, S.1    Wuddel, I.2    Apell, H.-J.3    Stürmer, W.4
  • 32
    • 0028355065 scopus 로고
    • Channel-like function of the Na, K pump probed at microsecond resolution in giant membrane patches.
    • Hilgemann, D.W. 1994. Channel-like function of the Na, K pump probed at microsecond resolution in giant membrane patches. Science. 263:1429-1432. http://dx.doi.org/10.1126/science.8128223
    • (1994) Science. , vol.263 , pp. 1429-1432
    • Hilgemann, D.W.1
  • 35
    • 0347065354 scopus 로고    scopus 로고
    • Electrophysiological analysis of the mutated Na, K-ATPase cation binding pocket.
    • Koenderink, J.B., S. Geibel, E. Grabsch, J.J. De Pont, E. Bamberg, and T. Friedrich. 2003. Electrophysiological analysis of the mutated Na, K-ATPase cation binding pocket. J. Biol. Chem. 278:51213-51222. http://dx.doi.org/10.1074/jbc. M306384200
    • (2003) J. Biol. Chem. , vol.278 , pp. 51213-51222
    • Koenderink, J.B.1    Geibel, S.2    Grabsch, E.3    De Pont, J.J.4    Bamberg, E.5    Friedrich, T.6
  • 36
    • 55549091439 scopus 로고    scopus 로고
    • An ion gating mechanism of gastric H, K-ATPase based on molecular dynamics simulations.
    • Law, R.J., K. Munson, G. Sachs, and F.C. Lightstone. 2008. An ion gating mechanism of gastric H, K-ATPase based on molecular dynamics simulations. Biophys. J. 95:2739-2749. http://dx.doi.org/10.1529/biophysj.107.128025
    • (2008) Biophys. J. , vol.95 , pp. 2739-2749
    • Law, R.J.1    Munson, K.2    Sachs, G.3    Lightstone, F.C.4
  • 38
    • 78649876136 scopus 로고    scopus 로고
    • Selectivity of externally facing ion-binding sites in the Na/K pump to alkali metals and organic cations.
    • Ratheal, I.M., G.K. Virgin, H. Yu, B. Roux, C. Gatto, and P. Artigas. 2010. Selectivity of externally facing ion-binding sites in the Na/K pump to alkali metals and organic cations. Proc. Natl. Acad. Sci. USA. 107:18718-18723. http://dx.doi.org/10.1073/pnas.1004214107
    • (2010) Proc. Natl. Acad. Sci. USA. , vol.107 , pp. 18718-18723
    • Ratheal, I.M.1    Virgin, G.K.2    Yu, H.3    Roux, B.4    Gatto, C.5    Artigas, P.6
  • 39
    • 33749169688 scopus 로고    scopus 로고
    • +-ATPase.
    • +-ATPase. Nature. 443:470-474. http://dx.doi.org/10.1038/nature05129
    • (2006) Nature , vol.443 , pp. 470-474
    • Reyes, N.1    Gadsby, D.C.2
  • 40
    • 72449164409 scopus 로고    scopus 로고
    • Transport mechanism of a bacterial homologue of glutamate transporters
    • Reyes, N., C. Ginter, and O. Boudker. 2009. Transport mechanism of a bacterial homologue of glutamate transporters. Nature. 462:880-885. http://dx.doi.org/10.1038/nature08616
    • (2009) Nature , vol.462 , pp. 880-885
    • Reyes, N.1    Ginter, C.2    Boudker, O.3
  • 42
    • 0035251757 scopus 로고    scopus 로고
    • Ion selectivity of the cytoplasmic binding sites of the Na, K-ATPase: II. Competition of various cations.
    • Schneeberger, A., and H.-J. Apell. 2001. Ion selectivity of the cytoplasmic binding sites of the Na, K-ATPase: II. Competition of various cations. J. Membr. Biol. 179:263-273. http://dx.doi.org/10.1007/s002320010051
    • (2001) J. Membr. Biol. , vol.179 , pp. 263-273
    • Schneeberger, A.1    Apell, H.-J.2
  • 43
    • 66249147196 scopus 로고    scopus 로고
    • Crystal structure of the sodium-potassium pump at 2.4 Å resolution.
    • Shinoda, T., H. Ogawa, F. Cornelius, and C. Toyoshima. 2009. Crystal structure of the sodium-potassium pump at 2.4 Å resolution. Nature. 459:446-450. http://dx.doi.org/10.1038/nature07939
    • (2009) Nature , vol.459 , pp. 446-450
    • Shinoda, T.1    Ogawa, H.2    Cornelius, F.3    Toyoshima, C.4
  • 45
    • 0035893707 scopus 로고    scopus 로고
    • Interstitial pH in human skeletal muscle during and after dynamic graded exercise
    • Street, D., J. Bangsbo, and C. Juel. 2001. Interstitial pH in human skeletal muscle during and after dynamic graded exercise. J. Physiol. 537:993-998. http://dx.doi.org/10.1113/jphysiol.2001.012954
    • (2001) J. Physiol. , vol.537 , pp. 993-998
    • Street, D.1    Bangsbo, J.2    Juel, C.3
  • 47
    • 0029805540 scopus 로고    scopus 로고
    • Novel chloridedependent acid loader in the guinea-pig ventricular myocyte: part of a dual acid-loading mechanism
    • Sun, B., C.H. Leem, and R.D. Vaughan-Jones. 1996. Novel chloridedependent acid loader in the guinea-pig ventricular myocyte: part of a dual acid-loading mechanism. J. Physiol. 495:65-82.
    • (1996) J. Physiol. , vol.495 , pp. 65-82
    • Sun, B.1    Leem, C.H.2    Vaughan-Jones, R.D.3
  • 49
    • 0019801558 scopus 로고
    • Equilibrium state of ATP-driven ion pumps in relation to physiological ion concentration gradients.
    • Tanford, C. 1981. Equilibrium state of ATP-driven ion pumps in relation to physiological ion concentration gradients. J. Gen. Physiol. 77:223-229. http://dx.doi.org/10.1085/jgp.77.2.223
    • (1981) J. Gen. Physiol. , vol.77 , pp. 223-229
    • Tanford, C.1
  • 50
    • 38049138584 scopus 로고    scopus 로고
    • How processing of aspartylphosphate is coupled to lumenal gating of the ion pathway in the calcium pump.
    • Toyoshima, C., Y. Norimatsu, S. Iwasawa, T. Tsuda, and H. Ogawa. 2007. How processing of aspartylphosphate is coupled to lumenal gating of the ion pathway in the calcium pump. Proc. Natl. Acad. Sci. USA. 104:19831-19836. http://dx.doi.org/10.1073/pnas.0709978104
    • (2007) Proc. Natl. Acad. Sci. USA. , vol.104 , pp. 19831-19836
    • Toyoshima, C.1    Norimatsu, Y.2    Iwasawa, S.3    Tsuda, T.4    Ogawa, H.5
  • 51
    • 36348975209 scopus 로고    scopus 로고
    • Glutamate transporters: confining runaway excitation by shaping synaptic transmission
    • Tzingounis, A.V., and J.I. Wadiche. 2007. Glutamate transporters: confining runaway excitation by shaping synaptic transmission. Nat. Rev. Neurosci. 8:935-947. http://dx.doi.org/10.1038/nrn2274
    • (2007) Nat. Rev. Neurosci. , vol.8 , pp. 935-947
    • Tzingounis, A.V.1    Wadiche, J.I.2
  • 52
    • 55749090236 scopus 로고    scopus 로고
    • Slips, leaks and channels in glutamate transporters
    • Vandenberg, R.J., S. Huang, and R.M. Ryan. 2008. Slips, leaks and channels in glutamate transporters. Channels (Austin). 2:51-58. http://dx.doi.org/10.4161/chan.2.1.6047
    • (2008) Channels (Austin) , vol.2 , pp. 51-58
    • Vandenberg, R.J.1    Huang, S.2    Ryan, R.M.3
  • 55
    • 77954347915 scopus 로고    scopus 로고
    • The two C-terminal tyrosines stabilize occluded Na/K pump conformations containing Na or K ions.
    • Vedovato, N., and D.C. Gadsby. 2010. The two C-terminal tyrosines stabilize occluded Na/K pump conformations containing Na or K ions. J. Gen. Physiol. 136:63-82. http://dx.doi.org/10.1085/jgp.201010407
    • (2010) J. Gen. Physiol. , vol.136 , pp. 63-82
    • Vedovato, N.1    Gadsby, D.C.2
  • 57
    • 33947313161 scopus 로고    scopus 로고
    • The third sodium binding site of Na, K-ATPase is functionally linked to acidic pHactivated inward current.
    • Li, C., K. Geering, and J.-D. Horisberger. 2006. The third sodium binding site of Na, K-ATPase is functionally linked to acidic pHactivated inward current. J. Membr. Biol. 213:1-9. http://dx.doi.org/10.1007/s00232-006-0035-0
    • (2006) J. Membr. Biol. , vol.213 , pp. 1-9
    • Li, C.1    Geering, K.2    Horisberger, J.-D.3
  • 60
    • 0022471974 scopus 로고
    • Voltage dependence of Na translocation by the Na/K pump.
    • Nakao, M., and D.C. Gadsby. 1986. Voltage dependence of Na translocation by the Na/K pump. Nature. 323:628-630. http://dx.doi.org/10.1038/323628a0
    • (1986) Nature , vol.323 , pp. 628-630
    • Nakao, M.1    Gadsby, D.C.2
  • 61
    • 0024342564 scopus 로고
    • [Na] and [K] dependence of the Na/K pump current-voltage relationship in guinea pig ventricular myocytes.
    • Nakao, M., and D.C. Gadsby. 1989. [Na] and [K] dependence of the Na/K pump current-voltage relationship in guinea pig ventricular myocytes. J. Gen. Physiol. 94:539-565. http://dx.doi.org/10.1085/jgp.94.3.539
    • (1989) J. Gen. Physiol. , vol.94 , pp. 539-565
    • Nakao, M.1    Gadsby, D.C.2
  • 62
    • 0032539646 scopus 로고    scopus 로고
    • Importance of intramembrane carboxylic acids for occlusion of K+ ions at equilibrium in renal Na, K-ATPase.
    • Nielsen, J.M., P.A. Pedersen, S.J. Karlish, and P.L. Jorgensen. 1998. Importance of intramembrane carboxylic acids for occlusion of K+ ions at equilibrium in renal Na, K-ATPase. Biochemistry. 37:1961-1968. http://dx.doi.org/10.1021/bi972524q
    • (1998) Biochemistry , vol.37 , pp. 1961-1968
    • Nielsen, J.M.1    Pedersen, P.A.2    Karlish, S.J.3    Jorgensen, P.L.4
  • 67
    • 18244412410 scopus 로고    scopus 로고
    • + and membrane potential-dependent properties of the Na, K-pump.
    • + and membrane potential-dependent properties of the Na, K-pump. J. Gen. Physiol. 116:47-60. http://dx.doi.org/10.1085/jgp.116.1.47
    • (2000) J. Gen. Physiol. , vol.116 , pp. 47-60
    • Peluffo, R.D.1    Argüello, J.M.2    Berlin, J.R.3
  • 68
    • 0000760057 scopus 로고
    • The linkage of sodium, potassium, and ammonium active transport across the human erythrocyte membrane.
    • Post, R.L., and P.C. Jolly. 1957. The linkage of sodium, potassium, and ammonium active transport across the human erythrocyte membrane. Biochim. Biophys. Acta. 25:118-128. http://dx.doi.org/10.1016/0006-3002(57)90426-2
    • (1957) Biochim. Biophys. Acta. , vol.25 , pp. 118-128
    • Post, R.L.1    Jolly, P.C.2
  • 69
    • 0015523849 scopus 로고
    • Activation by adenosine triphosphate in the phosphorylation kinetics of sodium and potassium ion transport adenosine triphosphatase
    • Post, R.L., C. Hegyvary, and S. Kume. 1972. Activation by adenosine triphosphate in the phosphorylation kinetics of sodium and potassium ion transport adenosine triphosphatase. J. Biol. Chem. 247:6530-6540.
    • (1972) J. Biol. Chem. , vol.247 , pp. 6530-6540
    • Post, R.L.1    Hegyvary, C.2    Kume, S.3
  • 71
    • 0024374825 scopus 로고
    • Stoichiometry and voltage dependence of the sodium pump in voltage-clamped, internally dialyzed squid giant axon.
    • Rakowski, R.F., D.C. Gadsby, and P. De Weer. 1989. Stoichiometry and voltage dependence of the sodium pump in voltage-clamped, internally dialyzed squid giant axon. J. Gen. Physiol. 93:903-941. http://dx.doi.org/10.1085/jgp.93.5.903
    • (1989) J. Gen. Physiol. , vol.93 , pp. 903-941
    • Rakowski, R.F.1    Gadsby, D.C.2    De Weer, P.3
  • 73
    • 84857992685 scopus 로고    scopus 로고
    • Crystal structure of an asymmetric trimer of a bacterial glutamate transporter homolog.
    • Verdon, G., and O. Boudker. 2012. Crystal structure of an asymmetric trimer of a bacterial glutamate transporter homolog. Nat. Struct. Mol. Biol. 19:355-357. http://dx.doi.org/10.1038/nsmb.2233
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 355-357
    • Verdon, G.1    Boudker, O.2
  • 75
    • 33750470835 scopus 로고    scopus 로고
    • Activation of a presynaptic glutamate transporter regulates synaptic transmission through electrical signaling.
    • Veruki, M.L., S.H. Mørkve, and E. Hartveit. 2006. Activation of a presynaptic glutamate transporter regulates synaptic transmission through electrical signaling. Nat. Neurosci. 9:1388-1396. http://dx.doi.org/10.1038/nn1793
    • (2006) Nat. Neurosci. , vol.9 , pp. 1388-1396
    • Veruki, M.L.1    Mørkve, S.H.2    Hartveit, E.3
  • 76
    • 0032483082 scopus 로고    scopus 로고
    • 2+-ATPase affects cation binding from both sides of the membrane and destabilizes the occluded enzyme forms
    • 2+-ATPase affects cation binding from both sides of the membrane and destabilizes the occluded enzyme forms. Biochemistry. 37:10961-10971. http://dx.doi.org/10.1021/bi9802925
    • (1998) Biochemistry , vol.37 , pp. 10961-10971
    • Vilsen, B.1    Andersen, J.P.2
  • 77
    • 0342684456 scopus 로고    scopus 로고
    • Ischemia-induced changes in the extracellular space diffusion parameters, K+, and pH in the developing rat cortex and corpus callosum.
    • Vorísek, I., and E. Syková. 1997. Ischemia-induced changes in the extracellular space diffusion parameters, K+, and pH in the developing rat cortex and corpus callosum. J. Cereb. Blood Flow Metab. 17:191-203. http://dx.doi.org/10.1097/00004647-199702000-00009
    • (1997) J. Cereb. Blood Flow Metab. , vol.17 , pp. 191-203
    • Vorísek, I.1    Syková, E.2
  • 78
    • 0032189020 scopus 로고    scopus 로고
    • Macroscopic and microscopic properties of a cloned glutamate transporter/chloride channel
    • Wadiche, J.I., and M.P. Kavanaugh. 1998. Macroscopic and microscopic properties of a cloned glutamate transporter/chloride channel. J. Neurosci. 18:7650-7661.
    • (1998) J. Neurosci. , vol.18 , pp. 7650-7661
    • Wadiche, J.I.1    Kavanaugh, M.P.2
  • 79
    • 0029142729 scopus 로고
    • Ion fluxes associated with excitatory amino acid transport.
    • Wadiche, J.I., S.G. Amara, and M.P. Kavanaugh. 1995. Ion fluxes associated with excitatory amino acid transport. Neuron. 15:721-728. http://dx.doi.org/10.1016/0896-6273(95)90159-0
    • (1995) Neuron. , vol.15 , pp. 721-728
    • Wadiche, J.I.1    Amara, S.G.2    Kavanaugh, M.P.3
  • 80
    • 0031469585 scopus 로고    scopus 로고
    • Ordered interaction of ions with Na/K-pump may confound interpretation of unidirectional fluxes.
    • Wagg, J., and D.C. Gadsby. 1997. Ordered interaction of ions with Na/K-pump may confound interpretation of unidirectional fluxes. Ann. NY Acad. Sci. 834:426-431. http://dx.doi.org/10.1111/j.1749-6632.1997.tb52290.x
    • (1997) Ann. NY Acad. Sci. , vol.834 , pp. 426-431
    • Wagg, J.1    Gadsby, D.C.2
  • 82
    • 0029089396 scopus 로고
    • Electrogenicity of the sodium transport pathway in the Na, K-ATPase probed by charge-pulse experiments.
    • Wuddel, I., and H.-J. Apell. 1995. Electrogenicity of the sodium transport pathway in the Na, K-ATPase probed by charge-pulse experiments. Biophys. J. 69:909-921. http://dx.doi.org/10.1016/S0006-3495(95)79965-9
    • (1995) Biophys. J. , vol.69 , pp. 909-921
    • Wuddel, I.1    Apell, H.-J.2
  • 83
    • 0026650314 scopus 로고
    • Changes in extracellular and intracellular pH in ischemic rabbit papillary muscle.
    • Yan, G.X., and A.G. Kléber. 1992. Changes in extracellular and intracellular pH in ischemic rabbit papillary muscle. Circ. Res. 71:460-470. http://dx.doi.org/10.1161/01.RES.71.2.460
    • (1992) Circ. Res. , vol.71 , pp. 460-470
    • Yan, G.X.1    Kléber, A.G.2
  • 84
    • 70349349159 scopus 로고    scopus 로고
    • Altered Na+ transport after an intracellular ?-subunit deletion reveals strict external sequential release of Na+ from the Na/K pump.
    • Yaragatupalli, S., J.F. Olivera, C. Gatto, and P. Artigas. 2009. Altered Na+ transport after an intracellular ?-subunit deletion reveals strict external sequential release of Na+ from the Na/K pump. Proc. Natl. Acad. Sci. USA. 106:15507-15512. http://dx.doi.org/10.1073/pnas.0903752106
    • (2009) Proc. Natl. Acad. Sci. USA. , vol.106 , pp. 15507-15512
    • Yaragatupalli, S.1    Olivera, J.F.2    Gatto, C.3    Artigas, P.4
  • 86
    • 0027266757 scopus 로고
    • 2+ pump in reconstituted proteoliposomes.
    • 2+ pump in reconstituted proteoliposomes. Biophys. J. 64:1232-1242. http://dx.doi.org/10.1016/S0006-3495(93)81489-9
    • (1993) Biophys. J. , vol.64 , pp. 1232-1242
    • Yu, X.1    Carroll, S.2    Rigaud, J.L.3    Inesi, G.4
  • 87
    • 0026672734 scopus 로고
    • Second messengers regulate endosomal acidification in Swiss 3T3 fibroblasts
    • Zen, K., J. Biwersi, N. Periasamy, and A.S. Verkman. 1992. Second messengers regulate endosomal acidification in Swiss 3T3 fibroblasts. J. Cell Biol. 119:99-110. http://dx.doi.org/10.1083/jcb.119.1.99
    • (1992) J. Cell Biol. , vol.119 , pp. 99-110
    • Zen, K.1    Biwersi, J.2    Periasamy, N.3    Verkman, A.S.4


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