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Volumn 132, Issue 4, 2008, Pages 465-480

Steady-state function of the ubiquitous mammalian Na/H exchanger (NHE1) in relation to dimer coupling models with 2Na/2H stoichiometry

Author keywords

[No Author keywords available]

Indexed keywords

DIMER; MONOMER; PROTON; SODIUM PROTON EXCHANGE PROTEIN 1; SODIUM PROTON EXCHANGE PROTEIN 3;

EID: 53549110255     PISSN: 00221295     EISSN: 00221295     Source Type: Journal    
DOI: 10.1085/jgp.200810016     Document Type: Article
Times cited : (50)

References (49)
  • 1
    • 0019874123 scopus 로고
    • Influence of EGTA on the apparent Ca2+ affinity of Mg2+-dependent, Ca2+-stimulated ATPase in the human erythrocyte membrane
    • Al-Jobore, A., and B.D. Roufogalis. 1981. Influence of EGTA on the apparent Ca2+ affinity of Mg2+-dependent, Ca2+-stimulated ATPase in the human erythrocyte membrane. Biochim. Biophys. Acta. 645:1-9.
    • (1981) Biochim. Biophys. Acta , vol.645 , pp. 1-9
    • Al-Jobore, A.1    Roufogalis, B.D.2
  • 3
    • 0019975497 scopus 로고
    • Modifier role of internal H+ in activating the Na+-H+ exchanger in renal microvillus membrane vesicles
    • Aronson, P.S., J. Nee, and M.A. Suhm. 1982. Modifier role of internal H+ in activating the Na+-H+ exchanger in renal microvillus membrane vesicles. Nature. 299:161-163.
    • (1982) Nature , vol.299 , pp. 161-163
    • Aronson, P.S.1    Nee, J.2    Suhm, M.A.3
  • 4
    • 12144271044 scopus 로고    scopus 로고
    • Evolutionary origins of eukaryotic sodium/proton exchangers
    • Brett, C.L., M. Donowitz, and R. Rao. 2005. Evolutionary origins of eukaryotic sodium/proton exchangers. Am. J. Physiol. Cell Physiol. 288:C223-C239.
    • (2005) Am. J. Physiol. Cell Physiol , vol.288
    • Brett, C.L.1    Donowitz, M.2    Rao, R.3
  • 5
    • 0025732373 scopus 로고
    • Inhibitions of sugar transport produced by ligands binding at opposite sides of the membrane. Evidence for simultaneous occupation of the carrier by maltose and cytochalasin B
    • Carruthers, A., and A.L. Helgerson. 1991. Inhibitions of sugar transport produced by ligands binding at opposite sides of the membrane. Evidence for simultaneous occupation of the carrier by maltose and cytochalasin B. Biochemistry. 30:3907-3915.
    • (1991) Biochemistry , vol.30 , pp. 3907-3915
    • Carruthers, A.1    Helgerson, A.L.2
  • 6
    • 0025753065 scopus 로고
    • Regulation of the Na+/H+ exchanger under conditions of abolished proton gradient: Isosmotic and hyperosmotic stimulation
    • Dascalu, A., Z. Nevo, and R. Korenstein. 1991. Regulation of the Na+/H+ exchanger under conditions of abolished proton gradient: isosmotic and hyperosmotic stimulation. FEBS Lett. 282:305-309.
    • (1991) FEBS Lett , vol.282 , pp. 305-309
    • Dascalu, A.1    Nevo, Z.2    Korenstein, R.3
  • 7
    • 0029009492 scopus 로고
    • The mammalian Na+/H+ antiporters NHE-1, NHE-2, and NHE-3 are electroneutral and voltage independent, but can couple to an H+ conductance
    • Demaurex, N., J. Orlowski, G. Brisseau, M. Woodside, and S. Grinstein. 1995. The mammalian Na+/H+ antiporters NHE-1, NHE-2, and NHE-3 are electroneutral and voltage independent, but can couple to an H+ conductance. J. Gen. Physiol. 106:85-111.
    • (1995) J. Gen. Physiol , vol.106 , pp. 85-111
    • Demaurex, N.1    Orlowski, J.2    Brisseau, G.3    Woodside, M.4    Grinstein, S.5
  • 8
    • 0034503095 scopus 로고    scopus 로고
    • Direct binding of the Na-H exchanger NHE1 to ERM proteins regulates the cortical cytoskeleton and cell shape independently of H(+) translocation
    • Denker, S.P., D.C. Huang, J. Orlowski, H. Furthmayr, and D.L. Barber. 2000. Direct binding of the Na-H exchanger NHE1 to ERM proteins regulates the cortical cytoskeleton and cell shape independently of H(+) translocation. Mol. Cell. 6:1425-1436.
    • (2000) Mol. Cell , vol.6 , pp. 1425-1436
    • Denker, S.P.1    Huang, D.C.2    Orlowski, J.3    Furthmayr, H.4    Barber, D.L.5
  • 9
    • 0023257555 scopus 로고
    • Estimation of the number and turnover rate of Na+/H+ exchangers in lymphocytes. Effect of phorbol ester and osmotic shrinking
    • Dixon, S.J., S. Cohen, E.J. Cragoe Jr., and S. Grinstein. 1987. Estimation of the number and turnover rate of Na+/H+ exchangers in lymphocytes. Effect of phorbol ester and osmotic shrinking. J. Biol. Chem. 262:3626-3632.
    • (1987) J. Biol. Chem , vol.262 , pp. 3626-3632
    • Dixon, S.J.1    Cohen, S.2    Cragoe Jr., E.J.3    Grinstein, S.4
  • 10
    • 0025768888 scopus 로고
    • Sodium dependence of sodium-proton exchange in platelets from patients with essential hypertension
    • Doktor, H.S., N. Benjamin, S.D. Todd, and J.M. Ritter. 1991. Sodium dependence of sodium-proton exchange in platelets from patients with essential hypertension. J. Hum. Hypertens. 5:161-165.
    • (1991) J. Hum. Hypertens , vol.5 , pp. 161-165
    • Doktor, H.S.1    Benjamin, N.2    Todd, S.D.3    Ritter, J.M.4
  • 11
    • 3142777645 scopus 로고    scopus 로고
    • Lipid- and mechanosensitivities of sodium/hydrogen exchangers analyzed by electrical methods
    • Fuster, D., O.W. Moe, and D.W. Hilgemann. 2004. Lipid- and mechanosensitivities of sodium/hydrogen exchangers analyzed by electrical methods. Proc. Natl. Acad. Sci. USA. 101:10482-10487.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 10482-10487
    • Fuster, D.1    Moe, O.W.2    Hilgemann, D.W.3
  • 12
    • 0023819546 scopus 로고
    • Cytosolic pH regulation in osteoblasts. Interaction of Na+ and H+ with the extracellular and intracellular faces of the Na+/H+ exchanger
    • Green, J., D.T. Yamaguchi, C.R. Kleeman, and S. Muallem. 1988. Cytosolic pH regulation in osteoblasts. Interaction of Na+ and H+ with the extracellular and intracellular faces of the Na+/H+ exchanger. J. Gen. Physiol. 92:239-261.
    • (1988) J. Gen. Physiol , vol.92 , pp. 239-261
    • Green, J.1    Yamaguchi, D.T.2    Kleeman, C.R.3    Muallem, S.4
  • 13
    • 0032319507 scopus 로고    scopus 로고
    • Giant membrane patches: Improvements and applications
    • Hilgemann, D.W., and C.C. Lu. 1998. Giant membrane patches: improvements and applications. Methods Enzymol. 293:267-280.
    • (1998) Methods Enzymol , vol.293 , pp. 267-280
    • Hilgemann, D.W.1    Lu, C.C.2
  • 15
    • 4644271441 scopus 로고    scopus 로고
    • Dimeric interaction between the cytoplasmic domains of the Na+/H+ exchanger NHE1 revealed by symmetrical intermolecular cross-linking and selective co-immunoprecipitation
    • Hisamitsu, T., T. Pang, M. Shigekawa, and S. Wakabayashi. 2004. Dimeric interaction between the cytoplasmic domains of the Na+/H+ exchanger NHE1 revealed by symmetrical intermolecular cross-linking and selective co-immunoprecipitation. Biochemistry. 43:11135-11143.
    • (2004) Biochemistry , vol.43 , pp. 11135-11143
    • Hisamitsu, T.1    Pang, T.2    Shigekawa, M.3    Wakabayashi, S.4
  • 16
    • 33750713348 scopus 로고    scopus 로고
    • Dimerization is crucial for the function of the Na+/H+ exchanger NHE1
    • Hisamitsu, T., A.Y. Ben, T.Y. Nakamura, and S. Wakabayashi. 2006 Dimerization is crucial for the function of the Na+/H+ exchanger NHE1. Biochemistry. 45:13346-13355.
    • (2006) Biochemistry , vol.45 , pp. 13346-13355
    • Hisamitsu, T.1    Ben, A.Y.2    Nakamura, T.Y.3    Wakabayashi, S.4
  • 17
    • 21744436321 scopus 로고    scopus 로고
    • Structure of a Na+/H+ antiporter and insights into mechanism of action and regulation by pH
    • Hunte, C., E. Screpanti, M. Venturi, A. Rimon, E. Padan, and H. Michel. 2005. Structure of a Na+/H+ antiporter and insights into mechanism of action and regulation by pH. Nature 435:1197-1202.
    • (2005) Nature , vol.435 , pp. 1197-1202
    • Hunte, C.1    Screpanti, E.2    Venturi, M.3    Rimon, A.4    Padan, E.5    Michel, H.6
  • 18
    • 0033578328 scopus 로고    scopus 로고
    • Na(+)-H(+) exchange in salivary secretory cells is controlled by an intracellular Na(+) receptor
    • Ishibashi, H., A. Dinudom, K.F. Harvey, S. Kumar, J.A. Young, and D.I. Cook. 1999. Na(+)-H(+) exchange in salivary secretory cells is controlled by an intracellular Na(+) receptor. Proc. Natl. Acad. Sci. USA. 96:9949-9953.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 9949-9953
    • Ishibashi, H.1    Dinudom, A.2    Harvey, K.F.3    Kumar, S.4    Young, J.A.5    Cook, D.I.6
  • 19
    • 0021837193 scopus 로고
    • Biochemical properties of the Na+/H+ exchange system in rat brain synaptosomes. Interdependence of internal and external pH control of the exchange activity
    • Jean, T., C. Frelin, P. Vigne, P. Barbry, and M. Lazdunski. 1985 Biochemical properties of the Na+/H+ exchange system in rat brain synaptosomes. Interdependence of internal and external pH control of the exchange activity. J. Biol. Chem. 260:9678-9684.
    • (1985) J. Biol. Chem , vol.260 , pp. 9678-9684
    • Jean, T.1    Frelin, C.2    Vigne, P.3    Barbry, P.4    Lazdunski, M.5
  • 20
    • 0037388654 scopus 로고    scopus 로고
    • Ion fluxes in giant excised cardiac membrane patches detected and quantified with ion-selective microelectrodes
    • Kang, T.M., V.S. Markin, and D.W. Hilgemann. 2003. Ion fluxes in giant excised cardiac membrane patches detected and quantified with ion-selective microelectrodes. J. Gen. Physiol. 121:325-347.
    • (2003) J. Gen. Physiol , vol.121 , pp. 325-347
    • Kang, T.M.1    Markin, V.S.2    Hilgemann, D.W.3
  • 21
    • 0020482239 scopus 로고
    • Determination of the coupling ratio for Na+ -H+ exchange in renal microvillus membrane vesicles
    • Kinsella, J.L., and P.S. Aronson. 1982. Determination of the coupling ratio for Na+ -H+ exchange in renal microvillus membrane vesicles. Biochim. Biophys. Acta. 689:161-164.
    • (1982) Biochim. Biophys. Acta , vol.689 , pp. 161-164
    • Kinsella, J.L.1    Aronson, P.S.2
  • 22
    • 0032452007 scopus 로고    scopus 로고
    • Na+/H+ exchanger: Proton modifier site regulation of activity
    • Kinsella, J.L., P. Heller, and J.P. Froehlich. 1998. Na+/H+ exchanger: proton modifier site regulation of activity. Biochem. Cell Biol. 76:743-749.
    • (1998) Biochem. Cell Biol , vol.76 , pp. 743-749
    • Kinsella, J.L.1    Heller, P.2    Froehlich, J.P.3
  • 23
    • 0020600630 scopus 로고
    • Activation of an islet cell plasma membrane (Ca2+ + Mg2+)-ATPase by calmodulin and Ca-EGTA
    • Kotagal, N., J.R. Colca, and M.L. McDaniel. 1983. Activation of an islet cell plasma membrane (Ca2+ + Mg2+)-ATPase by calmodulin and Ca-EGTA. J. Biol. Chem. 258:4808-4813.
    • (1983) J. Biol. Chem , vol.258 , pp. 4808-4813
    • Kotagal, N.1    Colca, J.R.2    McDaniel, M.L.3
  • 24
    • 1242321029 scopus 로고    scopus 로고
    • A mechanism for the activation of the Na/H exchanger NHE-1 by cytoplasmic acidification and mitogens
    • 5:91-96
    • Lacroix, J., M. Poet, C. Maehrel, and L. Counillon. 2004. A mechanism for the activation of the Na/H exchanger NHE-1 by cytoplasmic acidification and mitogens. EMBO Rep. 5:91-96.
    • (2004) EMBO Rep
    • Lacroix, J.1    Poet, M.2    Maehrel, C.3    Counillon, L.4
  • 25
    • 0023493787 scopus 로고
    • Voltage dependence of sodium-calcium exchange: Predictions from kinetic models
    • Lauger, P. 1987. Voltage dependence of sodium-calcium exchange: predictions from kinetic models. J. Membr. Biol. 99:1-11.
    • (1987) J. Membr. Biol , vol.99 , pp. 1-11
    • Lauger, P.1
  • 26
    • 0027525551 scopus 로고
    • Kinetics and regulation of three cloned mammalian Na+/H+ exchangers stably expressed in a fibroblast cell line
    • Levine, S.A., M.H. Montrose, C.M. Tse, and M. Donowitz. 1993 Kinetics and regulation of three cloned mammalian Na+/H+ exchangers stably expressed in a fibroblast cell line. J. Biol. Chem. 268:25527-25535.
    • (1993) J. Biol. Chem , vol.268 , pp. 25527-25535
    • Levine, S.A.1    Montrose, M.H.2    Tse, C.M.3    Donowitz, M.4
  • 27
    • 34250683573 scopus 로고    scopus 로고
    • Beyond ion translocation: Structural functions of the sodium-hydrogen exchanger isoform-1
    • Meima, M.E., J.R. Mackley, and D.L. Barber. 2007. Beyond ion translocation: structural functions of the sodium-hydrogen exchanger isoform-1. Curr. Opin. Nephrol. Hypertens. 16:365-372.
    • (2007) Curr. Opin. Nephrol. Hypertens , vol.16 , pp. 365-372
    • Meima, M.E.1    Mackley, J.R.2    Barber, D.L.3
  • 28
    • 42949152545 scopus 로고    scopus 로고
    • Dimeric structure of human Na+/H+ exchanger isoform 1 overproduced in Saccharomyces cerevisiae
    • Moncoq, K., G. Kemp, X. Li, L. Fliegel, and H.S. Young. 2008. Dimeric structure of human Na+/H+ exchanger isoform 1 overproduced in Saccharomyces cerevisiae. J. Biol. Chem. 283:4145-4154.
    • (2008) J. Biol. Chem , vol.283 , pp. 4145-4154
    • Moncoq, K.1    Kemp, G.2    Li, X.3    Fliegel, L.4    Young, H.S.5
  • 29
    • 1242272754 scopus 로고    scopus 로고
    • Diversity of the mammalian sodium/proton exchanger SLC9 gene family
    • Orlowski, J., and S. Grinstein. 2004. Diversity of the mammalian sodium/proton exchanger SLC9 gene family. Pflugers Arch. 447:549-565.
    • (2004) Pflugers Arch , vol.447 , pp. 549-565
    • Orlowski, J.1    Grinstein, S.2
  • 30
    • 34547963769 scopus 로고    scopus 로고
    • Emerging roles of alkali cation/proton exchangers in organellar homeostasis
    • Orlowski, J., and S. Grinstein. 2007. Emerging roles of alkali cation/proton exchangers in organellar homeostasis. Curr. Opin. Cell Biol. 19:483-492.
    • (2007) Curr. Opin. Cell Biol , vol.19 , pp. 483-492
    • Orlowski, J.1    Grinstein, S.2
  • 31
    • 0024314894 scopus 로고
    • Transient state kinetic evidence for an oligomer in the mechanism of Na+-H+ exchange
    • Otsu, K., J. Kinsella, B. Sacktor, and J.P. Froehlich. 1989. Transient state kinetic evidence for an oligomer in the mechanism of Na+-H+ exchange. Proc. Natl. Acad. Sci. USA. 86:4818-4822.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 4818-4822
    • Otsu, K.1    Kinsella, J.2    Sacktor, B.3    Froehlich, J.P.4
  • 32
    • 0027412188 scopus 로고
    • Sodium dependence of the Na(+)-H+ exchanger in the pre-steady state. Implications for the exchange mechanism
    • Otsu, K., J.L. Kinsella, P. Heller, and J.P. Froehlich. 1993. Sodium dependence of the Na(+)-H+ exchanger in the pre-steady state. Implications for the exchange mechanism. J. Biol. Chem. 268:3184-3193.
    • (1993) J. Biol. Chem , vol.268 , pp. 3184-3193
    • Otsu, K.1    Kinsella, J.L.2    Heller, P.3    Froehlich, J.P.4
  • 34
    • 1642414758 scopus 로고    scopus 로고
    • Role of calcineurin B homologous protein in pH regulation by the Na+/H+ exchanger 1: Tightly bound Ca2+ ions as important structural elements
    • Pang, T., T. Hisamitsu, H. Mori, M. Shigekawa, and S. Wakabayashi. 2004. Role of calcineurin B homologous protein in pH regulation by the Na+/H+ exchanger 1: tightly bound Ca2+ ions as important structural elements. Biochemistry. 43:3628-3636.
    • (2004) Biochemistry , vol.43 , pp. 3628-3636
    • Pang, T.1    Hisamitsu, T.2    Mori, H.3    Shigekawa, M.4    Wakabayashi, S.5
  • 35
    • 33646358260 scopus 로고    scopus 로고
    • A voltage-gated proton-selective channel lacking the pore domain
    • Ramsey, I.S., M.M. Moran, J.A. Chong, and D.E. Clapham. 2006. A voltage-gated proton-selective channel lacking the pore domain. Nature. 440:1213-1216.
    • (2006) Nature , vol.440 , pp. 1213-1216
    • Ramsey, I.S.1    Moran, M.M.2    Chong, J.A.3    Clapham, D.E.4
  • 36
    • 0029586449 scopus 로고
    • Alteration by EGTA of the human red cell Ca(2+)-ATPase
    • Romero, P.J., and V. Salas. 1995. Alteration by EGTA of the human red cell Ca(2+)-ATPase. Biochim. Biophys. Acta. 1240:115-117.
    • (1995) Biochim. Biophys. Acta , vol.1240 , pp. 115-117
    • Romero, P.J.1    Salas, V.2
  • 37
    • 0022999303 scopus 로고
    • Li+ as substrate of the synaptosomal Na+/H+ antiporter
    • Schmalzing, G., T. Schlosser, and P. Kutschera. 1986. Li+ as substrate of the synaptosomal Na+/H+ antiporter. J. Biol. Chem. 261:2759-2767.
    • (1986) J. Biol. Chem , vol.261 , pp. 2759-2767
    • Schmalzing, G.1    Schlosser, T.2    Kutschera, P.3
  • 38
    • 0024538849 scopus 로고
    • Kinetics and stoichiometry of the human red cell Na+/H+ exchanger
    • Semplicini, A., A. Spalvins, and M. Canessa. 1989. Kinetics and stoichiometry of the human red cell Na+/H+ exchanger. J. Membr. Biol. 107:219-228.
    • (1989) J. Membr. Biol , vol.107 , pp. 219-228
    • Semplicini, A.1    Spalvins, A.2    Canessa, M.3
  • 39
    • 33846870761 scopus 로고    scopus 로고
    • Structural and functional analysis of the Na+/H+ exchanger
    • Slepkov, E.R., J.K. Rainey, B.D. Sykes, and L. Fliegel. 2007. Structural and functional analysis of the Na+/H+ exchanger. Biochem. J. 401:623-633.
    • (2007) Biochem. J , vol.401 , pp. 623-633
    • Slepkov, E.R.1    Rainey, J.K.2    Sykes, B.D.3    Fliegel, L.4
  • 40
    • 0034995786 scopus 로고    scopus 로고
    • Noninvasive measurement of hydrogen and potassium ion flux from single cells and epithelial structures
    • Smith, P.J., and J. Trimarchi. 2001. Noninvasive measurement of hydrogen and potassium ion flux from single cells and epithelial structures. Am. J. Physiol. Cell Physiol. 280:C1-C11.
    • (2001) Am. J. Physiol. Cell Physiol , vol.280
    • Smith, P.J.1    Trimarchi, J.2
  • 41
    • 0021254471 scopus 로고
    • Stimulatory effect of calcium chelators on Na+-Ca2+ exchange in cardiac sarcolemmal vesicles
    • Trosper, T.L., and K.D. Philipson. 1984. Stimulatory effect of calcium chelators on Na+-Ca2+ exchange in cardiac sarcolemmal vesicles. Cell Calcium. 5:211-222.
    • (1984) Cell Calcium , vol.5 , pp. 211-222
    • Trosper, T.L.1    Philipson, K.D.2
  • 42
    • 0019640375 scopus 로고
    • Na+-Ca2+ exchange system and its physiological role (author ' s transl)
    • Wakabayashi, S., and K. Goshima. 1981. Na+-Ca2+ exchange system and its physiological role (author ' s transl). Tanpakushitsu Kakusan Koso. 26:2055-2069.
    • (1981) Tanpakushitsu Kakusan Koso , vol.26 , pp. 2055-2069
    • Wakabayashi, S.1    Goshima, K.2
  • 43
    • 0026582813 scopus 로고    scopus 로고
    • Wakabayashi, S., P. Fafournoux, C. Sardet, and J. Pouyssegur. 1992. The Na+/H+ antiporter cytoplasmic domain mediates growth factor signals and controls H(+)-sensing. Proc. Natl. Acad. Sci. USA. 89:2424-2428.
    • Wakabayashi, S., P. Fafournoux, C. Sardet, and J. Pouyssegur. 1992. The Na+/H+ antiporter cytoplasmic domain mediates growth factor signals and controls "H(+)-sensing." Proc. Natl. Acad. Sci. USA. 89:2424-2428.
  • 44
    • 0028100661 scopus 로고
    • Growth factor activation and "H(+)-sensing" of the Na+/H+ exchanger isoform 1 (NHE1). Evidence for an additional mechanism not requiring direct phosphorylation
    • Wakabayashi, S., B. Bertrand, M. Shigekawa, P. Fafournoux, and J. Pouyssegur. 1994. Growth factor activation and "H(+)-sensing" of the Na+/H+ exchanger isoform 1 (NHE1). Evidence for an additional mechanism not requiring direct phosphorylation. J. Biol. Chem. 269:5583-5588.
    • (1994) J. Biol. Chem , vol.269 , pp. 5583-5588
    • Wakabayashi, S.1    Bertrand, B.2    Shigekawa, M.3    Fafournoux, P.4    Pouyssegur, J.5
  • 45
    • 0030696884 scopus 로고    scopus 로고
    • Calmodulin-binding autoinhibitory domain controls "pH-sensing" in the Na+/H+ exchanger NHE1 through sequence-specific interaction
    • Wakabayashi, S., T. Ikeda, T. Iwamoto, J. Pouyssegur, and M. Shigekawa. 1997a. Calmodulin-binding autoinhibitory domain controls "pH-sensing" in the Na+/H+ exchanger NHE1 through sequence-specific interaction. Biochemistry. 36:12854-12861.
    • (1997) Biochemistry , vol.36 , pp. 12854-12861
    • Wakabayashi, S.1    Ikeda, T.2    Iwamoto, T.3    Pouyssegur, J.4    Shigekawa, M.5
  • 46
    • 0031035914 scopus 로고    scopus 로고
    • Molecular physiology of vertebrate Na+/H+ exchangers
    • Wakabayashi, S., M. Shigekawa, and J. Pouyssegur. 1997b. Molecular physiology of vertebrate Na+/H+ exchangers. Physiol. Rev. 77:51-74.
    • (1997) Physiol. Rev , vol.77 , pp. 51-74
    • Wakabayashi, S.1    Shigekawa, M.2    Pouyssegur, J.3
  • 47
    • 0242290261 scopus 로고    scopus 로고
    • Kinetic dissection of two distinct proton binding sites in Na+/H+ exchangers by measurement of reverse mode reaction
    • Wakabayashi, S., T. Hisamitsu, T. Pang, and M. Shigekawa. 2003. Kinetic dissection of two distinct proton binding sites in Na+/H+ exchangers by measurement of reverse mode reaction. J. Biol. Chem. 278:43580-43585.
    • (2003) J. Biol. Chem , vol.278 , pp. 43580-43585
    • Wakabayashi, S.1    Hisamitsu, T.2    Pang, T.3    Shigekawa, M.4
  • 48
    • 0344668550 scopus 로고    scopus 로고
    • A new sperm-specific Na+/H+ exchanger required for sperm motility and fertility
    • Wang, D., S.M. King, T.A. Quill, L.K. Doolittle, and D.L. Garbers. 2003. A new sperm-specific Na+/H+ exchanger required for sperm motility and fertility. Nat. Cell Biol. 5:1117-1122.
    • (2003) Nat. Cell Biol , vol.5 , pp. 1117-1122
    • Wang, D.1    King, S.M.2    Quill, T.A.3    Doolittle, L.K.4    Garbers, D.L.5
  • 49
    • 0031127371 scopus 로고    scopus 로고
    • Interaction between Na+ and H+ ions on Na-H exchange in sheep cardiac Purkinje fibers
    • Wu, M.L., and R.D. Vaughan-Jones. 1997. Interaction between Na+ and H+ ions on Na-H exchange in sheep cardiac Purkinje fibers. J. Mol. Cell. Cardiol. 29:1131-1140.
    • (1997) J. Mol. Cell. Cardiol , vol.29 , pp. 1131-1140
    • Wu, M.L.1    Vaughan-Jones, R.D.2


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