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Volumn 197, Issue 2, 2004, Pages 77-90

Molecular Mechanisms of Electrogenic Sodium Bicarbonate Cotransport: Structural and Equilibrium Thermodynamic Considerations

Author keywords

Acid base; Sodium bicarbonate; Transport

Indexed keywords

ANION; BICARBONATE SODIUM COTRANSPORTER; CARBONATE DEHYDRATASE; CATION; SODIUM;

EID: 1442310966     PISSN: 00222631     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00232-003-0643-x     Document Type: Review
Times cited : (29)

References (87)
  • 1
    • 0032504160 scopus 로고    scopus 로고
    • Molecular cloning, chromosomal localization, tissue distribution, and functional expression of the human pancreatic sodium bicarbonate cotransporter
    • Abuladze, N., Lee, I., Newman, D., Hwang, J., Boorer, K., Pushkin, A., Kurtz, I. 1998a. Molecular cloning, chromosomal localization, tissue distribution, and functional expression of the human pancreatic sodium bicarbonate cotransporter. J. Biol. Chem. 273:17689-17695
    • (1998) J. Biol. Chem. , vol.273 , pp. 17689-17695
    • Abuladze, N.1    Lee, I.2    Newman, D.3    Hwang, J.4    Boorer, K.5    Pushkin, A.6    Kurtz, I.7
  • 2
    • 0031895504 scopus 로고    scopus 로고
    • Axial heterogeneity of sodium-bicarbonate cotransporter expression in the rabbit proximal tubule
    • Abuladze, N., Lee, I., Newman, D., Hwang, J., Pushkin, A., Kurtz, I. 1998b. Axial heterogeneity of sodium-bicarbonate cotransporter expression in the rabbit proximal tubule. Am. J. Physiol. 274:F628-F633
    • (1998) Am. J. Physiol. , vol.274
    • Abuladze, N.1    Lee, I.2    Newman, D.3    Hwang, J.4    Pushkin, A.5    Kurtz, I.6
  • 3
    • 0034720855 scopus 로고    scopus 로고
    • Structural organization of the human NBC1 gene: KNBC1 is transcribed from an alternative promoter in intron3
    • Abuladze, N., Song, M., Pushkin, A., Newman, D., Lee, I., Nicholas, S., Kurtz, I. 2000. Structural organization of the human NBC1 gene: kNBC1 is transcribed from an alternative promoter in intron3. Gene 251:109-122
    • (2000) Gene , vol.251 , pp. 109-122
    • Abuladze, N.1    Song, M.2    Pushkin, A.3    Newman, D.4    Lee, I.5    Nicholas, S.6    Kurtz, I.7
  • 4
    • 0026070573 scopus 로고
    • The band 3-related anion exchanger (AE) gene family
    • Alper, S.L. 1991. The band 3-related anion exchanger (AE) gene family. Annu. Rev. Physiol. 53:549-564
    • (1991) Annu. Rev. Physiol. , vol.53 , pp. 549-564
    • Alper, S.L.1
  • 6
    • 0035200361 scopus 로고    scopus 로고
    • Immunolocalization of electrogenic sodium-bicarbonate cotransporters pNBC1 and kNBC1 in the rat eye
    • Bok, D., Schibler, M.J., Pushkin, A., Sassani, P., Abuladze, N., Naser, Z., Kurtz, I. 2001. Immunolocalization of electrogenic sodium-bicarbonate cotransporters pNBC1 and kNBC1 in the rat eye. Am. J. Physiol. 281:F920-F935
    • (2001) Am. J. Physiol. , vol.281
    • Bok, D.1    Schibler, M.J.2    Pushkin, A.3    Sassani, P.4    Abuladze, N.5    Naser, Z.6    Kurtz, I.7
  • 7
    • 0029560884 scopus 로고
    • Depletion of intercalated cells from collecting ducts of carbonic anhydrase II-deficient (CAR2 null) mice
    • Breton, S., Alper, S.L., Gluck, S.L., Sly, W.S., Barker, J.E., Brown, D. 1995. Depletion of intercalated cells from collecting ducts of carbonic anhydrase II-deficient (CAR2 null) mice. Am. J. Physiol. 269:F761-F774
    • (1995) Am. J. Physiol. , vol.269
    • Breton, S.1    Alper, S.L.2    Gluck, S.L.3    Sly, W.S.4    Barker, J.E.5    Brown, D.6
  • 9
    • 0032452006 scopus 로고    scopus 로고
    • Anion exchangers in the red cell and beyond
    • Casey, J.R., Reithmeier, R.A. 1998. Anion exchangers in the red cell and beyond. Biochem. Cell Biol. 76:709-713
    • (1998) Biochem. Cell Biol. , vol.76 , pp. 709-713
    • Casey, J.R.1    Reithmeier, R.A.2
  • 12
    • 0030664037 scopus 로고    scopus 로고
    • A conserved cytoplasmic region of ROMK modulates pH sensitivity, conductance, and gating
    • Choe, H., Zhou, H., Palmer, L.G., Sackin, H. 1997. A conserved cytoplasmic region of ROMK modulates pH sensitivity, conductance, and gating. Am. J. Physiol. 273:F516-F529
    • (1997) Am. J. Physiol. , vol.273
    • Choe, H.1    Zhou, H.2    Palmer, L.G.3    Sackin, H.4
  • 13
    • 0034213239 scopus 로고    scopus 로고
    • An electroneutral sodium/bicarbonate cotransporter NBCn1 and associated sodium channel
    • Choi, I., Aalkjaer, C., Boulpaep, E.L., Boron, W.F. 2000. An electroneutral sodium/bicarbonate cotransporter NBCn1 and associated sodium channel. Nature. 405:571-575
    • (2000) Nature , vol.405 , pp. 571-575
    • Choi, I.1    Aalkjaer, C.2    Boulpaep, E.L.3    Boron, W.F.4
  • 15
    • 0028844553 scopus 로고
    • Identification and molecular localization of a pH-sensing domain for the inward rectifier potassium channel HIR
    • Coulter, K.L., Perier, F., Radeke, C.M., Vandenberg, C.A. 1995. Identification and molecular localization of a pH-sensing domain for the inward rectifier potassium channel HIR. Neuron. 15:1157-1168
    • (1995) Neuron , vol.15 , pp. 1157-1168
    • Coulter, K.L.1    Perier, F.2    Radeke, C.M.3    Vandenberg, C.A.4
  • 18
    • 0027419744 scopus 로고
    • Role of the charge pair aspartic acid-237-lysine-358 in the lactose permease of Escherichia coli
    • Dunten, R.L., Sahin-Toth, M., Kaback, H.R. 1993. Role of the charge pair aspartic acid-237-lysine-358 in the lactose permease of Escherichia coli. Biochemistry 32:3139-3145
    • (1993) Biochemistry , vol.32 , pp. 3139-3145
    • Dunten, R.L.1    Sahin-Toth, M.2    Kaback, H.R.3
  • 19
    • 0032544693 scopus 로고    scopus 로고
    • In the uncoupling protein (UCP-1) His-214 is involved in the regulation of purine nucleoside triphosphate but not diphosphate binding
    • Echtay, K.S., Bienengraeber, M., Winkler, E., Klingenberg, M. 1998. In the uncoupling protein (UCP-1) His-214 is involved in the regulation of purine nucleoside triphosphate but not diphosphate binding. J. Biol. Chem. 273:24368-24374
    • (1998) J. Biol. Chem. , vol.273 , pp. 24368-24374
    • Echtay, K.S.1    Bienengraeber, M.2    Winkler, E.3    Klingenberg, M.4
  • 21
    • 0028339673 scopus 로고
    • Acid-base interactions during exocrine pancreatic secretion. Primary role for ductal bicarbonate in acinar lumen function
    • Freedman, S.D., Scheele, G.A. 1994. Acid-base interactions during exocrine pancreatic secretion. Primary role for ductal bicarbonate in acinar lumen function. Ann. N. Y. Acad. Sci. 713:199-206
    • (1994) Ann. N. Y. Acad. Sci. , vol.713 , pp. 199-206
    • Freedman, S.D.1    Scheele, G.A.2
  • 24
    • 0038718908 scopus 로고    scopus 로고
    • Phosphorylation-induced modulation of pNBC1 function: Distinct roles for the amino- and carboxy-termini
    • Gross, E., Fedotoff, O., Pushkin, A., Abuladze, N., Newman, D., Kurtz, I. 2003. Phosphorylation-induced modulation of pNBC1 function: distinct roles for the amino- and carboxy-termini. J. Physiol. 549:673-682
    • (2003) J. Physiol. , vol.549 , pp. 673-682
    • Gross, E.1    Fedotoff, O.2    Pushkin, A.3    Abuladze, N.4    Newman, D.5    Kurtz, I.6
  • 25
    • 0035868935 scopus 로고    scopus 로고
    • The stoichiometry of the electrogenic sodium bicarbonate cotransporter NBC1 is cell-type dependent
    • Gross, E., Hawkins, K., Abuladze, N., Pushkin, A., Cotton, C.U., Hopfer, U., Kurtz, I. 2001b. The stoichiometry of the electrogenic sodium bicarbonate cotransporter NBC1 is cell-type dependent. J. Physiol. 531:597-603
    • (2001) J. Physiol. , vol.531 , pp. 597-603
    • Gross, E.1    Hawkins, K.2    Abuladze, N.3    Pushkin, A.4    Cotton, C.U.5    Hopfer, U.6    Kurtz, I.7
  • 27
    • 0031824110 scopus 로고    scopus 로고
    • - cotransporter kinetics in renal proximal tubule cells
    • - cotransporter kinetics in renal proximal tubule cells. Biophys J. 75:810-824
    • (1998) Biophys. J. , vol.75 , pp. 810-824
    • Gross, E.1    Hopfer, U.2
  • 28
    • 0033001867 scopus 로고    scopus 로고
    • - cotransporter in renal proximal tubule
    • - cotransporter in renal proximal tubule. Biophys J. 76:3066-3075
    • (1999) Biophys. J. , vol.76 , pp. 3066-3075
    • Gross, E.1    Hopfer, U.2
  • 30
    • 0025217677 scopus 로고
    • Regulation of isocitrate dehydrogenase by phosphorylation involves no long-range conformational change in the free enzyme
    • Hurley, J.H., Dean, A.M., Thorsness, P.E., Koshland, D.E. Jr, Stroud, R.M. 1990. Regulation of isocitrate dehydrogenase by phosphorylation involves no long-range conformational change in the free enzyme. J. Biol. Chem. 265:3599-35602
    • (1990) J. Biol. Chem. , vol.265 , pp. 3599-35602
    • Hurley, J.H.1    Dean, A.M.2    Thorsness, P.E.3    Koshland Jr., D.E.4    Stroud, R.M.5
  • 31
    • 0032546477 scopus 로고    scopus 로고
    • Molecular cloning of a new sodium bicarbonate cotransporter cDNA from human retina
    • Ishibashi, K., Sasaki, S., Marumo, F. 1998. Molecular cloning of a new sodium bicarbonate cotransporter cDNA from human retina. Biochem. Biophys. Res. Commun. 246:535-538
    • (1998) Biochem. Biophys. Res. Commun. , vol.246 , pp. 535-538
    • Ishibashi, K.1    Sasaki, S.2    Marumo, F.3
  • 32
    • 0023715210 scopus 로고
    • Modification of a carboxyl group that appears to cross the permeability barrier in the red blood cell anion transporter
    • Jennings, M.L., Al-Rhaiyel, S. 1988. Modification of a carboxyl group that appears to cross the permeability barrier in the red blood cell anion transporter. J. Gen. Physiol. 92:161-178
    • (1988) J. Gen. Physiol. , vol.92 , pp. 161-178
    • Jennings, M.L.1    Al-Rhaiyel, S.2
  • 33
    • 0023203804 scopus 로고
    • Chemical modification and labeling of glutamate residues at the stilbenedisulfonate site of human red blood cell band 3 protein
    • Jennings, M.L., Anderson, M.P. 1987. Chemical modification and labeling of glutamate residues at the stilbenedisulfonate site of human red blood cell band 3 protein. J. Biol. Chem. 262:1691-1697
    • (1987) J. Biol. Chem. , vol.262 , pp. 1691-1697
    • Jennings, M.L.1    Anderson, M.P.2
  • 34
    • 0026689374 scopus 로고
    • Anion-proton cotransport through the human red blood cell band 3 protein. Role of glutamate 681
    • Jennings, M.L., Smith, J.S. 1992. Anion-proton cotransport through the human red blood cell band 3 protein. Role of glutamate 681. J. Biol. Chem. 267:13964-13971
    • (1992) J. Biol. Chem. , vol.267 , pp. 13964-13971
    • Jennings, M.L.1    Smith, J.S.2
  • 35
    • 0030934771 scopus 로고    scopus 로고
    • Molecular dissection of gating in the ClC-2 chloride channel
    • Jordt, S.E., Jentsch, T.J. 1997. Molecular dissection of gating in the ClC-2 chloride channel. EMBO J. 16:1582-1592
    • (1997) EMBO J. , vol.16 , pp. 1582-1592
    • Jordt, S.E.1    Jentsch, T.J.2
  • 36
    • 0034608878 scopus 로고    scopus 로고
    • Acid potentiation of the capsaicin receptor determined by a key extracellular site
    • Jordt, S.E., Tominaga, M., Julius, D. 2000. Acid potentiation of the capsaicin receptor determined by a key extracellular site. Proc. Natl. Acad. Sci. 97:8134-819
    • (2000) Proc. Natl. Acad. Sci. , vol.97 , pp. 8134-8819
    • Jordt, S.E.1    Tominaga, M.2    Julius, D.3
  • 37
    • 0027211134 scopus 로고
    • Interaction between red cell membrane band 3 and cytosolic carbonic anhydrase
    • Kifor, G., Toon, M.R., Janoshazi, A., Solomon, A.K. 1993. Interaction between red cell membrane band 3 and cytosolic carbonic anhydrase. J. Membrane Biol. 134:169-179
    • (1993) J. Membrane Biol. , vol.134 , pp. 169-179
    • Kifor, G.1    Toon, M.R.2    Janoshazi, A.3    Solomon, A.K.4
  • 39
    • 0001623359 scopus 로고    scopus 로고
    • Correction of renal tubular acidosis in carbonic anhydrase II-deficient mice with gene therapy
    • Lai, L.W., Chan, D.M., Erickson, R.P., Hsu, S.J., Lien, Y.H. 1998. Correction of renal tubular acidosis in carbonic anhydrase II-deficient mice with gene therapy. J. Clin. Invest. 101:1320-1325
    • (1998) J. Clin. Invest. , vol.101 , pp. 1320-1325
    • Lai, L.W.1    Chan, D.M.2    Erickson, R.P.3    Hsu, S.J.4    Lien, Y.H.5
  • 40
    • 0027203537 scopus 로고
    • Lysine 319 interacts with both glutamic acid 269 and aspartic acid 240 in the lactose carrier of Escherichia coli
    • Lee, J.I., Hwang, P.P., Wilson, T.H. 1993. Lysine 319 interacts with both glutamic acid 269 and aspartic acid 240 in the lactose carrier of Escherichia coli. J. Biol. Chem. 268:20007-20015
    • (1993) J. Biol. Chem. , vol.268 , pp. 20007-20015
    • Lee, J.I.1    Hwang, P.P.2    Wilson, T.H.3
  • 43
    • 0018988633 scopus 로고
    • Bicarbonate transport by proximal tubules: Effect of parathyroid hormone and dibutyryl cyclic AMP
    • McKinney, T.D., Myers, P. 1980a. Bicarbonate transport by proximal tubules: effect of parathyroid hormone and dibutyryl cyclic AMP. Am. J. Physiol. 238:F166-F174
    • (1980) Am. J. Physiol. , vol.238
    • McKinney, T.D.1    Myers, P.2
  • 44
    • 0019049599 scopus 로고
    • PTH inhibition of bicarbonate transport by proximal convoluted tubules
    • McKinney, T.D., Myers, P. 1980b. PTH inhibition of bicarbonate transport by proximal convoluted tubules. Am. J. Physiol. 239:F127-F134
    • (1980) Am. J. Physiol. , vol.239
    • McKinney, T.D.1    Myers, P.2
  • 46
    • 0029155295 scopus 로고
    • Roles of histidine 752 and glutamate 699 in the pH dependence of mouse band 3 protein-mediated anion transport
    • Muller-Berger, S., Karbach, D., Kang, D., Aranibar, N., Wood, P.G., Ruterjans, H., Passow, H. 1995. Roles of histidine 752 and glutamate 699 in the pH dependence of mouse band 3 protein-mediated anion transport. Biochemistry 34:9325-9332
    • (1995) Biochemistry , vol.34 , pp. 9325-9332
    • Muller-Berger, S.1    Karbach, D.2    Kang, D.3    Aranibar, N.4    Wood, P.G.5    Ruterjans, H.6    Passow, H.7
  • 49
    • 0030766463 scopus 로고    scopus 로고
    • Renal tubular acidosis and osteopetrosis with carbonic anhydrase II deficiency: Pathogenesis of impaired acidification
    • Nagai, R., Kooh, S.W., Balfe, J.W., Fenton, T., Halperin, M.L. 1997. Renal tubular acidosis and osteopetrosis with carbonic anhydrase II deficiency: pathogenesis of impaired acidification. Ped. Nephrol. 11:633-636
    • (1997) Ped. Nephrol. , vol.11 , pp. 633-636
    • Nagai, R.1    Kooh, S.W.2    Balfe, J.W.3    Fenton, T.4    Halperin, M.L.5
  • 51
    • 0011016829 scopus 로고    scopus 로고
    • Characterization of human "AE4" as an electroneutral sodium bicarbonate cotransporter
    • Parker, M.D., Boron, W.F., Tanner, M.J. 2002. Characterization of human "AE4" as an electroneutral sodium bicarbonate cotransporter. FASEB J. 16:A796
    • (2002) FASEB J. , vol.16
    • Parker, M.D.1    Boron, W.F.2    Tanner, M.J.3
  • 52
    • 0034801435 scopus 로고    scopus 로고
    • Human BTR1, a new bicarbonate transporter superfamily member and human AE4 from kidney
    • Parker, M.D., Ourmozdi, E.P., Tanner, M.J. 2001. Human BTR1, a new bicarbonate transporter superfamily member and human AE4 from kidney. Biochem. Biophys. Res. Commun. 282:1103-1109
    • (2001) Biochem. Biophys. Res. Commun. , vol.282 , pp. 1103-1109
    • Parker, M.D.1    Ourmozdi, E.P.2    Tanner, M.J.3
  • 53
    • 0016586549 scopus 로고
    • Ion-membrane interactions as structural forces
    • Parsegian, VA. 1975. Ion-membrane interactions as structural forces. Ann. N. Y. Acad. Sci. 264:161-171
    • (1975) Ann. N. Y. Acad. Sci. , vol.264 , pp. 161-171
    • Parsegian, V.A.1
  • 54
    • 0021804775 scopus 로고
    • Sulphate sequestered in the sulphate-binding protein of Salmonella typhimurium is bound solely by hydrogen bonds
    • Pflugrath, J.W., Quiocho, F.A. 1985. Sulphate sequestered in the sulphate-binding protein of Salmonella typhimurium is bound solely by hydrogen bonds. Nature 314:257-260
    • (1985) Nature , vol.314 , pp. 257-260
    • Pflugrath, J.W.1    Quiocho, F.A.2
  • 55
    • 0024278240 scopus 로고
    • The 2 Å resolution structure of the sulfate-binding protein involved in active transport in Salmonella typhimurium
    • Pflugrath, J.W., Quiocho, F.A. 1988. The 2 Å resolution structure of the sulfate-binding protein involved in active transport in Salmonella typhimurium. J. Mol. Biol. 200:163-180
    • (1988) J. Mol. Biol. , vol.200 , pp. 163-180
    • Pflugrath, J.W.1    Quiocho, F.A.2
  • 58
  • 59
    • 0033523090 scopus 로고    scopus 로고
    • Cloning, tissue distribution, genomic organization, and functional characterization of NBC: A new member of the sodium bicarbonate cotransporter family
    • Pushkin, A., Abuladze, N., Lee, I., Newman, D., Hwang, J., Kurtz, I I., 1999b. Cloning, tissue distribution, genomic organization, and functional characterization of NBC: A new member of the sodium bicarbonate cotransporter family. J. Biol. Chem. 274: 16569-16575
    • (1999) J. Biol. Chem. , vol.274 , pp. 16569-16575
    • Pushkin, A.1    Abuladze, N.2    Lee, I.3    Newman, D.4    Hwang, J.5    Kurtz, I.I.6
  • 60
    • 0034618609 scopus 로고    scopus 로고
    • Cloning, characterization and chromosomal assignment of NBC4, a new member of the sodium bicarbonate cotransporter family
    • Pushkin, A., Abuladze, N., Newman, D., Lee, I., Xu, G., Kurtz, I. 2000a. Cloning, characterization and chromosomal assignment of NBC4, a new member of the sodium bicarbonate cotransporter family. Biochim. Biophys. Acta 1493:215-218
    • (2000) Biochim. Biophys. Acta , vol.1493 , pp. 215-218
    • Pushkin, A.1    Abuladze, N.2    Newman, D.3    Lee, I.4    Xu, G.5    Kurtz, I.6
  • 61
    • 0033788472 scopus 로고    scopus 로고
    • Two C-terminal variants of NBC4, a new member of the sodium bicarbonate cotransporter family: Cloning, characterization, and localization
    • Pushkin, A., Abuladze, N., Newman, D., Lee, I., Xu, G., Kurtz, I. 2000b. Two C-terminal variants of NBC4, a new member of the sodium bicarbonate cotransporter family: cloning, characterization, and localization. IUBMB Life 50:13-19
    • (2000) IUBMB Life , vol.50 , pp. 13-19
    • Pushkin, A.1    Abuladze, N.2    Newman, D.3    Lee, I.4    Xu, G.5    Kurtz, I.6
  • 63
    • 0028866973 scopus 로고
    • + antiporter of Escherichia coli. Cysteine (H226C) or serine (H226S) retain both normal activity and pH sensitivity, aspartate (H226D) shifts the pH profile toward basic pH, and alanine (H226A) inactivates the carrier at all pH values
    • + antiporter of Escherichia coli. Cysteine (H226C) or serine (H226S) retain both normal activity and pH sensitivity, aspartate (H226D) shifts the pH profile toward basic pH, and alanine (H226A) inactivates the carrier at all pH values. J. Biol. Chem. 270:26813-26817
    • (1995) J. Biol. Chem. , vol.270 , pp. 26813-26817
    • Rimon, A.1    Gerchman, Y.2    Olami, Y.3    Schuldiner, S.4    Padan, E.5
  • 65
    • 0027382884 scopus 로고
    • Properties of interacting aspartic acid and lysine residues in the lactose permease of Escherichia coli
    • Sahin-Toth, M., Kaback, H.R. 1993. Properties of interacting aspartic acid and lysine residues in the lactose permease of Escherichia coli. Biochemistry 32:10027-10035
    • (1993) Biochemistry , vol.32 , pp. 10027-10035
    • Sahin-Toth, M.1    Kaback, H.R.2
  • 69
    • 0030595365 scopus 로고    scopus 로고
    • A cluster of cytoplasmic histidine residues specifies pH dependence of the AE2 plasma membrane anion exchanger
    • Sekler, I., Kobayashi, S., Kopito, R.R. 1996. A cluster of cytoplasmic histidine residues specifies pH dependence of the AE2 plasma membrane anion exchanger. Cell 86:929-935
    • (1996) Cell , vol.86 , pp. 929-935
    • Sekler, I.1    Kobayashi, S.2    Kopito, R.R.3
  • 70
    • 0028882542 scopus 로고
    • A conserved glutamate is responsible for ion selectivity and pH dependence of the mammalian anion exchangers AE1 and AE2
    • Sekler, I., Lo, R.S., Kopito, R.R. 1995. A conserved glutamate is responsible for ion selectivity and pH dependence of the mammalian anion exchangers AE1 and AE2. J. Biol. Chem. 270:28751-28758
    • (1995) J. Biol. Chem. , vol.270 , pp. 28751-28758
    • Sekler, I.1    Lo, R.S.2    Kopito, R.R.3
  • 72
    • 0035930581 scopus 로고    scopus 로고
    • A transport metabolon. Functional interaction of carbonic anhydrase II and chloride/bicarbonate exchangers
    • Sterling, D., Reithmeier, R.A., Casey, J.R. 2001. A transport metabolon. Functional interaction of carbonic anhydrase II and chloride/bicarbonate exchangers. J. Biol. Chem. 276:47886-47894
    • (2001) J. Biol. Chem. , vol.276 , pp. 47886-47894
    • Sterling, D.1    Reithmeier, R.A.2    Casey, J.R.3
  • 75
    • 0033524944 scopus 로고    scopus 로고
    • Identification of residues lining the translocation pore of human AE1, plasma membrane anion exchange protein
    • Tang, X.B., Kovacs, M., Sterling, D., Casey, J.R. 1999. Identification of residues lining the translocation pore of human AE1, plasma membrane anion exchange protein. J. Biol. Chem. 274:3557-3564
    • (1999) J. Biol. Chem. , vol.274 , pp. 3557-3564
    • Tang, X.B.1    Kovacs, M.2    Sterling, D.3    Casey, J.R.4
  • 76
    • 0037469144 scopus 로고    scopus 로고
    • Identification of membrane topography of the electrogenic sodium bicarbonate cotransporter pNBC1 by in vitro transcription/translation
    • Tatishchev, S., Abuladze, N., Pushkin, A., Newman, D., Liu, W., Weeks, D., Sachs, G., Kurtz, I. 2003. Identification of membrane topography of the electrogenic sodium bicarbonate cotransporter pNBC1 by in vitro transcription/translation. Biochemistry 42:755-765
    • (2003) Biochemistry , vol.42 , pp. 755-765
    • Tatishchev, S.1    Abuladze, N.2    Pushkin, A.3    Newman, D.4    Liu, W.5    Weeks, D.6    Sachs, G.7    Kurtz, I.8
  • 77
    • 0035504871 scopus 로고    scopus 로고
    • Cysteine-directed cross-linking localizes regions of the human erythrocyte anion-exchange protein (AE1) relative to the dimeric interface
    • Taylor, A.M., Zhu, Q., Casey, J.R. 2001. Cysteine-directed cross-linking localizes regions of the human erythrocyte anion-exchange protein (AE1) relative to the dimeric interface. Biochem. J. 359:661-668
    • (2001) Biochem. J. , vol.359 , pp. 661-668
    • Taylor, A.M.1    Zhu, Q.2    Casey, J.R.3
  • 78
    • 0026439856 scopus 로고
    • Involvement of histidine-2I in the pH-induced switch in porin channel size
    • Todt, J.C., McGroarty, E.J. 1992. Involvement of histidine-2I in the pH-induced switch in porin channel size. Biochemistry 131:10479-10482
    • (1992) Biochemistry , vol.131 , pp. 10479-10482
    • Todt, J.C.1    McGroarty, E.J.2
  • 80
    • 0034619277 scopus 로고    scopus 로고
    • - anion exchanger binding site to the amino-terminal region of carbonic anhydrase II
    • - anion exchanger binding site to the amino-terminal region of carbonic anhydrase II. Biochemistry 39:13344-13349
    • (2000) Biochemistry , vol.39 , pp. 13344-13349
    • Vince, J.W.1    Carlsson, U.2    Reithmeier, R.A.3
  • 83
    • 0034634583 scopus 로고    scopus 로고
    • - exchanger. Cloning, tissue distribution, and functional characterization
    • - exchanger. Cloning, tissue distribution, and functional characterization. J. Biol. Chem. 275:35486-35490
    • (2000) J. Biol. Chem. , vol.275 , pp. 35486-35490
    • Wang, C.Z.1    Yano, H.2    Nagashima, K.3    Seino, S.4
  • 86
    • 0033754410 scopus 로고    scopus 로고
    • A single residue contributes to the difference between Kir4.1 and Kir1.1 channels in pH sensitivity, rectification and single channel conductance
    • Xu, H., Yang, Z., Cui, N., Chanchevalap, S., Valesky, W.W., Jiang, C. 2000. A single residue contributes to the difference between Kir4.1 and Kir1.1 channels in pH sensitivity, rectification and single channel conductance. J. Physiol. 528:267-277
    • (2000) J. Physiol. , vol.528 , pp. 267-277
    • Xu, H.1    Yang, Z.2    Cui, N.3    Chanchevalap, S.4    Valesky, W.W.5    Jiang, C.6
  • 87
    • 0037474222 scopus 로고    scopus 로고
    • Novel topography in C-terminal region of the human plasma membrane anion exchanger, AE1
    • Zhu, Q., Lee, D.W., Casey, J.R. 2003. Novel topography in C-terminal region of the human plasma membrane anion exchanger, AE1. J. Biol. Chem. 278:3112-3120
    • (2003) J. Biol. Chem. , vol.278 , pp. 3112-3120
    • Zhu, Q.1    Lee, D.W.2    Casey, J.R.3


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