메뉴 건너뛰기




Volumn , Issue , 2010, Pages 43-79

From cloning to structure, function, and regulation of chloride-dependent and independent bicarbonate transporters

Author keywords

[No Author keywords available]

Indexed keywords


EID: 84882464106     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-0-12-374373-2.00004-2     Document Type: Chapter
Times cited : (5)

References (341)
  • 1
    • 0032504160 scopus 로고    scopus 로고
    • Molecular Cloning, Chromosomal Localization, Tissue Distribution, and Functional Expression of the Human Pancreatic Sodium Bicarbonate Cotransporter
    • Abuladze N., et al. Molecular Cloning, Chromosomal Localization, Tissue Distribution, and Functional Expression of the Human Pancreatic Sodium Bicarbonate Cotransporter. J. Biol. Chem. 1998, 273:17689-17695.
    • (1998) J. Biol. Chem. , vol.273 , pp. 17689-17695
    • Abuladze, N.1
  • 3
    • 0034720855 scopus 로고    scopus 로고
    • Structural organization of the human NBC1 gene: kNBC1 is transcribed from an alternative promoter in intron 3
    • Abuladze N., et al. Structural organization of the human NBC1 gene: kNBC1 is transcribed from an alternative promoter in intron 3. Gene 2000, 251:109-122.
    • (2000) Gene , vol.251 , pp. 109-122
    • Abuladze, N.1
  • 5
    • 1542288949 scopus 로고    scopus 로고
    • Secondary active transport mediated by a prokaryotic homologue of ClC Cl- channels
    • Accardi A., Miller C. Secondary active transport mediated by a prokaryotic homologue of ClC Cl- channels. Nature 2004, 427:803-807.
    • (2004) Nature , vol.427 , pp. 803-807
    • Accardi, A.1    Miller, C.2
  • 7
    • 0035907291 scopus 로고    scopus 로고
    • - salvage mechanisms in model systems and the mouse pancreatic duct
    • - salvage mechanisms in model systems and the mouse pancreatic duct. J. Biol. Chem. 2001, 276:17236-17243.
    • (2001) J. Biol. Chem. , vol.276 , pp. 17236-17243
    • Ahn, W.1
  • 8
    • 34147192135 scopus 로고    scopus 로고
    • Voltage-sensitive prestin orthologue expressed in zebrafish hair cells
    • Albert J.T., et al. Voltage-sensitive prestin orthologue expressed in zebrafish hair cells. J. Physiol. 2007, 580:451-461.
    • (2007) J. Physiol. , vol.580 , pp. 451-461
    • Albert, J.T.1
  • 9
    • 0036197399 scopus 로고    scopus 로고
    • Genetic diseases of acid-base transporters
    • Alper S.L. Genetic diseases of acid-base transporters. Annu. Rev. Physiol. 2002, 64:899-923.
    • (2002) Annu. Rev. Physiol. , vol.64 , pp. 899-923
    • Alper, S.L.1
  • 12
    • 0023760537 scopus 로고
    • Cloning and characterization of a murine band 3-related cDNA from kidney and from a lymphoid cell line
    • Alper S.L., Kopito R.R., Libresco S.M., Lodish H.F. Cloning and characterization of a murine band 3-related cDNA from kidney and from a lymphoid cell line. J. Biol. Chem. 1988, 263:17092-17099.
    • (1988) J. Biol. Chem. , vol.263 , pp. 17092-17099
    • Alper, S.L.1    Kopito, R.R.2    Libresco, S.M.3    Lodish, H.F.4
  • 16
    • 0022413879 scopus 로고
    • - transport in the rat proximal convoluted tubule. A sodium-coupled electrogenic process
    • - transport in the rat proximal convoluted tubule. A sodium-coupled electrogenic process. J. Gen. Physiol. 1985, 86:613-636.
    • (1985) J. Gen. Physiol. , vol.86 , pp. 613-636
    • Alpern, R.J.1
  • 17
    • 0002460248 scopus 로고    scopus 로고
    • Renal Acidification Mechanisms
    • W.B. Saunders Co, Philadelphia, PA, B.M. Brenner, F.C. Rector (Eds.)
    • Alpern R.J., Rector F.C. Renal Acidification Mechanisms. The kidney 1996, Vol. 1. W.B. Saunders Co, Philadelphia, PA. B.M. Brenner, F.C. Rector (Eds.).
    • (1996) The kidney , vol.1
    • Alpern, R.J.1    Rector, F.C.2
  • 18
    • 11344282403 scopus 로고    scopus 로고
    • Slc26a6: a cardiac chloride-hydroxyl exchanger and predominant chloride-bicarbonate exchanger of the mouse heart
    • Alvarez B.V., Kieller D.M., Quon A.L., Markovich D., Casey J.R. Slc26a6: a cardiac chloride-hydroxyl exchanger and predominant chloride-bicarbonate exchanger of the mouse heart. J. Physiol. 2004, 561:721-734.
    • (2004) J. Physiol. , vol.561 , pp. 721-734
    • Alvarez, B.V.1    Kieller, D.M.2    Quon, A.L.3    Markovich, D.4    Casey, J.R.5
  • 19
    • 23044434059 scopus 로고    scopus 로고
    • Metabolon disruption: a mechanism that regulates bicarbonate transport
    • Alvarez B.V., Vilas G.L., Casey J.R. Metabolon disruption: a mechanism that regulates bicarbonate transport. Embo J. 2005, 24:2499-2511.
    • (2005) Embo J. , vol.24 , pp. 2499-2511
    • Alvarez, B.V.1    Vilas, G.L.2    Casey, J.R.3
  • 20
    • 0033953284 scopus 로고    scopus 로고
    • The STAS domain - a link between anion transporters and antisigma-factor antagonists
    • Aravind L., Koonin E.V. The STAS domain - a link between anion transporters and antisigma-factor antagonists. Curr. Biol. 2000, 10:R53-R55.
    • (2000) Curr. Biol. , vol.10
    • Aravind, L.1    Koonin, E.V.2
  • 21
    • 38349152499 scopus 로고    scopus 로고
    • Cochlear outer hair cell motility
    • Ashmore J. Cochlear outer hair cell motility. Physiol. Rev. 2008, 88:173-210.
    • (2008) Physiol. Rev. , vol.88 , pp. 173-210
    • Ashmore, J.1
  • 22
    • 0024431385 scopus 로고
    • Identification by site-directed mutagenesis of Lys-558 as the covalent attachment site of H2DIDS in the mouse erythroid band 3 protein
    • Bartel D., Hans H., Passow H. Identification by site-directed mutagenesis of Lys-558 as the covalent attachment site of H2DIDS in the mouse erythroid band 3 protein. Biochim. Biophys. Acta. 1989, 985:355-358.
    • (1989) Biochim. Biophys. Acta. , vol.985 , pp. 355-358
    • Bartel, D.1    Hans, H.2    Passow, H.3
  • 23
    • 0024804353 scopus 로고
    • Anion transport in oocytes of Xenopus laevis induced by expression of mouse erythroid band 3 protein--encoding cRNA and of a cRNA derivative obtained by site-directed mutagenesis at the stilbene disulfonate binding site
    • Bartel D., Lepke S., Layh-Schmitt G., Legrum B., Passow H. Anion transport in oocytes of Xenopus laevis induced by expression of mouse erythroid band 3 protein--encoding cRNA and of a cRNA derivative obtained by site-directed mutagenesis at the stilbene disulfonate binding site. Embo J. 1989, 8:3601-3609.
    • (1989) Embo J. , vol.8 , pp. 3601-3609
    • Bartel, D.1    Lepke, S.2    Layh-schmitt, G.3    Legrum, B.4    Passow, H.5
  • 24
    • 0018759156 scopus 로고
    • Anion transport in red blood cells. I. Chemical properties of anion recognition sites as revealed by structure-activity relationships of aromatic sulfonic acids
    • Barzilay M., Ship S., Cabantchik Z.I. Anion transport in red blood cells. I. Chemical properties of anion recognition sites as revealed by structure-activity relationships of aromatic sulfonic acids. Membr. Biochem. 1979, 2:227-254.
    • (1979) Membr. Biochem. , vol.2 , pp. 227-254
    • Barzilay, M.1    Ship, S.2    Cabantchik, Z.I.3
  • 26
    • 0346688718 scopus 로고    scopus 로고
    • Facilitated Lactate Transport by MCT1 when Coexpressed with the Sodium Bicarbonate Cotransporter (NBC) in Xenopus Oocytes
    • Becker H.M., Broer S., Deitmer J.W. Facilitated Lactate Transport by MCT1 when Coexpressed with the Sodium Bicarbonate Cotransporter (NBC) in Xenopus Oocytes. Biophys. J. 2004, 86:235-247.
    • (2004) Biophys. J. , vol.86 , pp. 235-247
    • Becker, H.M.1    Broer, S.2    Deitmer, J.W.3
  • 27
    • 3142544856 scopus 로고    scopus 로고
    • Voltage dependence of h+ buffering mediated by sodium bicarbonate cotransport expressed in Xenopus oocytes
    • Becker H.M., Deitmer J.W. Voltage dependence of h+ buffering mediated by sodium bicarbonate cotransport expressed in Xenopus oocytes. J. Biol. Chem. 2004, 279:28057-28062.
    • (2004) J. Biol. Chem. , vol.279 , pp. 28057-28062
    • Becker, H.M.1    Deitmer, J.W.2
  • 29
    • 52049118802 scopus 로고    scopus 로고
    • +-lactate cotransport via monocarboxylate transporter 1
    • +-lactate cotransport via monocarboxylate transporter 1. J. Biol. Chem. 2008, 283:21655-21667.
    • (2008) J. Biol. Chem. , vol.283 , pp. 21655-21667
    • Becker, H.M.1    Deitmer, J.W.2
  • 31
    • 0034529826 scopus 로고    scopus 로고
    • - symporter and Pendred syndrome genes in trophoblast cells
    • - symporter and Pendred syndrome genes in trophoblast cells. J. Clin. Endocrinol Metab. 2000, 85:4367-4372.
    • (2000) J. Clin. Endocrinol Metab. , vol.85 , pp. 4367-4372
    • Bidart, J.M.1
  • 32
    • 0027935348 scopus 로고
    • Functional expression cloning of the canalicular sulfate transport system of rat hepatocytes
    • Bissig M., Hagenbuch B., Stieger B., Koller T., Meier P.J. Functional expression cloning of the canalicular sulfate transport system of rat hepatocytes. J. Biol. Chem. 1994, 269:3017-3021.
    • (1994) J. Biol. Chem. , vol.269 , pp. 3017-3021
    • Bissig, M.1    Hagenbuch, B.2    Stieger, B.3    Koller, T.4    Meier, P.J.5
  • 33
    • 0035200361 scopus 로고    scopus 로고
    • Immunolocalization of electrogenic sodium-bicarbonate cotransporters pNBC1 and kNBC1 in the rat eye
    • Bok D., et al. Immunolocalization of electrogenic sodium-bicarbonate cotransporters pNBC1 and kNBC1 in the rat eye. Am. J. Physiol. Renal Physiol. 2001, 281:F920-F935.
    • (2001) Am. J. Physiol. Renal Physiol. , vol.281
    • Bok, D.1
  • 34
    • 0021319373 scopus 로고
    • Characterization of matrix-bound Band 3, the anion transport protein from human erythrocyte membranes
    • Boodhoo A., Reithmeier R.A. Characterization of matrix-bound Band 3, the anion transport protein from human erythrocyte membranes. J. Biol. Chem. 1984, 259:785-790.
    • (1984) J. Biol. Chem. , vol.259 , pp. 785-790
    • Boodhoo, A.1    Reithmeier, R.A.2
  • 35
    • 0002703073 scopus 로고
    • Intracellular pH transients in giant barnacle muscle fibers
    • Boron W.F. Intracellular pH transients in giant barnacle muscle fibers. Am. J. Physiol. 1977, 233:C61-C73.
    • (1977) Am. J. Physiol. , vol.233
    • Boron, W.F.1
  • 37
  • 38
    • 0020624853 scopus 로고
    • Stoichiometry and ion dependencies of the intracellular-pH-regulating mechanism in squid giant axons
    • Boron W.F., Russell J.M. Stoichiometry and ion dependencies of the intracellular-pH-regulating mechanism in squid giant axons. J. Gen. Physiol. 1983, 81:373-399.
    • (1983) J. Gen. Physiol. , vol.81 , pp. 373-399
    • Boron, W.F.1    Russell, J.M.2
  • 39
    • 0031426999 scopus 로고    scopus 로고
    • AE anion exchanger mRNA and protein expression in vascular smooth muscle cells, aorta, and renal microvessels
    • Brosius F.C., et al. AE anion exchanger mRNA and protein expression in vascular smooth muscle cells, aorta, and renal microvessels. Am. J. Physiol. 1997, 273:F1039-F1047.
    • (1997) Am. J. Physiol. , vol.273
    • Brosius, F.C.1
  • 40
    • 0024383334 scopus 로고
    • The major kidney band 3 gene transcript predicts an amino-terminal truncated band 3 polypeptide
    • Brosius F.C.d., Alper S.L., Garcia A.M., Lodish H.F. The major kidney band 3 gene transcript predicts an amino-terminal truncated band 3 polypeptide. J. Biol. Chem. 1989, 264:7784-7787.
    • (1989) J. Biol. Chem. , vol.264 , pp. 7784-7787
    • Brosius, F.1    Alper, S.L.2    Garcia, A.M.3    Lodish, H.F.4
  • 41
    • 0021915137 scopus 로고
    • Evoked mechanical responses of isolated cochlear outer hair cells
    • Brownell W.E., Bader C.R., Bertrand D., de Ribaupierre Y. Evoked mechanical responses of isolated cochlear outer hair cells. Science 1985, 227:194-196.
    • (1985) Science , vol.227 , pp. 194-196
    • Brownell, W.E.1    Bader, C.R.2    Bertrand, D.3    de Ribaupierre, Y.4
  • 42
    • 0030923557 scopus 로고    scopus 로고
    • Familial distal renal tubular acidosis is associated with mutations in the red cell anion exchanger (Band 3, AE1) gene
    • Bruce L.J., et al. Familial distal renal tubular acidosis is associated with mutations in the red cell anion exchanger (Band 3, AE1) gene. J. Clin. Invest. 1997, 100:1693-1707.
    • (1997) J. Clin. Invest. , vol.100 , pp. 1693-1707
    • Bruce, L.J.1
  • 43
    • 0034663483 scopus 로고    scopus 로고
    • Band 3 mutations, renal tubular acidosis and South-East Asian ovalocytosis in Malaysia and Papua New Guinea: loss of up to 95% band 3 transport in red cells
    • Bruce L.J., et al. Band 3 mutations, renal tubular acidosis and South-East Asian ovalocytosis in Malaysia and Papua New Guinea: loss of up to 95% band 3 transport in red cells. Biochem. J. 2000, 350(Pt 1):41-51.
    • (2000) Biochem. J. , vol.350 , Issue.PT 1 , pp. 41-51
    • Bruce, L.J.1
  • 45
    • 9044234777 scopus 로고    scopus 로고
    • The down-regulated in adenoma (DRA) gene encodes an intestine-specific membrane glycoprotein
    • Byeon M.K., et al. The down-regulated in adenoma (DRA) gene encodes an intestine-specific membrane glycoprotein. Oncogene 1996, 12:387-396.
    • (1996) Oncogene , vol.12 , pp. 387-396
    • Byeon, M.K.1
  • 46
    • 0026572717 scopus 로고
    • Chemical probes for anion transporters of mammalian cell membranes
    • Cabantchik Z.I., Greger R. Chemical probes for anion transporters of mammalian cell membranes. Am. J. Physiol. 1992, 262:C803-C827.
    • (1992) Am. J. Physiol. , vol.262
    • Cabantchik, Z.I.1    Greger, R.2
  • 47
    • 0015529173 scopus 로고
    • The nature of the membrane sites controlling anion permeability of human red blood cells as determined by studies with disulfonic stilbene derivatives
    • Cabantchik Z.I., Rothstein A. The nature of the membrane sites controlling anion permeability of human red blood cells as determined by studies with disulfonic stilbene derivatives. J. Membr. Biol. 1972, 10:311-330.
    • (1972) J. Membr. Biol. , vol.10 , pp. 311-330
    • Cabantchik, Z.I.1    Rothstein, A.2
  • 48
    • 0015962082 scopus 로고
    • Membrane proteins related to anion permeability of human red blood cells. I. Localization of disulfonic stilbene binding sites in proteins involved in permeation
    • Cabantchik Z.I., Rothstein A. Membrane proteins related to anion permeability of human red blood cells. I. Localization of disulfonic stilbene binding sites in proteins involved in permeation. J. Membr. Biol. 1974, 15:207-226.
    • (1974) J. Membr. Biol. , vol.15 , pp. 207-226
    • Cabantchik, Z.I.1    Rothstein, A.2
  • 50
    • 0030807188 scopus 로고    scopus 로고
    • Fluoroquinolone (ciprofloxacin) secretion by human intestinal epithelial (Caco-2) cells
    • Cavet M.E., West M., Simmons N.L. Fluoroquinolone (ciprofloxacin) secretion by human intestinal epithelial (Caco-2) cells. Br. J. Pharmacol. 1997, 121:1567-1578.
    • (1997) Br. J. Pharmacol. , vol.121 , pp. 1567-1578
    • Cavet, M.E.1    West, M.2    Simmons, N.L.3
  • 53
    • 0037470168 scopus 로고    scopus 로고
    • Identification of a critical ankyrin-binding loop on the cytoplasmic domain of erythrocyte membrane band 3 by crystal structure analysis and site-directed mutagenesis
    • Chang S.H., Low P.S. Identification of a critical ankyrin-binding loop on the cytoplasmic domain of erythrocyte membrane band 3 by crystal structure analysis and site-directed mutagenesis. J. Biol. Chem. 2003, 278:6879-6884.
    • (2003) J. Biol. Chem. , vol.278 , pp. 6879-6884
    • Chang, S.H.1    Low, P.S.2
  • 54
    • 0036732041 scopus 로고    scopus 로고
    • The Colon Anion Transporter, Down-Regulated in Adenoma, Induces Growth Suppression That Is Abrogated by E1A
    • Chapman J.M., Knoepp S.M., Byeon M.K., Henderson K.W., Schweinfest C.W. The Colon Anion Transporter, Down-Regulated in Adenoma, Induces Growth Suppression That Is Abrogated by E1A. Cancer Res. 2002, 62:5083-5088.
    • (2002) Cancer Res. , vol.62 , pp. 5083-5088
    • Chapman, J.M.1    Knoepp, S.M.2    Byeon, M.K.3    Henderson, K.W.4    Schweinfest, C.W.5
  • 55
    • 0025338674 scopus 로고
    • A bicarbonate-dependent increase in extracellular pH mediated by GABAA receptors in turtle cerebellum
    • Chen J.C., Chesler M. A bicarbonate-dependent increase in extracellular pH mediated by GABAA receptors in turtle cerebellum. Neurosci Lett. 1990, 116:130-135.
    • (1990) Neurosci Lett. , vol.116 , pp. 130-135
    • Chen, J.C.1    Chesler, M.2
  • 56
    • 0026503811 scopus 로고
    • Modulation of extracellular pH by glutamate and GABA in rat hippocampal slices
    • Chen J.C., Chesler M. Modulation of extracellular pH by glutamate and GABA in rat hippocampal slices. J. Neurophysiol. 1992, 67:29-36.
    • (1992) J. Neurophysiol. , vol.67 , pp. 29-36
    • Chen, J.C.1    Chesler, M.2
  • 57
    • 1242295211 scopus 로고    scopus 로고
    • Synaptic uptake and beyond: the sodium- and chloride-dependent neurotransmitter transporter family SLC6
    • Chen N.H., Reith M.E., Quick M.W. Synaptic uptake and beyond: the sodium- and chloride-dependent neurotransmitter transporter family SLC6. Pflugers Arch. 2004, 447:519-531.
    • (2004) Pflugers Arch. , vol.447 , pp. 519-531
    • Chen, N.H.1    Reith, M.E.2    Quick, M.W.3
  • 58
    • 84882488168 scopus 로고    scopus 로고
    • Cl- Is Required for HCO3- Entry Necessary for Sperm Capacitation in Guinea Pig: Involvement of a Cl-/HCO3- Exchanger (SLC26A3) and CFTR. Biol. Reprod
    • Chen, W.Y. et al. (2008). Cl- Is Required for HCO3- Entry Necessary for Sperm Capacitation in Guinea Pig: Involvement of a Cl-/HCO3- Exchanger (SLC26A3) and CFTR. Biol. Reprod.
    • (2008)
    • Chen, W.Y.1
  • 59
    • 14844335679 scopus 로고    scopus 로고
    • Functional comparison of mouse slc26a6 anion exchanger with human SLC26A6 polypeptide variants: Differences in anion selectivity, regulation, and electrogenicity
    • Chernova M.N., et al. Functional comparison of mouse slc26a6 anion exchanger with human SLC26A6 polypeptide variants: Differences in anion selectivity, regulation, and electrogenicity. J. Biol. Chem. 2005, 280:8564-8580.
    • (2005) J. Biol. Chem. , vol.280 , pp. 8564-8580
    • Chernova, M.N.1
  • 60
    • 0037512530 scopus 로고    scopus 로고
    • Acute regulation of the SLC26A3 congenital chloride diarrhoea anion exchanger (DRA) expressed in Xenopus oocytes
    • Chernova M.N., et al. Acute regulation of the SLC26A3 congenital chloride diarrhoea anion exchanger (DRA) expressed in Xenopus oocytes. J. Physiol. 2003, 549:3-19.
    • (2003) J. Physiol. , vol.549 , pp. 3-19
    • Chernova, M.N.1
  • 63
    • 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. An electroneutral sodium/bicarbonate cotransporter NBCn1 and associated sodium channel. Nature 2000, 405:571-575.
    • (2000) Nature , vol.405 , pp. 571-575
    • Choi, I.1    Aalkjaer, C.2    Boulpaep, E.L.3    Boron, W.F.4
  • 67
    • 24044457597 scopus 로고    scopus 로고
    • 3 cotransporter NBCn1 in rat hippocampal neurons
    • 3 cotransporter NBCn1 in rat hippocampal neurons. J. Biol. Chem. 2005, 280:17823-17830.
    • (2005) J. Biol. Chem. , vol.280 , pp. 17823-17830
    • Cooper, D.S.1
  • 68
    • 0032245776 scopus 로고    scopus 로고
    • 2 permeability of xenopus oocytes expressing aquaporin 1 or its C189S mutant
    • 2 permeability of xenopus oocytes expressing aquaporin 1 or its C189S mutant. Am. J. Physiol. 1998, 275:C1481-C1486.
    • (1998) Am. J. Physiol. , vol.275
    • Cooper, G.J.1    Boron, W.F.2
  • 69
    • 61449242807 scopus 로고    scopus 로고
    • - oxalate transporter in patients with primary hyperparathyroidism
    • - oxalate transporter in patients with primary hyperparathyroidism. Eur. J. Endocrinol. 2009, 160:283-288.
    • (2009) Eur. J. Endocrinol. , vol.160 , pp. 283-288
    • Corbetta, S.1
  • 70
    • 8244263673 scopus 로고    scopus 로고
    • Pendred syndrome (goitre and sensorineural hearing loss) maps to chromosome 7 in the region containing the nonsyndromic deafness gene DFNB4
    • Coyle B., et al. Pendred syndrome (goitre and sensorineural hearing loss) maps to chromosome 7 in the region containing the nonsyndromic deafness gene DFNB4. Nat. Genet. 1996, 12:421-423.
    • (1996) Nat. Genet. , vol.12 , pp. 421-423
    • Coyle, B.1
  • 71
    • 7144261720 scopus 로고    scopus 로고
    • Molecular analysis of the PDS gene in Pendred syndrome
    • Coyle B., et al. Molecular analysis of the PDS gene in Pendred syndrome. Hum. Mol. Genet. 1998, 7:1105-1112.
    • (1998) Hum. Mol. Genet. , vol.7 , pp. 1105-1112
    • Coyle, B.1
  • 72
    • 0032518518 scopus 로고    scopus 로고
    • Polyvariant mutant cystic fibrosis transmembrane conductance regulator genes. The polymorphic (Tg)m locus explains the partial penetrance of the T5 polymorphism as a disease mutation
    • Cuppens H., et al. Polyvariant mutant cystic fibrosis transmembrane conductance regulator genes. The polymorphic (Tg)m locus explains the partial penetrance of the T5 polymorphism as a disease mutation. J. Clin. Invest. 1998, 101:487-496.
    • (1998) J. Clin. Invest. , vol.101 , pp. 487-496
    • Cuppens, H.1
  • 73
    • 42949132296 scopus 로고    scopus 로고
    • Prestin-based outer hair cell motility is necessary for mammalian cochlear amplification
    • Dallos P., et al. Prestin-based outer hair cell motility is necessary for mammalian cochlear amplification. Neuron 2008, 58:333-339.
    • (2008) Neuron , vol.58 , pp. 333-339
    • Dallos, P.1
  • 74
    • 0033864469 scopus 로고    scopus 로고
    • Glial strategy for metabolic shuttling and neuronal function
    • Deitmer J.W. Glial strategy for metabolic shuttling and neuronal function. Bioessays 2000, 22:747-752.
    • (2000) Bioessays , vol.22 , pp. 747-752
    • Deitmer, J.W.1
  • 75
    • 33645704166 scopus 로고    scopus 로고
    • Proximal renal tubular acidosis and ocular pathology: L522P, a novel missense mutation in the gene (SLC4A4) for Sodium Bicarbonate Cotransporter protein (NBCe1)
    • Demirci F.Y., Chang M.-H., Mah T.S., Romero M.F., Gorin M.B. Proximal renal tubular acidosis and ocular pathology: L522P, a novel missense mutation in the gene (SLC4A4) for Sodium Bicarbonate Cotransporter protein (NBCe1). Mol. Vision 2006, 12:324-330.
    • (2006) Mol. Vision , vol.12 , pp. 324-330
    • Demirci, F.Y.1    Chang, M.-H.2    Mah, T.S.3    Romero, M.F.4    Gorin, M.B.5
  • 76
    • 0022725851 scopus 로고
    • Cloning and structural characterization of a human non-erythroid band 3-like protein
    • Demuth D.R., et al. Cloning and structural characterization of a human non-erythroid band 3-like protein. Embo J. 1986, 5:1205-1214.
    • (1986) Embo J. , vol.5 , pp. 1205-1214
    • Demuth, D.R.1
  • 77
    • 42949110371 scopus 로고    scopus 로고
    • Conserved Dimeric Subunit Stoichiometry of SLC26 Multifunctional Anion Exchangers
    • Detro-Dassen S., et al. Conserved Dimeric Subunit Stoichiometry of SLC26 Multifunctional Anion Exchangers. J. Biol. Chem. 2008, 283:4177-4188.
    • (2008) J. Biol. Chem. , vol.283 , pp. 4177-4188
    • Detro-dassen, S.1
  • 78
    • 10844221389 scopus 로고    scopus 로고
    • A novel missense mutation in the sodium bicarbonate cotransporter (NBCe1/SLC4A4) causes proximal tubular acidosis and glaucoma through ion transport defects
    • Dinour D., et al. A novel missense mutation in the sodium bicarbonate cotransporter (NBCe1/SLC4A4) causes proximal tubular acidosis and glaucoma through ion transport defects. J. Biol. Chem. 2004, 279:52238-52246.
    • (2004) J. Biol. Chem. , vol.279 , pp. 52238-52246
    • Dinour, D.1
  • 79
    • 50549175610 scopus 로고
    • The preparation and chemical characteristics of hemoglobin-free ghosts of human erythrocytes
    • Dodge J.T., Mitchell C., Hanahan D.J. The preparation and chemical characteristics of hemoglobin-free ghosts of human erythrocytes. Arch. Biochem. Biophys. 1963, 100:119-130.
    • (1963) Arch. Biochem. Biophys. , vol.100 , pp. 119-130
    • Dodge, J.T.1    Mitchell, C.2    Hanahan, D.J.3
  • 80
    • 43749089149 scopus 로고    scopus 로고
    • Congenital chloride-losing diarrhea causing mutations in the stas domain result in misfolding and mistrafficking of SLC26A3
    • Dorwart M.R., Shcheynikov N., Baker J.M., Forman-Kay J.D., Muallem S., Thomas P.J. Congenital chloride-losing diarrhea causing mutations in the stas domain result in misfolding and mistrafficking of SLC26A3. J. Biol. Chem. 2008, 283:8711-8722.
    • (2008) J. Biol. Chem. , vol.283 , pp. 8711-8722
    • Dorwart, M.R.1    Shcheynikov, N.2    Baker, J.M.3    Forman-kay, J.D.4    Muallem, S.5    Thomas, P.J.6
  • 82
    • 0034859548 scopus 로고    scopus 로고
    • - cotransporter expressed in Xenopus laevis oocytes: Inhibition by tenidap and benzamil and effect of temperature on transport rate and stoichiometry
    • - cotransporter expressed in Xenopus laevis oocytes: Inhibition by tenidap and benzamil and effect of temperature on transport rate and stoichiometry. Pflügers Arch. 2001, 442:709-717.
    • (2001) Pflügers Arch. , vol.442 , pp. 709-717
    • Ducoudret, O.1    Diakov, A.2    Mueller-berger, S.3    Romero, M.F.4    Boron, W.F.5    Frömter, E.6
  • 84
    • 0037122805 scopus 로고    scopus 로고
    • X-ray structure of a ClC chloride channel at 3.0 A reveals the molecular basis of anion selectivity
    • Dutzler R., Campbell E.B., Cadene M., Chait B.T., MacKinnon R. X-ray structure of a ClC chloride channel at 3.0 A reveals the molecular basis of anion selectivity. Nature 2002, 415:287-294.
    • (2002) Nature , vol.415 , pp. 287-294
    • Dutzler, R.1    Campbell, E.B.2    Cadene, M.3    Chait, B.T.4    MacKinnon, R.5
  • 85
    • 0032964405 scopus 로고    scopus 로고
    • Transport characteristics of the apical anion exchanger of rabbit cortical collecting duct beta-cells
    • Emmons C. Transport characteristics of the apical anion exchanger of rabbit cortical collecting duct beta-cells. Am. J. Physiol. 1999, 276:F635-F643.
    • (1999) Am. J. Physiol. , vol.276
    • Emmons, C.1
  • 86
    • 0035862723 scopus 로고    scopus 로고
    • Targeted disruption of mouse Pds provides insight about the inner-ear defects encountered in Pendred syndrome
    • Everett L.A., et al. Targeted disruption of mouse Pds provides insight about the inner-ear defects encountered in Pendred syndrome. Hum. Mol. Genet. 2001, 10:153-161.
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 153-161
    • Everett, L.A.1
  • 87
    • 16944366606 scopus 로고    scopus 로고
    • Pendred syndrome is caused by mutations in a putative sulphate transporter gene (PDS)
    • Everett L.A., et al. Pendred syndrome is caused by mutations in a putative sulphate transporter gene (PDS). Nat. Genet. 1997, 17:411-422.
    • (1997) Nat. Genet. , vol.17 , pp. 411-422
    • Everett, L.A.1
  • 88
    • 0032837375 scopus 로고    scopus 로고
    • A family of mammalian anion transporters and their involvement in human genetic diseases
    • Everett L.A., Green E.D. A family of mammalian anion transporters and their involvement in human genetic diseases. Hum. Mol. Genet. 1999, 8:1883-1891.
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 1883-1891
    • Everett, L.A.1    Green, E.D.2
  • 89
    • 0033578352 scopus 로고    scopus 로고
    • Expression pattern of the mouse ortholog of the Pendred's syndrome gene (Pds) suggests a key role for pendrin in the inner ear
    • Everett L.A., Morsli H., Wu D.K., Green E.D. Expression pattern of the mouse ortholog of the Pendred's syndrome gene (Pds) suggests a key role for pendrin in the inner ear. Proc. Natl. Acad. Sci. U. S. A. 1999, 96:9727-9732.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 9727-9732
    • Everett, L.A.1    Morsli, H.2    Wu, D.K.3    Green, E.D.4
  • 90
    • 0015236352 scopus 로고
    • Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane
    • Fairbanks G., Steck T.L., Wallach D.F. Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane. Biochemistry 1971, 10:2606-2617.
    • (1971) Biochemistry , vol.10 , pp. 2606-2617
    • Fairbanks, G.1    Steck, T.L.2    Wallach, D.F.3
  • 93
    • 34247847733 scopus 로고    scopus 로고
    • - cotransporter
    • - cotransporter. J. Biol. Chem. 2007, 282:9042-9052.
    • (2007) J. Biol. Chem. , vol.282 , pp. 9042-9052
    • Gawenis, L.R.1
  • 94
    • 0024381341 scopus 로고
    • Basolateral sodium-coupled acid-base transport mechanisms of the rabbit proximal tubule
    • Geibel J., Giebisch G., Boron W.F. Basolateral sodium-coupled acid-base transport mechanisms of the rabbit proximal tubule. Am. J. Physiol. 1989, 257:F790-F797.
    • (1989) Am. J. Physiol. , vol.257
    • Geibel, J.1    Giebisch, G.2    Boron, W.F.3
  • 95
    • 33846810181 scopus 로고    scopus 로고
    • Mechanism underlying inhibition of intestinal apical Cl/OH exchange following infection with enteropathogenic E. coli
    • Gill R.K., et al. Mechanism underlying inhibition of intestinal apical Cl/OH exchange following infection with enteropathogenic E. coli. J. Clin. Invest. 2007, 117:428-437.
    • (2007) J. Clin. Invest. , vol.117 , pp. 428-437
    • Gill, R.K.1
  • 97
    • 0028077918 scopus 로고
    • Depolarization-induced acid secretion in gliotic hippocampal slices
    • Grichtchenko I.I., Chesler M. Depolarization-induced acid secretion in gliotic hippocampal slices. Neuroscience 1994, 62:1057-1070.
    • (1994) Neuroscience , vol.62 , pp. 1057-1070
    • Grichtchenko, I.I.1    Chesler, M.2
  • 98
    • 0027943529 scopus 로고
    • Depolarization-induced alkalinization of astrocytes in gliotic hippocampal slices
    • Grichtchenko I.I., Chesler M. Depolarization-induced alkalinization of astrocytes in gliotic hippocampal slices. Neuroscience 1994, 62:1071-1078.
    • (1994) Neuroscience , vol.62 , pp. 1071-1078
    • Grichtchenko, I.I.1    Chesler, M.2
  • 101
    • 0029998532 scopus 로고    scopus 로고
    • Functional cell surface expression of the anion transport domain of human red cell band 3 (AE1) in the yeast Saccharomyces cerevisiae
    • Groves J.D., Falson P., le Maire M., Tanner M.J. Functional cell surface expression of the anion transport domain of human red cell band 3 (AE1) in the yeast Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. U. S. A. 1996, 93:12245-12250.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 12245-12250
    • Groves, J.D.1    Falson, P.2    le Maire, M.3    Tanner, M.J.4
  • 102
    • 0026499518 scopus 로고
    • Glycophorin A facilitates the expression of human band 3-mediated anion transport in Xenopus oocytes
    • Groves J.D., Tanner M.J. Glycophorin A facilitates the expression of human band 3-mediated anion transport in Xenopus oocytes. J. Biol. Chem. 1992, 267:22163-22170.
    • (1992) J. Biol. Chem. , vol.267 , pp. 22163-22170
    • Groves, J.D.1    Tanner, M.J.2
  • 103
    • 0028918239 scopus 로고
    • Co-expressed complementary fragments of the human red cell anion exchanger (band 3, AE1) generate stilbene disulfonate-sensitive anion transport
    • Groves J.D., Tanner M.J. Co-expressed complementary fragments of the human red cell anion exchanger (band 3, AE1) generate stilbene disulfonate-sensitive anion transport. J. Biol. Chem. 1995, 270:9097-9105.
    • (1995) J. Biol. Chem. , vol.270 , pp. 9097-9105
    • Groves, J.D.1    Tanner, M.J.2
  • 104
    • 0034925793 scopus 로고    scopus 로고
    • Slc26a2 (diastrophic dysplasia sulfate transporter) is expressed in developing and mature cartilage but also in other tissues and cell types
    • Haila S., Hastbacka J., Bohling T., Karjalainen-Lindsberg M.L., Kere J., Saarialho-Kere U. Slc26a2 (diastrophic dysplasia sulfate transporter) is expressed in developing and mature cartilage but also in other tissues and cell types. J. Histochem. Cytochem. 2001, 49:973-982.
    • (2001) J. Histochem. Cytochem. , vol.49 , pp. 973-982
    • Haila, S.1    Hastbacka, J.2    Bohling, T.3    Karjalainen-lindsberg, M.L.4    Kere, J.5    Saarialho-kere, U.6
  • 105
    • 0034105706 scopus 로고    scopus 로고
    • The congenital chloride diarrhea gene is expressed in seminal vesicle, sweat gland, inflammatory colon epithelium, and in some dysplastic colon cells
    • Haila S., et al. The congenital chloride diarrhea gene is expressed in seminal vesicle, sweat gland, inflammatory colon epithelium, and in some dysplastic colon cells. Histochem. Cell Biol. 2000, 113:279-286.
    • (2000) Histochem. Cell Biol. , vol.113 , pp. 279-286
    • Haila, S.1
  • 107
    • 0026949420 scopus 로고
    • Linkage disequilibrium mapping in isolated founder populations: diastrophic dysplasia in Finland
    • Hastbacka J., de la Chapelle A., Kaitila I., Sistonen P., Weaver A., Lander E. Linkage disequilibrium mapping in isolated founder populations: diastrophic dysplasia in Finland. Nat. Genet. 1992, 2:204-211.
    • (1992) Nat. Genet. , vol.2 , pp. 204-211
    • Hastbacka, J.1    De La Chapelle, A.2    Kaitila, I.3    Sistonen, P.4    Weaver, A.5    Lander, E.6
  • 108
    • 0027978110 scopus 로고
    • The diastrophic dysplasia gene encodes a novel sulfate transporter: positional cloning by fine-structure linkage disequilibrium mapping
    • Hastbacka J., et al. The diastrophic dysplasia gene encodes a novel sulfate transporter: positional cloning by fine-structure linkage disequilibrium mapping. Cell 1994, 78:1073-1087.
    • (1994) Cell , vol.78 , pp. 1073-1087
    • Hastbacka, J.1
  • 109
    • 0032485066 scopus 로고    scopus 로고
    • Intestinal cancer in patients with a germline mutation in the down-regulated in adenoma (DRA) gene
    • Hemminki A., et al. Intestinal cancer in patients with a germline mutation in the down-regulated in adenoma (DRA) gene. Oncogene 1998, 16:681-684.
    • (1998) Oncogene , vol.16 , pp. 681-684
    • Hemminki, A.1
  • 110
    • 33645213727 scopus 로고    scopus 로고
    • - exchanger AE3 display a reduced seizure threshold
    • - exchanger AE3 display a reduced seizure threshold. Mol. Cell. Biol. 2006, 26:182-191.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 182-191
    • Hentschke, M.1
  • 111
    • 16144368521 scopus 로고    scopus 로고
    • Mutations of the Down-regulated in adenoma (DRA) gene cause congenital chloride diarrhoea
    • Hoglund P., et al. Mutations of the Down-regulated in adenoma (DRA) gene cause congenital chloride diarrhoea. Nat. Genet. 1996, 14:316-319.
    • (1996) Nat. Genet. , vol.14 , pp. 316-319
    • Hoglund, P.1
  • 112
    • 30344485162 scopus 로고    scopus 로고
    • Disruption of the SLC26A3-mediated anion transport is associated with male subfertility
    • Hoglund P., Hihnala S., Kujala M., Tiitinen A., Dunkel L., Holmberg C. Disruption of the SLC26A3-mediated anion transport is associated with male subfertility. Fertil. Steril. 2006, 85:232-235.
    • (2006) Fertil. Steril. , vol.85 , pp. 232-235
    • Hoglund, P.1    Hihnala, S.2    Kujala, M.3    Tiitinen, A.4    Dunkel, L.5    Holmberg, C.6
  • 113
    • 0035029623 scopus 로고    scopus 로고
    • Distinct outcomes of chloride diarrhoea in two siblings with identical genetic background of the disease: implications for early diagnosis and treatment
    • Hoglund P., Holmberg C., Sherman P., Kere J. Distinct outcomes of chloride diarrhoea in two siblings with identical genetic background of the disease: implications for early diagnosis and treatment. Gut 2001, 48:724-727.
    • (2001) Gut , vol.48 , pp. 724-727
    • Hoglund, P.1    Holmberg, C.2    Sherman, P.3    Kere, J.4
  • 114
    • 0035174408 scopus 로고    scopus 로고
    • Contribution of dietary oxalate to urinary oxalate excretion
    • Holmes R.P., Goodman H.O., Assimos D.G. Contribution of dietary oxalate to urinary oxalate excretion. Kidney Int. 2001, 59:270-276.
    • (2001) Kidney Int. , vol.59 , pp. 270-276
    • Holmes, R.P.1    Goodman, H.O.2    Assimos, D.G.3
  • 115
    • 18944380326 scopus 로고    scopus 로고
    • The role of cysteine residues in the sulphate transporter, SHST1: construction of a functional cysteine-less transporter
    • Howitt S.M. The role of cysteine residues in the sulphate transporter, SHST1: construction of a functional cysteine-less transporter. Biochim. Biophys. Acta. 2005, 1669:95-100.
    • (2005) Biochim. Biophys. Acta. , vol.1669 , pp. 95-100
    • Howitt, S.M.1
  • 116
    • 0028864685 scopus 로고
    • Addition of carbonic anhydrase augments extracellular pH buffering in rat cerebral cortex
    • Huang W., Smith S.E., Chesler M. Addition of carbonic anhydrase augments extracellular pH buffering in rat cerebral cortex. J. Neurophysiol. 1995, 74:1806-1809.
    • (1995) J. Neurophysiol. , vol.74 , pp. 1806-1809
    • Huang, W.1    Smith, S.E.2    Chesler, M.3
  • 118
    • 0028888516 scopus 로고
    • Hypertonic activation of AE2 anion exchanger in Xenopus oocytes via NHE- mediated intracellular alkalinization
    • Humphreys B.D., Jiang L., Chernova M.N., Alper S.L. Hypertonic activation of AE2 anion exchanger in Xenopus oocytes via NHE- mediated intracellular alkalinization. Am. J. Physiol. 1995, 268:C201-C209.
    • (1995) Am. J. Physiol. , vol.268
    • Humphreys, B.D.1    Jiang, L.2    Chernova, M.N.3    Alper, S.L.4
  • 119
    • 0032720230 scopus 로고    scopus 로고
    • Mutations in SLC4A4 cause permanent isolated proximal renal tubular acidosis with ocular abnormalities
    • Igarashi T., et al. Mutations in SLC4A4 cause permanent isolated proximal renal tubular acidosis with ocular abnormalities. Nat. Genet. 1999, 23:264-266.
    • (1999) Nat. Genet. , vol.23 , pp. 264-266
    • Igarashi, T.1
  • 120
    • 0035088571 scopus 로고    scopus 로고
    • - cotransporter gene (SLC4A4) in a patient with permanent isolated proximal renal tubular acidosis and bilateral glaucoma
    • - cotransporter gene (SLC4A4) in a patient with permanent isolated proximal renal tubular acidosis and bilateral glaucoma. J. Am. Soc. Nephrol. 2001, 12:713-718.
    • (2001) J. Am. Soc. Nephrol. , vol.12 , pp. 713-718
    • Igarashi, T.1
  • 122
    • 0036070022 scopus 로고    scopus 로고
    • Unraveling the molecular pathogenesis of isolated proximal renal tubular acidosis
    • Igarashi T., Sekine T., Inatomi J., Seki G. Unraveling the molecular pathogenesis of isolated proximal renal tubular acidosis. J Am Soc Nephrol. 2002, 13:2171-2177.
    • (2002) J Am Soc Nephrol. , vol.13 , pp. 2171-2177
    • Igarashi, T.1    Sekine, T.2    Inatomi, J.3    Seki, G.4
  • 123
    • 3442880476 scopus 로고    scopus 로고
    • Mutational and functional analysis of SLC4A4 in a patient with proximal renal tubular acidosis
    • Inatomi J., et al. Mutational and functional analysis of SLC4A4 in a patient with proximal renal tubular acidosis. Pflugers Arch. 2004, 448:438-444.
    • (2004) Pflugers Arch. , vol.448 , pp. 438-444
    • Inatomi, J.1
  • 124
    • 33846160522 scopus 로고    scopus 로고
    • - exchanger activity and cAMP-stimulated bicarbonate secretion in pancreatic duct
    • - exchanger activity and cAMP-stimulated bicarbonate secretion in pancreatic duct. Am J Physiol Gastrointest Liver Physiol. 2007, 292:G447-G455.
    • (2007) Am J Physiol Gastrointest Liver Physiol. , vol.292
    • Ishiguro, H.1
  • 125
    • 0036179392 scopus 로고    scopus 로고
    • - exchange in rabbit, rat, and human duodenum
    • - exchange in rabbit, rat, and human duodenum. Gastroenterology 2002, 122:709-724.
    • (2002) Gastroenterology , vol.122 , pp. 709-724
    • Jacob, P.1
  • 126
    • 0032513292 scopus 로고    scopus 로고
    • - exchanger
    • - exchanger. J. Biol. Chem. 1998, 273:6380-6388.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6380-6388
    • Jarolim, P.1
  • 127
    • 0017185295 scopus 로고
    • Proton fluxes associated with erythrocyte membrane anion exchange
    • Jennings M.L. Proton fluxes associated with erythrocyte membrane anion exchange. J. Membr. Biol. 1976, 28:187-205.
    • (1976) J. Membr. Biol. , vol.28 , pp. 187-205
    • Jennings, M.L.1
  • 128
    • 0017903097 scopus 로고
    • 2-independent pH equilibration in human red blood cells
    • 2-independent pH equilibration in human red blood cells. J. Membr. Biol. 1978, 40:365-391.
    • (1978) J. Membr. Biol. , vol.40 , pp. 365-391
    • Jennings, M.L.1
  • 129
    • 0032992027 scopus 로고    scopus 로고
    • Localization of sodium bicarbonate cotransporter (NBC) protein and messenger ribonucleic acid in rat epididymis
    • Jensen L.J., et al. Localization of sodium bicarbonate cotransporter (NBC) protein and messenger ribonucleic acid in rat epididymis. Biol. Reprod. 1999, 60:573-579.
    • (1999) Biol. Reprod. , vol.60 , pp. 573-579
    • Jensen, L.J.1
  • 130
    • 39849092445 scopus 로고    scopus 로고
    • CLC chloride channels and transporters: from genes to protein structure, pathology and physiology
    • Jentsch T.J. CLC chloride channels and transporters: from genes to protein structure, pathology and physiology. Crit. Rev. Biochem. Mol. Biol. 2008, 43:3-36.
    • (2008) Crit. Rev. Biochem. Mol. Biol. , vol.43 , pp. 3-36
    • Jentsch, T.J.1
  • 131
    • 0021200886 scopus 로고
    • Evidence for coupled transport of bicarbonate and sodium in cultured bovine corneal endothelial cells
    • Jentsch T.J., Keller S.K., Koch M., Wiederholt M. Evidence for coupled transport of bicarbonate and sodium in cultured bovine corneal endothelial cells. J. Membr. Biol. 1984, 81:189-204.
    • (1984) J. Membr. Biol. , vol.81 , pp. 189-204
    • Jentsch, T.J.1    Keller, S.K.2    Koch, M.3    Wiederholt, M.4
  • 133
    • 0036083537 scopus 로고    scopus 로고
    • Molecular structure and physiological function of chloride channels
    • Jentsch T.J., Stein V., Weinreich F., Zdebik A.A. Molecular structure and physiological function of chloride channels. Physiol. Rev. 2002, 82:503-568.
    • (2002) Physiol. Rev. , vol.82 , pp. 503-568
    • Jentsch, T.J.1    Stein, V.2    Weinreich, F.3    Zdebik, A.A.4
  • 134
    • 33645412380 scopus 로고    scopus 로고
    • Calcium oxalate urolithiasis in mice lacking anion transporter Slc26a6
    • Jiang Z., et al. Calcium oxalate urolithiasis in mice lacking anion transporter Slc26a6. Nat. Genet. 2006, 38:474-478.
    • (2006) Nat. Genet. , vol.38 , pp. 474-478
    • Jiang, Z.1
  • 137
    • 0345659215 scopus 로고    scopus 로고
    • + secretion
    • + secretion. Nat. Genet. 2003, 35:372-376.
    • (2003) Nat. Genet. , vol.35 , pp. 372-376
    • Kahle, K.T.1
  • 138
    • 0026512293 scopus 로고
    • PH transients due to monosynaptic activation of GABAA receptors in rat hippocampal slices
    • Kaila K., Paalasmaa P., Taira T., Voipio J. pH transients due to monosynaptic activation of GABAA receptors in rat hippocampal slices. Neuroreport 1992, 3:105-108.
    • (1992) Neuroreport , vol.3 , pp. 105-108
    • Kaila, K.1    Paalasmaa, P.2    Taira, T.3    Voipio, J.4
  • 139
    • 0024465190 scopus 로고
    • Influence of GABA-gated bicarbonate conductance on potential, current and intracellular chloride in crayfish muscle fibres
    • Kaila K., Pasternack M., Saarikoski J., Voipio J. Influence of GABA-gated bicarbonate conductance on potential, current and intracellular chloride in crayfish muscle fibres. J. Physiol. (Lond) 1989, 416:161-181.
    • (1989) J. Physiol. (Lond) , vol.416 , pp. 161-181
    • Kaila, K.1    Pasternack, M.2    Saarikoski, J.3    Voipio, J.4
  • 141
    • 0027336327 scopus 로고
    • The role of bicarbonate in GABAA receptor-mediated IPSPs of rat neocortical neurones
    • Kaila K., Voipio J., Paalasmaa P., Pasternack M., Deisz R.A. The role of bicarbonate in GABAA receptor-mediated IPSPs of rat neocortical neurones. J. Physiol. (Lond) 1993, 464:273-289.
    • (1993) J. Physiol. (Lond) , vol.464 , pp. 273-289
    • Kaila, K.1    Voipio, J.2    Paalasmaa, P.3    Pasternack, M.4    Deisz, R.A.5
  • 142
    • 13144262840 scopus 로고    scopus 로고
    • Mutations in the chloride-bicarbonate exchanger gene AE1 cause autosomal dominant but not autosomal recessive distal renal tubular acidosis
    • Karet F.E., et al. Mutations in the chloride-bicarbonate exchanger gene AE1 cause autosomal dominant but not autosomal recessive distal renal tubular acidosis. Proc. Natl. Acad. Sci. U. S. A. 1998, 95:6337-6342.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 6337-6342
    • Karet, F.E.1
  • 143
    • 0035393922 scopus 로고    scopus 로고
    • Mutations in the diastrophic dysplasia sulfate transporter (DTDST) gene: correlation between sulfate transport activity and chondrodysplasia phenotype
    • Karniski L.P. Mutations in the diastrophic dysplasia sulfate transporter (DTDST) gene: correlation between sulfate transport activity and chondrodysplasia phenotype. Hum. Mol. Genet. 2001, 10:1485-1490.
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 1485-1490
    • Karniski, L.P.1
  • 147
    • 0034648013 scopus 로고    scopus 로고
    • Homologous mutations in two diverse sulphate transporters have similar effects
    • Khurana O.K., Coupland L.A., Shelden M.C., Howitt S.M. Homologous mutations in two diverse sulphate transporters have similar effects. FEBS Lett. 2000, 477:118-122.
    • (2000) FEBS Lett. , vol.477 , pp. 118-122
    • Khurana, O.K.1    Coupland, L.A.2    Shelden, M.C.3    Howitt, S.M.4
  • 149
    • 0036783931 scopus 로고    scopus 로고
    • Immunocytochemical localization of pendrin in intercalated cell subtypes in rat and mouse kidney
    • Kim Y.H., et al. Immunocytochemical localization of pendrin in intercalated cell subtypes in rat and mouse kidney. Am. J. Physiol. Renal Physiol. 2002, 283:F744-F754.
    • (2002) Am. J. Physiol. Renal Physiol. , vol.283
    • Kim, Y.H.1
  • 150
    • 0035979278 scopus 로고    scopus 로고
    • Identification of a chloride-formate exchanger expressed on the brush border membrane of renal proximal tubule cells
    • Knauf F., Yang C.L., Thomson R.B., Mentone S.A., Giebisch G., Aronson P.S. Identification of a chloride-formate exchanger expressed on the brush border membrane of renal proximal tubule cells. Proc. Natl. Acad. Sci. U. S. A. 2001, 98:9425-9430.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 9425-9430
    • Knauf, F.1    Yang, C.L.2    Thomson, R.B.3    Mentone, S.A.4    Giebisch, G.5    Aronson, P.S.6
  • 151
    • 0015104527 scopus 로고
    • Chemical modification of membranes. I. Effects of sulfhydryl and amino reactive reagents on anion and cation permeability of the human red blood cell
    • Knauf P.A., Rothstein A. Chemical modification of membranes. I. Effects of sulfhydryl and amino reactive reagents on anion and cation permeability of the human red blood cell. J. Gen. Physiol. 1971, 58:190-210.
    • (1971) J. Gen. Physiol. , vol.58 , pp. 190-210
    • Knauf, P.A.1    Rothstein, A.2
  • 152
    • 0022610679 scopus 로고
    • Oxalate transport by anion exchange across rabbit ileal brush border
    • Knickelbein R.G., Aronson P.S., Dobbins J.W. Oxalate transport by anion exchange across rabbit ileal brush border. J. Clin. Invest. 1986, 77:170-175.
    • (1986) J. Clin. Invest. , vol.77 , pp. 170-175
    • Knickelbein, R.G.1    Aronson, P.S.2    Dobbins, J.W.3
  • 153
    • 17644449375 scopus 로고    scopus 로고
    • - exchanger in the basolateral membrane of the renal CCD and the SMG duct
    • - exchanger in the basolateral membrane of the renal CCD and the SMG duct. Am. J. Physiol. Cell Physiol. 2002, 283:C1206-C1218.
    • (2002) Am. J. Physiol. Cell Physiol. , vol.283
    • Ko, S.B.1
  • 154
    • 18744409048 scopus 로고    scopus 로고
    • - transport in cystic fibrosis
    • - transport in cystic fibrosis. Embo J. 2002, 21:5662-5672.
    • (2002) Embo J. , vol.21 , pp. 5662-5672
    • Ko, S.B.1
  • 155
    • 2342449944 scopus 로고    scopus 로고
    • Gating of CFTR by the STAS domain of SLC26 transporters
    • Ko S.B., et al. Gating of CFTR by the STAS domain of SLC26 transporters. Nat. Cell. Biol. 2004, 6:343-350.
    • (2004) Nat. Cell. Biol. , vol.6 , pp. 343-350
    • Ko, S.B.1
  • 157
    • 0028124125 scopus 로고
    • AE3 anion exchanger isoforms in the vertebrate retina: developmental regulation and differential expression in neurons and glia
    • Kobayashi S., Morgans C.W., Casey J.R., Kopito R.R. AE3 anion exchanger isoforms in the vertebrate retina: developmental regulation and differential expression in neurons and glia. J. Neurosci. 1994, 14:6266-6279.
    • (1994) J. Neurosci. , vol.14 , pp. 6266-6279
    • Kobayashi, S.1    Morgans, C.W.2    Casey, J.R.3    Kopito, R.R.4
  • 158
    • 0024805898 scopus 로고
    • Regulation of intracellular pH by a neuronal homolog of the erythrocyte anion exchanger
    • Kopito R.R., Lee B.S., Simmons D.M., Lindsey A.E., Morgans C.W., Schneider K. Regulation of intracellular pH by a neuronal homolog of the erythrocyte anion exchanger. Cell 1989, 59:927-937.
    • (1989) Cell , vol.59 , pp. 927-937
    • Kopito, R.R.1    Lee, B.S.2    Simmons, D.M.3    Lindsey, A.E.4    Morgans, C.W.5    Schneider, K.6
  • 159
    • 0022428478 scopus 로고
    • Primary structure and transmembrane orientation of the murine anion exchange protein
    • Kopito R.R., Lodish H.F. Primary structure and transmembrane orientation of the murine anion exchange protein. Nature 1985, 316:234-238.
    • (1985) Nature , vol.316 , pp. 234-238
    • Kopito, R.R.1    Lodish, H.F.2
  • 160
    • 34548311571 scopus 로고    scopus 로고
    • SLC26A7 Can function as a chloride-loading mechanism in parietal cells
    • Kosiek, O. et al. (2007). SLC26A7 Can function as a chloride-loading mechanism in parietal cells. Pflugers Arch.
    • (2007) Pflugers Arch
    • Kosiek, O.1
  • 161
    • 0018422046 scopus 로고
    • A comparison of the inhibitory potency of reversibly acting inhibitors of anion transport on chloride and sulfate movements across the human red cell membrane
    • Ku C.P., Jennings M.L., Passow H. A comparison of the inhibitory potency of reversibly acting inhibitors of anion transport on chloride and sulfate movements across the human red cell membrane. Biochim. Biophys. Acta. 1979, 553:132-141.
    • (1979) Biochim. Biophys. Acta. , vol.553 , pp. 132-141
    • Ku, C.P.1    Jennings, M.L.2    Passow, H.3
  • 163
    • 23244457836 scopus 로고    scopus 로고
    • Dissecting asthma using focused transgenic modeling and functional genomics
    • Kuperman D.A., et al. Dissecting asthma using focused transgenic modeling and functional genomics. J. Allergy Clin. Immunol. 2005, 116:305-311.
    • (2005) J. Allergy Clin. Immunol. , vol.116 , pp. 305-311
    • Kuperman, D.A.1
  • 164
    • 41749096569 scopus 로고    scopus 로고
    • Identification of intestinal bicarbonate transporters involved in formation of carbonate precipitates to stimulate water absorption in marine teleost fish
    • Kurita Y., et al. Identification of intestinal bicarbonate transporters involved in formation of carbonate precipitates to stimulate water absorption in marine teleost fish. Am. J. Physiol. - Comp. & Reg. Physiol. 2008, 284:R1402-R1412.
    • (2008) Am. J. Physiol. - Comp. & Reg. Physiol. , vol.284
    • Kurita, Y.1
  • 165
    • 0028365512 scopus 로고
    • Mechanism of apical and basolateral Na(+)-independent Cl-/base exchange in the rabbit superficial proximal straight tubule
    • Kurtz I., Nagami G., Yanagawa N., Li L., Emmons C., Lee I. Mechanism of apical and basolateral Na(+)-independent Cl-/base exchange in the rabbit superficial proximal straight tubule. J. Clin. Invest. 1994, 94:173-183.
    • (1994) J. Clin. Invest. , vol.94 , pp. 173-183
    • Kurtz, I.1    Nagami, G.2    Yanagawa, N.3    Li, L.4    Emmons, C.5    Lee, I.6
  • 166
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 167
    • 0029286220 scopus 로고
    • Transmembrane helix-helix interactions and accessibility of H2DIDS on labelled band 3, the erythrocyte anion exchange protein
    • Landolt-Marticorena C., Casey J.R., Reithmeier R.A. Transmembrane helix-helix interactions and accessibility of H2DIDS on labelled band 3, the erythrocyte anion exchange protein. Mol. Membr. Biol. 1995, 12:173-182.
    • (1995) Mol. Membr. Biol. , vol.12 , pp. 173-182
    • Landolt-marticorena, C.1    Casey, J.R.2    Reithmeier, R.A.3
  • 168
    • 0033524506 scopus 로고    scopus 로고
    • - exchange by cystic fibrosis transmembrane conductance regulator expressed in NIH 3T3 and HEK 293 cells
    • - exchange by cystic fibrosis transmembrane conductance regulator expressed in NIH 3T3 and HEK 293 cells. J. Biol. Chem. 1999, 274:3414-3421.
    • (1999) J. Biol. Chem. , vol.274 , pp. 3414-3421
    • Lee, M.G.1
  • 169
    • 0015502274 scopus 로고
    • The effect of pH at hemolysis on the reconstitution of low cation permeability in human erythrocyte ghosts
    • Lepke S., Passow H. The effect of pH at hemolysis on the reconstitution of low cation permeability in human erythrocyte ghosts. Biochim. Biophys. Acta. 1972, 255:696-702.
    • (1972) Biochim. Biophys. Acta. , vol.255 , pp. 696-702
    • Lepke, S.1    Passow, H.2
  • 170
    • 48349141803 scopus 로고    scopus 로고
    • Polar residues in a conserved motif spanning helices 1 and 2 are functionally important in the SulP transporter family
    • Leves F.P., Tierney M.L., Howitt S.M. Polar residues in a conserved motif spanning helices 1 and 2 are functionally important in the SulP transporter family. Int. J. Biochem. Cell Biol. 2008, 40:2596-2605.
    • (2008) Int. J. Biochem. Cell Biol. , vol.40 , pp. 2596-2605
    • Leves, F.P.1    Tierney, M.L.2    Howitt, S.M.3
  • 172
    • 0032011145 scopus 로고    scopus 로고
    • A mutation in PDS causes non-syndromic recessive deafness
    • Li X.C., et al. A mutation in PDS causes non-syndromic recessive deafness. Nat. Genet. 1998, 18:215-217.
    • (1998) Nat. Genet. , vol.18 , pp. 215-217
    • Li, X.C.1
  • 173
    • 0037136582 scopus 로고    scopus 로고
    • Prestin is required for electromotility of the outer hair cell and for the cochlear amplifier
    • Liberman M.C., Gao J., He D.Z., Wu X., Jia S., Zuo J. Prestin is required for electromotility of the outer hair cell and for the cochlear amplifier. Nature 2002, 419:300-304.
    • (2002) Nature , vol.419 , pp. 300-304
    • Liberman, M.C.1    Gao, J.2    He, D.Z.3    Wu, X.4    Jia, S.5    Zuo, J.6
  • 174
    • 0026661993 scopus 로고
    • - exchanger. Cloning of a cardiac AE3 cDNA, organization of the AE3 gene, and identification of an alternative transcription initiation site
    • - exchanger. Cloning of a cardiac AE3 cDNA, organization of the AE3 gene, and identification of an alternative transcription initiation site. J. Biol. Chem. 1992, 267:7927-7935.
    • (1992) J. Biol. Chem. , vol.267 , pp. 7927-7935
    • Linn, S.C.1    Kudrycki, K.E.2    Shull, G.E.3
  • 175
    • 0035234701 scopus 로고    scopus 로고
    • A novel sodium bicarbonate cotransporter-like gene in an ancient duplicated region: SLC4A9 at 5q31
    • Lipovich, L., Lynch, E.D., Lee, M.K., and King, M.C. (2001). A novel sodium bicarbonate cotransporter-like gene in an ancient duplicated region: SLC4A9 at 5q31. Genome Biol. 2.
    • (2001) Genome Biol. , pp. 2
    • Lipovich, L.1    Lynch, E.D.2    Lee, M.K.3    King, M.C.4
  • 176
    • 12444302838 scopus 로고    scopus 로고
    • Prestin, a cochlear motor protein, is defective in non-syndromic hearing loss
    • Liu X.Z., et al. Prestin, a cochlear motor protein, is defective in non-syndromic hearing loss. Hum. Mol. Genet. 2003, 12:1155-1162.
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 1155-1162
    • Liu, X.Z.1
  • 177
    • 0034672636 scopus 로고    scopus 로고
    • Mapping of five new putative anion transporter genes in human and characterization of SLC26A6, a candidate gene for pancreatic anion exchanger
    • Lohi H., Kujala M., Kerkela E., Saarialho-Kere U., Kestila M., Kere J. Mapping of five new putative anion transporter genes in human and characterization of SLC26A6, a candidate gene for pancreatic anion exchanger. Genomics 2000, 70:102-112.
    • (2000) Genomics , vol.70 , pp. 102-112
    • Lohi, H.1    Kujala, M.2    Kerkela, E.3    Saarialho-kere, U.4    Kestila, M.5    Kere, J.6
  • 178
    • 0037134440 scopus 로고    scopus 로고
    • Functional characterization of three novel tissue-specific anion exchangers SLC26A7, -A8, and -A9
    • Lohi H., et al. Functional characterization of three novel tissue-specific anion exchangers SLC26A7, -A8, and -A9. J. Biol. Chem. 2002, 277:14246-14254.
    • (2002) J. Biol. Chem. , vol.277 , pp. 14246-14254
    • Lohi, H.1
  • 179
    • 1242290339 scopus 로고    scopus 로고
    • Isoforms of the anion exchanger SLC26A6 (PAT1) mediate chloride and sulfate transport and have functional PDZ interaction domains
    • Lohi, H. et al. (2002b). Isoforms of the anion exchanger SLC26A6 (PAT1) mediate chloride and sulfate transport and have functional PDZ interaction domains. Am. J. Physiol. Cell Physiol.
    • (2002) Am. J. Physiol. Cell Physiol.
    • Lohi, H.1
  • 180
    • 0037369278 scopus 로고    scopus 로고
    • Isoforms of SLC26A6 mediate anion transport and have functional PDZ interaction domains
    • Lohi H., et al. Isoforms of SLC26A6 mediate anion transport and have functional PDZ interaction domains. Am. J. Physiol. Cell Physiol. 2003, 284:C769-C779.
    • (2003) Am. J. Physiol. Cell Physiol. , vol.284
    • Lohi, H.1
  • 181
    • 51149118485 scopus 로고    scopus 로고
    • (-) transport by bicarbonate
    • (-) transport by bicarbonate. Cell Physiol. Biochem. 2008, 22:15-30.
    • (2008) Cell Physiol. Biochem. , vol.22 , pp. 15-30
    • Loriol, C.1
  • 182
    • 0018081626 scopus 로고
    • Specific cation modulation of anion transport across the human erythrocyte membrane
    • Low P.S. Specific cation modulation of anion transport across the human erythrocyte membrane. Biochim. Biophys. Acta. 1978, 514:264-273.
    • (1978) Biochim. Biophys. Acta. , vol.514 , pp. 264-273
    • Low, P.S.1
  • 183
    • 34250620938 scopus 로고    scopus 로고
    • 3 cotransporter NBCe1-A: role of lysines in the KKMIK motif of TM5
    • 3 cotransporter NBCe1-A: role of lysines in the KKMIK motif of TM5. Am. J. Physiol. Cell Physiol. 2007, 292:C1787-C1798.
    • (2007) Am. J. Physiol. Cell Physiol. , vol.292
    • Lu, J.1    Boron, W.F.2
  • 184
    • 0032483028 scopus 로고    scopus 로고
    • Evolutionary parameters of the transcribed mammalian genome: an analysis of 2,820 orthologous rodent and human sequences
    • Makalowski W., Boguski M.S. Evolutionary parameters of the transcribed mammalian genome: an analysis of 2,820 orthologous rodent and human sequences. Proc. Natl. Acad. Sci. U. S. A. 1998, 95:9407-9412.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 9407-9412
    • Makalowski, W.1    Boguski, M.S.2
  • 185
    • 0036451660 scopus 로고    scopus 로고
    • SLC26A3 mutations in congenital chloride diarrhea
    • Makela S., Kere J., Holmberg C., Hoglund P. SLC26A3 mutations in congenital chloride diarrhea. Hum. Mutat. 2002, 20:425-438.
    • (2002) Hum. Mutat. , vol.20 , pp. 425-438
    • Makela, S.1    Kere, J.2    Holmberg, C.3    Hoglund, P.4
  • 186
    • 0033987133 scopus 로고    scopus 로고
    • Pendred syndrome: phenotypic variability in two families carrying the same PDS missense mutation [In Process Citation]
    • Masmoudi S., et al. Pendred syndrome: phenotypic variability in two families carrying the same PDS missense mutation [In Process Citation]. Am. J. Med. Genet. 2000, 90:38-44.
    • (2000) Am. J. Med. Genet. , vol.90 , pp. 38-44
    • Masmoudi, S.1
  • 187
    • 0025274876 scopus 로고
    • Postsynaptic fall in intracellular pH and increase in surface pH caused by efflux of formate and acetate anions through GABA-gated channels in crayfish muscle fibres
    • Mason M.J., Mattsson K., Pasternack M., Voipio J., Kaila K. Postsynaptic fall in intracellular pH and increase in surface pH caused by efflux of formate and acetate anions through GABA-gated channels in crayfish muscle fibres. Neuroscience 1990, 34:359-368.
    • (1990) Neuroscience , vol.34 , pp. 359-368
    • Mason, M.J.1    Mattsson, K.2    Pasternack, M.3    Voipio, J.4    Kaila, K.5
  • 189
    • 40449116229 scopus 로고    scopus 로고
    • Expression of anion exchanger 3 influences respiratory rate in awake and isoflurane anesthetized mice
    • Meier S., Hubner C.A., Groeben H., Peters J., Bingmann D., Wiemann M. Expression of anion exchanger 3 influences respiratory rate in awake and isoflurane anesthetized mice. J. Physiol. Pharmacol. 2007, 58(Suppl. 5):371-378.
    • (2007) J. Physiol. Pharmacol. , vol.58 , Issue.SUPPL. 5 , pp. 371-378
    • Meier, S.1    Hubner, C.A.2    Groeben, H.3    Peters, J.4    Bingmann, D.5    Wiemann, M.6
  • 190
    • 38949185690 scopus 로고    scopus 로고
    • Prestin's role in cochlear frequency tuning and transmission of mechanical responses to neural excitation
    • Mellado Lagarde M.M., Drexl M., Lukashkin A.N., Zuo J., Russell I.J. Prestin's role in cochlear frequency tuning and transmission of mechanical responses to neural excitation. Curr. Biol. 2008, 18:200-202.
    • (2008) Curr. Biol. , vol.18 , pp. 200-202
    • Mellado Lagarde, M.M.1    Drexl, M.2    Lukashkin, A.N.3    Zuo, J.4    Russell, I.J.5
  • 192
    • 0344528790 scopus 로고    scopus 로고
    • Downregulated in adenoma gene encodes a chloride transporter defective in congenital chloride diarrhea
    • Moseley R.H., et al. Downregulated in adenoma gene encodes a chloride transporter defective in congenital chloride diarrhea. Am. J. Physiol. 1999, 276:G185-G192.
    • (1999) Am. J. Physiol. , vol.276
    • Moseley, R.H.1
  • 193
    • 1242317663 scopus 로고    scopus 로고
    • The SLC26 gene family of multifunctional anion exchangers
    • Mount D.B., Romero M.F. The SLC26 gene family of multifunctional anion exchangers. Pflügers Arch. 2004, 447:710-721.
    • (2004) Pflügers Arch. , vol.447 , pp. 710-721
    • Mount, D.B.1    Romero, M.F.2
  • 194
    • 33744913771 scopus 로고    scopus 로고
    • An anion antiporter model of prestin, the outer hair cell motor protein
    • Muallem D., Ashmore J. An anion antiporter model of prestin, the outer hair cell motor protein. Biophys. J. 2006, 90:4035-4045.
    • (2006) Biophys. J. , vol.90 , pp. 4035-4045
    • Muallem, D.1    Ashmore, J.2
  • 196
    • 49649089518 scopus 로고    scopus 로고
    • The epithelial anion transporter pendrin is induced by allergy and rhinovirus infection, regulates airway surface liquid, and increases airway reactivity and inflammation in an asthma model
    • Nakagami Y., et al. The epithelial anion transporter pendrin is induced by allergy and rhinovirus infection, regulates airway surface liquid, and increases airway reactivity and inflammation in an asthma model. J. Immunol. 2008, 181:2203-2210.
    • (2008) J. Immunol. , vol.181 , pp. 2203-2210
    • Nakagami, Y.1
  • 197
    • 44449127236 scopus 로고    scopus 로고
    • Identification of pendrin as a common mediator for mucus production in bronchial asthma and chronic obstructive pulmonary disease
    • Nakao I., et al. Identification of pendrin as a common mediator for mucus production in bronchial asthma and chronic obstructive pulmonary disease. J. Immunol. 2008, 180:6262-6269.
    • (2008) J. Immunol. , vol.180 , pp. 6262-6269
    • Nakao, I.1
  • 198
    • 34247854823 scopus 로고    scopus 로고
    • 2+] by inhibition of acid-sensitive TRPV5 and TRPV6 channels
    • 2+] by inhibition of acid-sensitive TRPV5 and TRPV6 channels. Am. J. Physiol. Renal Physiol. 2007, 292:F1314-F1321.
    • (2007) Am. J. Physiol. Renal Physiol. , vol.292
    • Nakaya, K.1
  • 200
    • 4243391059 scopus 로고    scopus 로고
    • Processing and functional expression of carbonic anhydrase isoforms in Xenopus laevis oocytes
    • Nakhoul N.L., et al. Processing and functional expression of carbonic anhydrase isoforms in Xenopus laevis oocytes. FASEB J. 1996, 10:A88.
    • (1996) FASEB J. , vol.10
    • Nakhoul, N.L.1
  • 201
    • 0032725269 scopus 로고    scopus 로고
    • Structural characterization of substrates for the anion exchange transporter in caco-2 cells
    • Ogihara T., Tamai I., Tsuji A. Structural characterization of substrates for the anion exchange transporter in caco-2 cells. J. Pharm. Sci. 1999, 88:1217-1221.
    • (1999) J. Pharm. Sci. , vol.88 , pp. 1217-1221
    • Ogihara, T.1    Tamai, I.2    Tsuji, A.3
  • 202
    • 0028006541 scopus 로고
    • Red blood cell band 3. Lysine 539 and lysine 851 react with the same H2DIDS (4,4'-diisothiocyanodihydrostilbene-2,2'-disulfonic acid) molecule
    • Okubo K., Kang D., Hamasaki N., Jennings M.L. Red blood cell band 3. Lysine 539 and lysine 851 react with the same H2DIDS (4,4'-diisothiocyanodihydrostilbene-2,2'-disulfonic acid) molecule. J. Biol. Chem. 1994, 269:1918-1926.
    • (1994) J. Biol. Chem. , vol.269 , pp. 1918-1926
    • Okubo, K.1    Kang, D.2    Hamasaki, N.3    Jennings, M.L.4
  • 203
    • 0035933514 scopus 로고    scopus 로고
    • Intracellular anions as the voltage sensor of prestin, the outer hair cell motor protein
    • Oliver D., et al. Intracellular anions as the voltage sensor of prestin, the outer hair cell motor protein. Science 2001, 292:2340-2343.
    • (2001) Science , vol.292 , pp. 2340-2343
    • Oliver, D.1
  • 205
    • 0037184919 scopus 로고    scopus 로고
    • - cotransport isoform 3
    • - cotransport isoform 3. J. Biol. Chem. 2002, 277:50503-50509.
    • (2002) J. Biol. Chem. , vol.277 , pp. 50503-50509
    • Park, M.1
  • 206
    • 8644251840 scopus 로고    scopus 로고
    • (+)-Coupled Borate Transporter Essential for Cellular Boron Homeostasis and Cell Growth and Proliferation
    • (+)-Coupled Borate Transporter Essential for Cellular Boron Homeostasis and Cell Growth and Proliferation. Mol. Cell. 2004, 16:331-341.
    • (2004) Mol. Cell. , vol.16 , pp. 331-341
    • Park, M.1    Li, Q.2    Shcheynikov, N.3    Zeng, W.4    Muallem, S.5
  • 207
    • 0011016829 scopus 로고    scopus 로고
    • Characterization of human 'AE4' as an electroneutral, sodium-dependent bicarbonate transporter
    • Parker M.D., Boron W.F., Tanner M.J.A. Characterization of human 'AE4' as an electroneutral, sodium-dependent bicarbonate transporter. FASEB J. 2002, 16:A796.
    • (2002) FASEB J. , vol.16
    • Parker, M.D.1    Boron, W.F.2    Tanner, M.J.A.3
  • 209
    • 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. Human BTR1, a new bicarbonate transporter superfamily member and human AE4 from kidney. Biochem. Biophys. Res. Commun. 2001, 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
  • 210
    • 57449093793 scopus 로고    scopus 로고
    • Functional assessment of allelic variants in the SLC26A4 gene involved in Pendred syndrome and nonsyndromic EVA
    • Pera, A. et al. (2008). Functional assessment of allelic variants in the SLC26A4 gene involved in Pendred syndrome and nonsyndromic EVA. Proc. Natl. Acad. Sci. U. S. A.
    • (2008) Proc. Natl. Acad. Sci. U. S. A.
    • Pera, A.1
  • 211
    • 0036125836 scopus 로고    scopus 로고
    • Differences in endolymphatic sac mitochondria-rich cells indicate specific functions
    • Peters T.A., Tonnaer E.L., Kuijpers W., Cremers C.W., Curfs J.H. Differences in endolymphatic sac mitochondria-rich cells indicate specific functions. Laryngoscope 2002, 112:534-541.
    • (2002) Laryngoscope , vol.112 , pp. 534-541
    • Peters, T.A.1    Tonnaer, E.L.2    Kuijpers, W.3    Cremers, C.W.4    Curfs, J.H.5
  • 212
    • 0347360286 scopus 로고    scopus 로고
    • - exchanger specific to intercalated cells of the outer medullary collecting duct
    • - exchanger specific to intercalated cells of the outer medullary collecting duct. Am. J. Physiol. Renal Physiol. 2004, 286:F161-F169.
    • (2004) Am. J. Physiol. Renal Physiol. , vol.286
    • Petrovic, S.1
  • 213
    • 0036841327 scopus 로고    scopus 로고
    • - exchanger PAT1 and gastric H-K-ATPase in stomach parietal cells
    • - exchanger PAT1 and gastric H-K-ATPase in stomach parietal cells. Am. J. Physiol. Gastrointest Liver Physiol. 2002, 283:G1207-G1216.
    • (2002) Am. J. Physiol. Gastrointest Liver Physiol. , vol.283
    • Petrovic, S.1
  • 215
    • 22944475536 scopus 로고    scopus 로고
    • Chloride/proton antiporter activity of mammalian CLC proteins ClC-4 and ClC-5
    • Picollo A., Pusch M. Chloride/proton antiporter activity of mammalian CLC proteins ClC-4 and ClC-5. Nature. 2005, 436:420-423.
    • (2005) Nature. , vol.436 , pp. 420-423
    • Picollo, A.1    Pusch, M.2
  • 218
    • 0026332210 scopus 로고
    • Isolation of the cDNA for erythrocyte integral membrane protein of 28 kilodaltons: member of an ancient channel family
    • Preston G.M., Agre P. Isolation of the cDNA for erythrocyte integral membrane protein of 28 kilodaltons: member of an ancient channel family. Proc. Natl. Acad. Sci. U. S. A. 1991, 88:11110-11114.
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 11110-11114
    • Preston, G.M.1    Agre, P.2
  • 219
    • 0033523090 scopus 로고    scopus 로고
    • Cloning, Tissue Distribution, Genomic Organization, and Functional Characterization of NBC3, a New Member of the Sodium Bicarbonate Cotransporter Family
    • Pushkin A., Abuladze N., Lee I., Newman D., Hwang J., Kurtz I. Cloning, Tissue Distribution, Genomic Organization, and Functional Characterization of NBC3, a New Member of the Sodium Bicarbonate Cotransporter Family. J. Biol. Chem. 1999, 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.6
  • 220
    • 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. Cloning, characterization and chromosomal assignment of NBC4, a new member of the sodium bicarbonate cotransporter family. Biochim. Biophys. Acta. 2000, 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
  • 221
    • 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. Two C-terminal variants of NBC4, a new member of the sodium bicarbonate cotransporter family: cloning, characterization, and localization. IUBMB Life. 2000, 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
  • 222
    • 33645581428 scopus 로고    scopus 로고
    • 2-) transporters: classification, function, structure, genetic diseases, and knockout models
    • 2-) transporters: classification, function, structure, genetic diseases, and knockout models. Am. J. Physiol. Renal Physiol. 2006, 290:F580-F599.
    • (2006) Am. J. Physiol. Renal Physiol. , vol.290
    • Pushkin, A.1    Kurtz, I.2
  • 223
    • 8644243107 scopus 로고    scopus 로고
    • - exchanger pendrin in the rat kidney is regulated in response to chronic alterations in chloride balance
    • - exchanger pendrin in the rat kidney is regulated in response to chronic alterations in chloride balance. Am. J. Physiol. Renal Physiol. 2004, 287:F1179-F1188.
    • (2004) Am. J. Physiol. Renal Physiol. , vol.287
    • Quentin, F.1
  • 224
    • 33845424990 scopus 로고    scopus 로고
    • Essential helix interactions in the anion transporter domain of prestin revealed by evolutionary trace analysis
    • Rajagopalan L., et al. Essential helix interactions in the anion transporter domain of prestin revealed by evolutionary trace analysis. J. Neurosci. 2006, 26:12727-12734.
    • (2006) J. Neurosci. , vol.26 , pp. 12727-12734
    • Rajagopalan, L.1
  • 225
    • 0033668133 scopus 로고    scopus 로고
    • Regulation of DRA and AE1 in rat colon by dietary Na depletion
    • Rajendran V.M., et al. Regulation of DRA and AE1 in rat colon by dietary Na depletion. Am. J. Physiol. Gastrointest Liver Physiol. 2000, 279:G931-G942.
    • (2000) Am. J. Physiol. Gastrointest Liver Physiol. , vol.279
    • Rajendran, V.M.1
  • 226
    • 0033964071 scopus 로고    scopus 로고
    • Enlarged vestibular aqueduct: a radiological marker of pendred syndrome, and mutation of the PDS gene
    • Reardon W., CF O.M., Trembath R., Jan H., Phelps P.D. Enlarged vestibular aqueduct: a radiological marker of pendred syndrome, and mutation of the PDS gene. Qjm. 2000, 93:99-104.
    • (2000) Qjm. , vol.93 , pp. 99-104
    • Reardon, W.1    Cf, O.M.2    Trembath, R.3    Jan, H.4    Phelps, P.D.5
  • 227
    • 0032773714 scopus 로고    scopus 로고
    • Prevalence, age of onset, and natural history of thyroid disease in Pendred syndrome
    • Reardon W., et al. Prevalence, age of onset, and natural history of thyroid disease in Pendred syndrome. J. Med. Genet. 1999, 36:595-598.
    • (1999) J. Med. Genet. , vol.36 , pp. 595-598
    • Reardon, W.1
  • 228
    • 0020964097 scopus 로고
    • Inhibition of anion transport in human red blood cells by 5,5'- dithiobis(2-nitrobenzoic acid)
    • Reithmeier R.A. Inhibition of anion transport in human red blood cells by 5,5'- dithiobis(2-nitrobenzoic acid). Biochim. Biophys. Acta. 1983, 732:122-125.
    • (1983) Biochim. Biophys. Acta. , vol.732 , pp. 122-125
    • Reithmeier, R.A.1
  • 229
    • 0037225536 scopus 로고    scopus 로고
    • Prolactin regulation of the pendrin-iodide transporter in the mammary gland
    • Rillema J.A., Hill M.A. Prolactin regulation of the pendrin-iodide transporter in the mammary gland. Am. J. Physiol. Endocrinol. Metab. 2003, 284:E25-E28.
    • (2003) Am. J. Physiol. Endocrinol. Metab. , vol.284
    • Rillema, J.A.1    Hill, M.A.2
  • 230
    • 28044458544 scopus 로고    scopus 로고
    • - cotransporters required for normal blood pressure homeostasis
    • - cotransporters required for normal blood pressure homeostasis. Proc. Natl. Acad. Sci. U. S. A. 2005, 102:16777-16782.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 16777-16782
    • Rinehart, J.1
  • 231
    • 0035411726 scopus 로고    scopus 로고
    • - Cotransporter, NBC
    • - Cotransporter, NBC. J. Pancreas 2001, 2:182-191.
    • (2001) J. Pancreas , vol.2 , pp. 182-191
    • Romero, M.F.1
  • 232
    • 0032587119 scopus 로고    scopus 로고
    • 3 cotransporters: Expression cloning and physiology
    • 3 cotransporters: Expression cloning and physiology. Ann. Rev. Physiol. 1999, 61:699-723.
    • (1999) Ann. Rev. Physiol. , vol.61 , pp. 699-723
    • Romero, M.F.1    Boron, W.F.2
  • 233
    • 70350385933 scopus 로고    scopus 로고
    • "Physiology of electrogenic SLC26 paralogs" In - Epithelial Anion Transport in Health and Disease: the role of the SLC26 transporters family
    • Romero M.F., et al. "Physiology of electrogenic SLC26 paralogs" In - Epithelial Anion Transport in Health and Disease: the role of the SLC26 transporters family. Novartis Found. Symp. 2006, 273:126-147.
    • (2006) Novartis Found. Symp. , vol.273 , pp. 126-147
    • Romero, M.F.1
  • 239
    • 84882537726 scopus 로고    scopus 로고
    • Slc4 and Slc26 bicarbonate transporter function and localization in the eye
    • Romero, M.F. et al. (2009). Slc4 and Slc26 bicarbonate transporter function and localization in the eye. IVOS.
    • (2009) IVOS
    • Romero, M.F.1
  • 240
    • 0017262691 scopus 로고
    • Mechanism of anion transport in red blood cells: role of membrane proteins
    • Rothstein A., Cabantchik Z.I., Knauf P. Mechanism of anion transport in red blood cells: role of membrane proteins. Fed. Proc. 1976, 35:3-10.
    • (1976) Fed. Proc. , vol.35 , pp. 3-10
    • Rothstein, A.1    Cabantchik, Z.I.2    Knauf, P.3
  • 241
    • 0036797830 scopus 로고    scopus 로고
    • Retention of pendrin in the endoplasmic reticulum is a major mechanism for Pendred syndrome
    • Rotman-Pikielny P., et al. Retention of pendrin in the endoplasmic reticulum is a major mechanism for Pendred syndrome. Hum. Mol. Genet. 2002, 11:2625-2633.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 2625-2633
    • Rotman-pikielny, P.1
  • 242
    • 0035957363 scopus 로고    scopus 로고
    • Pendrin, encoded by the Pendred syndrome gene, resides in the apical region of renal intercalated cells and mediates bicarbonate secretion
    • Royaux I.E., et al. Pendrin, encoded by the Pendred syndrome gene, resides in the apical region of renal intercalated cells and mediates bicarbonate secretion. Proc. Natl. Acad. Sci. U. S. A. 2001, 98:4221-4226.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 4221-4226
    • Royaux, I.E.1
  • 243
    • 0017103272 scopus 로고
    • Role of choloride transport in regulation of intracellular pH
    • Russell J.M., Boron W.F. Role of choloride transport in regulation of intracellular pH. Nature 1976, 264:73-74.
    • (1976) Nature , vol.264 , pp. 73-74
    • Russell, J.M.1    Boron, W.F.2
  • 244
    • 58149155957 scopus 로고    scopus 로고
    • Anion control of voltage sensing by the motor protein prestin in outer hair cells
    • Rybalchenko V., Santos-Sacchi J. Anion control of voltage sensing by the motor protein prestin in outer hair cells. Biophys. J. 2008, 95:4439-4447.
    • (2008) Biophys. J. , vol.95 , pp. 4439-4447
    • Rybalchenko, V.1    Santos-sacchi, J.2
  • 246
    • 0028585820 scopus 로고
    • The structure and organization of the human erythroid anion exchanger (AE1) gene
    • Sahr K.E., Taylor W.M., Daniels B.P., Rubin H.L., Jarolim P. The structure and organization of the human erythroid anion exchanger (AE1) gene. Genomics 1994, 24:491-501.
    • (1994) Genomics , vol.24 , pp. 491-501
    • Sahr, K.E.1    Taylor, W.M.2    Daniels, B.P.3    Rubin, H.L.4    Jarolim, P.5
  • 247
    • 0344286495 scopus 로고    scopus 로고
    • Phylogenetic characterization of novel transport protein families revealed by genome analyses
    • Saier M.H., et al. Phylogenetic characterization of novel transport protein families revealed by genome analyses. Biochim. Biophys. Acta. 1999, 1422:1-56.
    • (1999) Biochim. Biophys. Acta. , vol.1422 , pp. 1-56
    • Saier, M.H.1
  • 248
    • 0029736440 scopus 로고    scopus 로고
    • (+)-coupled formate transport in rabbit renal microvillus membranes
    • (+)-coupled formate transport in rabbit renal microvillus membranes. Am. J. Physiol. 1996, 271:F401-F407.
    • (1996) Am. J. Physiol. , vol.271
    • Saleh, A.M.1    Rudnick, H.2    Aronson, P.S.3
  • 249
    • 0036774137 scopus 로고    scopus 로고
    • Association of the 867Asp variant of the human anion exchanger 3 gene with common subtypes of idiopathic generalized epilepsy
    • Sander T., et al. Association of the 867Asp variant of the human anion exchanger 3 gene with common subtypes of idiopathic generalized epilepsy. Epilepsy Res. 2002, 51:249-255.
    • (2002) Epilepsy Res. , vol.51 , pp. 249-255
    • Sander, T.1
  • 250
    • 33646114286 scopus 로고    scopus 로고
    • Control of mammalian cochlear amplification by chloride anions
    • Santos-Sacchi J., Song L., Zheng J., Nuttall A.L. Control of mammalian cochlear amplification by chloride anions. J. Neurosci. 2006, 26:3992-3998.
    • (2006) J. Neurosci. , vol.26 , pp. 3992-3998
    • Santos-sacchi, J.1    Song, L.2    Zheng, J.3    Nuttall, A.L.4
  • 251
    • 0036083851 scopus 로고    scopus 로고
    • Functional characterization of NBC4: a new electrogenic sodium- bicarbonate cotransporter
    • Sassani P., et al. Functional characterization of NBC4: a new electrogenic sodium- bicarbonate cotransporter. Am. J. Physiol. Cell Physiol. 2002, 282:C408-C416.
    • (2002) Am. J. Physiol. Cell Physiol. , vol.282
    • Sassani, P.1
  • 252
    • 0032524288 scopus 로고    scopus 로고
    • Functional analysis of diastrophic dysplasia sulfate transporter. Its involvement in growth regulation of chondrocytes mediated by sulfated proteoglycans
    • Satoh H., Susaki M., Shukunami C., Iyama K., Negoro T., Hiraki Y. Functional analysis of diastrophic dysplasia sulfate transporter. Its involvement in growth regulation of chondrocytes mediated by sulfated proteoglycans. J. Biol. Chem. 1998, 273:12307-12315.
    • (1998) J. Biol. Chem. , vol.273 , pp. 12307-12315
    • Satoh, H.1    Susaki, M.2    Shukunami, C.3    Iyama, K.4    Negoro, T.5    Hiraki, Y.6
  • 253
    • 34250637947 scopus 로고    scopus 로고
    • Nonmammalian orthologs of prestin (SLC26A5) are electrogenic divalent/chloride anion exchangers
    • Schaechinger T.J., Oliver D. Nonmammalian orthologs of prestin (SLC26A5) are electrogenic divalent/chloride anion exchangers. Proc. Natl. Acad. Sci. U. S. A. 2007, 104:7693-7698.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 7693-7698
    • Schaechinger, T.J.1    Oliver, D.2
  • 254
    • 22944479662 scopus 로고    scopus 로고
    • Voltage-dependent electrogenic chloride/proton exchange by endosomal CLC proteins
    • Scheel O., Zdebik A.A., Lourdel S., Jentsch T.J. Voltage-dependent electrogenic chloride/proton exchange by endosomal CLC proteins. Nature 2005, 436:424-427.
    • (2005) Nature , vol.436 , pp. 424-427
    • Scheel, O.1    Zdebik, A.A.2    Lourdel, S.3    Jentsch, T.J.4
  • 255
    • 33947520707 scopus 로고    scopus 로고
    • Heterologous expression of the glutamine transporter SNAT3 in Xenopus oocytes is associated with four modes of uncoupled transport
    • Schneider H.P., Broer S., Broer A., Deitmer J.W. Heterologous expression of the glutamine transporter SNAT3 in Xenopus oocytes is associated with four modes of uncoupled transport. J. Biol. Chem. 2007, 282:3788-3798.
    • (2007) J. Biol. Chem. , vol.282 , pp. 3788-3798
    • Schneider, H.P.1    Broer, S.2    Broer, A.3    Deitmer, J.W.4
  • 256
    • 0029004497 scopus 로고
    • Characterization of the stilbenedisulfonate binding site on band 3
    • Schopfer L.M., Salhany J.M. Characterization of the stilbenedisulfonate binding site on band 3. Biochemistry. 1995, 34:8320-8329.
    • (1995) Biochemistry. , vol.34 , pp. 8320-8329
    • Schopfer, L.M.1    Salhany, J.M.2
  • 259
    • 33846006916 scopus 로고    scopus 로고
    • Slc26a3 (dra)-deficient mice display chloride-losing diarrhea, enhanced colonic proliferation, and distinct up-regulation of ion transporters in the colon
    • Schweinfest C.W., et al. slc26a3 (dra)-deficient mice display chloride-losing diarrhea, enhanced colonic proliferation, and distinct up-regulation of ion transporters in the colon. J. Biol. Chem. 2006, 281:37962-37971.
    • (2006) J. Biol. Chem. , vol.281 , pp. 37962-37971
    • Schweinfest, C.W.1
  • 260
    • 0015764378 scopus 로고
    • Preparation and properties of human erythrocyte ghosts
    • Schwoch G., Passow H. Preparation and properties of human erythrocyte ghosts. Mol. Cell. Biochem. 1973, 2:197-218.
    • (1973) Mol. Cell. Biochem. , vol.2 , pp. 197-218
    • Schwoch, G.1    Passow, H.2
  • 261
    • 10844285790 scopus 로고    scopus 로고
    • Characterization and localization of the sodium mediated bicarbonate transporters NBC and NDAE1
    • Case Western Reserve University, Cleveland, OH
    • Sciortino C.M. Characterization and localization of the sodium mediated bicarbonate transporters NBC and NDAE1. Physiology & Biophysics 2001, 252. Case Western Reserve University, Cleveland, OH.
    • (2001) Physiology & Biophysics , pp. 252
    • Sciortino, C.M.1
  • 264
    • 0033956476 scopus 로고    scopus 로고
    • Human pendrin expressed in Xenopus laevis oocytes mediates chloride/formate exchange
    • Scott D.A., Karniski L.P. Human pendrin expressed in Xenopus laevis oocytes mediates chloride/formate exchange. Am. J. Physiol. Cell Physiol. 2000, 278:C207-C211.
    • (2000) Am. J. Physiol. Cell Physiol. , vol.278
    • Scott, D.A.1    Karniski, L.P.2
  • 265
    • 0034235222 scopus 로고    scopus 로고
    • Functional differences of the PDS gene product are associated with phenotypic variation in patients with Pendred syndrome and non-syndromic hearing loss (DFNB4)
    • Scott D.A., et al. Functional differences of the PDS gene product are associated with phenotypic variation in patients with Pendred syndrome and non-syndromic hearing loss (DFNB4). Hum. Mol. Genet. 2000, 9:1709-1715.
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 1709-1715
    • Scott, D.A.1
  • 267
    • 36348986799 scopus 로고    scopus 로고
    • Sodium and chloride absorptive defects in the small intestine in Slc26a6 null mice
    • Seidler U., et al. Sodium and chloride absorptive defects in the small intestine in Slc26a6 null mice. Pflugers Arch. 2008, 455:757-766.
    • (2008) Pflugers Arch. , vol.455 , pp. 757-766
    • Seidler, U.1
  • 269
    • 37349060674 scopus 로고    scopus 로고
    • Regulatory interaction between CFTR and the SLC26 transporters
    • discussion 186-92, 261-4
    • Shcheynikov N., et al. Regulatory interaction between CFTR and the SLC26 transporters. Novartis Found. Symp. 2006, 273:177-186. discussion 186-92, 261-4.
    • (2006) Novartis Found. Symp. , vol.273 , pp. 177-186
    • Shcheynikov, N.1
  • 270
    • 33646139664 scopus 로고    scopus 로고
    • - Exchange by slc26a3 and slc26a6
    • - Exchange by slc26a3 and slc26a6. J. Gen. Physiol. 2006, 127:511-524.
    • (2006) J. Gen. Physiol. , vol.127 , pp. 511-524
    • Shcheynikov, N.1
  • 271
    • 50049122837 scopus 로고    scopus 로고
    • - secretion and in regulation of CFTR in the parotid duct
    • - secretion and in regulation of CFTR in the parotid duct. J. Physiol. 2008, 586:3813-3824.
    • (2008) J. Physiol. , vol.586 , pp. 3813-3824
    • Shcheynikov, N.1
  • 272
    • 0029963073 scopus 로고    scopus 로고
    • Pendred syndrome maps to chromosome 7q21-34 and is caused by an intrinsic defect in thyroid iodine organification
    • Sheffield V.C., et al. Pendred syndrome maps to chromosome 7q21-34 and is caused by an intrinsic defect in thyroid iodine organification. Nat. Genet. 1996, 12:424-426.
    • (1996) Nat. Genet. , vol.12 , pp. 424-426
    • Sheffield, V.C.1
  • 273
    • 0035366669 scopus 로고    scopus 로고
    • Proline residues in two tightly coupled helices of the sulphate transporter, SHST1, are important for sulphate transport
    • Shelden M.C., Loughlin P., Tierney M.L., Howitt S.M. Proline residues in two tightly coupled helices of the sulphate transporter, SHST1, are important for sulphate transport. Biochem. J. 2001, 356:589-594.
    • (2001) Biochem. J. , vol.356 , pp. 589-594
    • Shelden, M.C.1    Loughlin, P.2    Tierney, M.L.3    Howitt, S.M.4
  • 274
    • 33747357532 scopus 로고    scopus 로고
    • The role of the STAS domain in the function and biogenesis of a sulfate transporter as probed by random mutagenesis
    • Shibagaki N., Grossman A.R. The role of the STAS domain in the function and biogenesis of a sulfate transporter as probed by random mutagenesis. J. Biol. Chem. 2006, 281:22964-22973.
    • (2006) J. Biol. Chem. , vol.281 , pp. 22964-22973
    • Shibagaki, N.1    Grossman, A.R.2
  • 276
    • 0028977983 scopus 로고
    • The Down regulated in Adenoma (dra) gene encodes an intestine-specific membrane sulfate transport protein
    • Silberg D.G., Wang W., Moseley R.H., Traber P.G. The Down regulated in Adenoma (dra) gene encodes an intestine-specific membrane sulfate transport protein. J. Biol. Chem. 1995, 270:11897-11902.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11897-11902
    • Silberg, D.G.1    Wang, W.2    Moseley, R.H.3    Traber, P.G.4
  • 277
    • 34147133736 scopus 로고    scopus 로고
    • - exchanger in the upper villous epithelium of the murine duodenum
    • - exchanger in the upper villous epithelium of the murine duodenum. Am. J. Physiol. Gastrointest Liver Physiol. 2007, 292:G1079-G1088.
    • (2007) Am. J. Physiol. Gastrointest Liver Physiol. , vol.292
    • Simpson, J.E.1
  • 279
    • 48649091964 scopus 로고    scopus 로고
    • Fructose-induced hypertension: Essential role of chloride and fructose absorbing transporters PAT1 and Glut5
    • Singh A.K., et al. Fructose-induced hypertension: Essential role of chloride and fructose absorbing transporters PAT1 and Glut5. Kidney Int. 2008, 74:438-447.
    • (2008) Kidney Int. , vol.74 , pp. 438-447
    • Singh, A.K.1
  • 280
    • 38349028899 scopus 로고    scopus 로고
    • Free radical stress-mediated loss of Kcnj10 protein expression in stria vascularis contributes to deafness in Pendred syndrome mouse model
    • Singh R., Wangemann P. Free radical stress-mediated loss of Kcnj10 protein expression in stria vascularis contributes to deafness in Pendred syndrome mouse model. Am. J. Physiol. Renal Physiol. 2008, 294:F139-F148.
    • (2008) Am. J. Physiol. Renal Physiol. , vol.294
    • Singh, R.1    Wangemann, P.2
  • 281
    • 0029057703 scopus 로고
    • Human carbonic anhydrases and carbonic anhydrase deficiencies
    • Sly W.S., Hu P.Y. Human carbonic anhydrases and carbonic anhydrase deficiencies. Annu. Rev. Biochem. 1995, 64:375-401.
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 375-401
    • Sly, W.S.1    Hu, P.Y.2
  • 282
    • 0018178624 scopus 로고
    • The effects of anion transport inhibitors on structural transitions in erythrocyte membranes
    • Snow J.W., Brandts J.F., Low P.S. The effects of anion transport inhibitors on structural transitions in erythrocyte membranes. Biochim. Biophys. Acta. 1978, 512:579-591.
    • (1978) Biochim. Biophys. Acta. , vol.512 , pp. 579-591
    • Snow, J.W.1    Brandts, J.F.2    Low, P.S.3
  • 284
    • 15644379801 scopus 로고    scopus 로고
    • Recognition of unique carboxyl-terminal motifs by distinct PDZ domains
    • Songyang Z., et al. Recognition of unique carboxyl-terminal motifs by distinct PDZ domains. Science 1997, 275:73-77.
    • (1997) Science , vol.275 , pp. 73-77
    • Songyang, Z.1
  • 285
    • 0036838032 scopus 로고    scopus 로고
    • The functional and physical relationship between the DRA bicarbonate transporter and carbonic anhydrase II
    • Sterling D., Brown N.J., Supuran C.T., Casey J.R. The functional and physical relationship between the DRA bicarbonate transporter and carbonic anhydrase II. Am. J. Physiol. Cell Physiol. 2002, 283:C1522-C1529.
    • (2002) Am. J. Physiol. Cell Physiol. , vol.283
    • Sterling, D.1    Brown, N.J.2    Supuran, C.T.3    Casey, J.R.4
  • 286
    • 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. A transport metabolon. Functional interaction of carbonic anhydrase II and chloride/bicarbonate exchangers. J. Biol. Chem. 2001, 276:47886-47894.
    • (2001) J. Biol. Chem. , vol.276 , pp. 47886-47894
    • Sterling, D.1    Reithmeier, R.A.2    Casey, J.R.3
  • 287
    • 0036846879 scopus 로고    scopus 로고
    • Regulation of AE2-mediated Cl(-) Transport by Intracellular or by Extracellular pH Requires Highly Conserved Amino Acid Residues of the AE2 NH(2)-terminal Cytoplasmic Domain
    • Stewart A.K., Chernova M.N., Shmukler B.E., Wilhelm S., Alper S.L. Regulation of AE2-mediated Cl(-) Transport by Intracellular or by Extracellular pH Requires Highly Conserved Amino Acid Residues of the AE2 NH(2)-terminal Cytoplasmic Domain. J. Gen. Physiol. 2002, 120:707-722.
    • (2002) J. Gen. Physiol. , vol.120 , pp. 707-722
    • Stewart, A.K.1    Chernova, M.N.2    Shmukler, B.E.3    Wilhelm, S.4    Alper, S.L.5
  • 288
    • 10644289225 scopus 로고    scopus 로고
    • Acute pH-dependent regulation of AE2-mediated anion exchange involves discrete local surfaces of the NH2-terminal cytoplasmic domain
    • Stewart A.K., Kerr N., Chernova M.N., Alper S.L., Vaughan-Jones R.D. Acute pH-dependent regulation of AE2-mediated anion exchange involves discrete local surfaces of the NH2-terminal cytoplasmic domain. J. Biol. Chem. 2004, 279:52664-52676.
    • (2004) J. Biol. Chem. , vol.279 , pp. 52664-52676
    • Stewart, A.K.1    Kerr, N.2    Chernova, M.N.3    Alper, S.L.4    Vaughan-jones, R.D.5
  • 289
    • 0028278936 scopus 로고
    • Immunolocalization of anion exchanger AE2 and cation exchanger NHE-1 in distinct adjacent cells of gastric mucosa
    • Stuart-Tilley A., Sardet C., Pouyssegur J., Schwartz M.A., Brown D., Alper S.L. Immunolocalization of anion exchanger AE2 and cation exchanger NHE-1 in distinct adjacent cells of gastric mucosa. Am. J. Physiol. 1994, 266:C559-C568.
    • (1994) Am. J. Physiol. , vol.266
    • Stuart-tilley, A.1    Sardet, C.2    Pouyssegur, J.3    Schwartz, M.A.4    Brown, D.5    Alper, S.L.6
  • 290
    • 0031779780 scopus 로고    scopus 로고
    • Immunolocalization and tissue-specific splicing of AE2 anion exchanger in mouse kidney
    • Stuart-Tilley A.K., Shmukler B.E., Brown D., Alper S.L. Immunolocalization and tissue-specific splicing of AE2 anion exchanger in mouse kidney. J. Am. Soc. Nephrol. 1998, 9:946-959.
    • (1998) J. Am. Soc. Nephrol. , vol.9 , pp. 946-959
    • Stuart-tilley, A.K.1    Shmukler, B.E.2    Brown, D.3    Alper, S.L.4
  • 291
    • 0043123052 scopus 로고    scopus 로고
    • - cotransporter (NBC) in human corneal endothelium
    • - cotransporter (NBC) in human corneal endothelium. Exp. Eye. Res. 2003, 77:287-295.
    • (2003) Exp. Eye. Res. , vol.77 , pp. 287-295
    • Sun, X.C.1    Bonanno, J.A.2
  • 293
    • 13344278021 scopus 로고    scopus 로고
    • Achondrogenesis type IB is caused by mutations in the diastrophic dysplasia sulphate transporter gene
    • Superti-Furga A., et al. Achondrogenesis type IB is caused by mutations in the diastrophic dysplasia sulphate transporter gene. Nat. Genet. 1996, 12:100-102.
    • (1996) Nat. Genet. , vol.12 , pp. 100-102
    • Superti-furga, A.1
  • 294
    • 0015388904 scopus 로고
    • Separation and some properties of the major proteins of the human erythrocyte membrane
    • Tanner M.J., Boxer D.H. Separation and some properties of the major proteins of the human erythrocyte membrane. Biochem. J. 1972, 129:333-347.
    • (1972) Biochem. J. , vol.129 , pp. 333-347
    • Tanner, M.J.1    Boxer, D.H.2
  • 295
    • 0015177154 scopus 로고
    • The isolation and functional identification of a protein from the human erythrocyte 'ghost'
    • Tanner M.J., Gray W.R. The isolation and functional identification of a protein from the human erythrocyte 'ghost'. Biochem. J. 1971, 125:1109-1117.
    • (1971) Biochem. J. , vol.125 , pp. 1109-1117
    • Tanner, M.J.1    Gray, W.R.2
  • 296
    • 0032535372 scopus 로고    scopus 로고
    • Novel AE1 mutations in recessive distal renal tubular acidosis. Loss-of-function is rescued by glycophorin A
    • Tanphaichitr V.S., et al. Novel AE1 mutations in recessive distal renal tubular acidosis. Loss-of-function is rescued by glycophorin A. J. Clin. Invest. 1998, 102:2173-2179.
    • (1998) J. Clin. Invest. , vol.102 , pp. 2173-2179
    • Tanphaichitr, V.S.1
  • 297
    • 0037469144 scopus 로고    scopus 로고
    • Identification of Membrane Topography of the Electrogenic Sodium Bicarbonate Cotransporter pNBC1 by in Vitro Transcription/Translation
    • Tatishchev S., et al. Identification of Membrane Topography of the Electrogenic Sodium Bicarbonate Cotransporter pNBC1 by in Vitro Transcription/Translation. Biochemistry. 2003, 42:755-765.
    • (2003) Biochemistry. , vol.42 , pp. 755-765
    • Tatishchev, S.1
  • 298
    • 0036283790 scopus 로고    scopus 로고
    • Mutations of the PDS gene, encoding pendrin, are associated with protein mislocalization and loss of iodide efflux: implications for thyroid dysfunction in Pendred syndrome
    • Taylor J.P., Metcalfe R.A., Watson P.F., Weetman A.P., Trembath R.C. Mutations of the PDS gene, encoding pendrin, are associated with protein mislocalization and loss of iodide efflux: implications for thyroid dysfunction in Pendred syndrome. J. Clin. Endocrinol Metab. 2002, 87:1778-1784.
    • (2002) J. Clin. Endocrinol Metab. , vol.87 , pp. 1778-1784
    • Taylor, J.P.1    Metcalfe, R.A.2    Watson, P.F.3    Weetman, A.P.4    Trembath, R.C.5
  • 299
    • 0017233517 scopus 로고
    • The effect of carbon dioxide on the intracellular pH and buffering power of snail neurones
    • Thomas R.C. The effect of carbon dioxide on the intracellular pH and buffering power of snail neurones. J. Physiol. (Lond) 1976, 255:715-735.
    • (1976) J. Physiol. (Lond) , vol.255 , pp. 715-735
    • Thomas, R.C.1
  • 300
    • 0017128063 scopus 로고
    • + pump in a snail neurone
    • + pump in a snail neurone. Nature 1976, 262:54-55.
    • (1976) Nature , vol.262 , pp. 54-55
    • Thomas, R.C.1
  • 301
    • 0017760271 scopus 로고
    • The role of bicarbonate, chloride and sodium ions in the regulation of intracellular pH in snail neurones
    • Thomas R.C. The role of bicarbonate, chloride and sodium ions in the regulation of intracellular pH in snail neurones. J. Physiol. (Lond) 1977, 273:317-338.
    • (1977) J. Physiol. (Lond) , vol.273 , pp. 317-338
    • Thomas, R.C.1
  • 302
    • 34547851813 scopus 로고    scopus 로고
    • The Testis Anion Transporter 1 (Slc26a8) is required for sperm terminal differentiation and male fertility in the mouse
    • Toure, A. et al. (2007). The Testis Anion Transporter 1 (Slc26a8) is required for sperm terminal differentiation and male fertility in the mouse. Hum. Mol. Genet.
    • (2007) Hum. Mol. Genet.
    • Toure, A.1
  • 303
    • 0035827612 scopus 로고    scopus 로고
    • Tat1, a novel sulfate transporter specifically expressed in human male germ cells and potentially linked to rhogtpase signaling
    • Toure A., Morin L., Pineau C., Becq F., Dorseuil O., Gacon G. Tat1, a novel sulfate transporter specifically expressed in human male germ cells and potentially linked to rhogtpase signaling. J. Biol. Chem. 2001, 276:20309-20315.
    • (2001) J. Biol. Chem. , vol.276 , pp. 20309-20315
    • Toure, A.1    Morin, L.2    Pineau, C.3    Becq, F.4    Dorseuil, O.5    Gacon, G.6
  • 304
    • 0035896561 scopus 로고    scopus 로고
    • - transporter superfamily is an apical anion exchanger of β -intercalated cells in the kidney
    • - transporter superfamily is an apical anion exchanger of β -intercalated cells in the kidney. J. Biol. Chem. 2001, 276:8180-8189.
    • (2001) J. Biol. Chem. , vol.276 , pp. 8180-8189
    • Tsuganezawa, H.1
  • 306
    • 0042333487 scopus 로고    scopus 로고
    • Deoxycorticosterone upregulates PDS (Slc26a4) in mouse kidney: role of pendrin in mineralocorticoid-induced hypertension
    • Verlander J.W., et al. Deoxycorticosterone upregulates PDS (Slc26a4) in mouse kidney: role of pendrin in mineralocorticoid-induced hypertension. Hypertension 2003, 42:356-362.
    • (2003) Hypertension , vol.42 , pp. 356-362
    • Verlander, J.W.1
  • 307
    • 33749411910 scopus 로고    scopus 로고
    • Dietary Cl(-) restriction upregulates pendrin expression within the apical plasma membrane of type B intercalated cells
    • Verlander J.W., et al. Dietary Cl(-) restriction upregulates pendrin expression within the apical plasma membrane of type B intercalated cells. Am. J. Physiol. Renal Physiol. 2006, 291:F833-F839.
    • (2006) Am. J. Physiol. Renal Physiol. , vol.291
    • Verlander, J.W.1
  • 309
    • 0037646994 scopus 로고    scopus 로고
    • Molecular and functional characterization of SLC26A11, a sodium-independent sulfate transporter from high endothelial venules
    • Vincourt J.B., Jullien D., Amalric F., Girard J.P. Molecular and functional characterization of SLC26A11, a sodium-independent sulfate transporter from high endothelial venules. Faseb J. 2003, 17:890-892.
    • (2003) Faseb J. , vol.17 , pp. 890-892
    • Vincourt, J.B.1    Jullien, D.2    Amalric, F.3    Girard, J.P.4
  • 313
    • 0036436278 scopus 로고    scopus 로고
    • -/anion exchanger pendrin in mouse kidney by acid-base status
    • -/anion exchanger pendrin in mouse kidney by acid-base status. Kidney Int. 2002, 62:2109-2117.
    • (2002) Kidney Int. , vol.62 , pp. 2109-2117
    • Wagner, C.A.1
  • 314
    • 55249127294 scopus 로고    scopus 로고
    • 3 exchanger couples with Na/H exchanger 3 for NaCl absorption in murine small intestine
    • e3
    • 3 exchanger couples with Na/H exchanger 3 for NaCl absorption in murine small intestine. Gastroenterology 2008, 135:1645-1653. e3.
    • (2008) Gastroenterology , vol.135 , pp. 1645-1653
    • Walker, N.M.1
  • 315
    • 0037216245 scopus 로고    scopus 로고
    • Localization of pendrin in mouse kidney
    • Wall S.M., et al. Localization of pendrin in mouse kidney. Am. J. Physiol. Renal Physiol. 2003, 284:F229-F241.
    • (2003) Am. J. Physiol. Renal Physiol. , vol.284
    • Wall, S.M.1
  • 316
    • 0034634583 scopus 로고    scopus 로고
    • - Exchanger. Cloning, tissue distribution, and functional characterization
    • - Exchanger. Cloning, tissue distribution, and functional characterization. J. Biol. Chem. 2000, 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
  • 317
    • 33750481850 scopus 로고    scopus 로고
    • - secretion: relevance to cystic fibrosis
    • - secretion: relevance to cystic fibrosis. Embo J. 2006, 25:5049-5057.
    • (2006) Embo J. , vol.25 , pp. 5049-5057
    • Wang, Y.1
  • 320
    • 20144368257 scopus 로고    scopus 로고
    • Renal and intestinal transport defects in Slc26a6-null mice
    • Wang Z., et al. Renal and intestinal transport defects in Slc26a6-null mice. Am. J. Physiol. Cell Physiol. 2005, 288:C957-C965.
    • (2005) Am. J. Physiol. Cell Physiol. , vol.288
    • Wang, Z.1
  • 321
    • 34247860643 scopus 로고    scopus 로고
    • 2+ reabsorption in a Pendred syndrome mouse model
    • 2+ reabsorption in a Pendred syndrome mouse model. Am. J. Physiol. Renal Physiol. 2007, 292:F1345-F1353.
    • (2007) Am. J. Physiol. Renal Physiol. , vol.292
    • Wangemann, P.1
  • 322
    • 53049095054 scopus 로고    scopus 로고
    • The impact of sodium chloride and volume depletion in the chronic kidney disease of congenital chloride diarrhea
    • Wedenoja S., et al. The impact of sodium chloride and volume depletion in the chronic kidney disease of congenital chloride diarrhea. Kidney Int. 2008, 74:1085-1093.
    • (2008) Kidney Int. , vol.74 , pp. 1085-1093
    • Wedenoja, S.1
  • 323
    • 34547626591 scopus 로고    scopus 로고
    • Enzymatic suppression of the membrane conductance associated with the glutamine transporter SNAT3 expressed in Xenopus oocytes by carbonic anhydrase II
    • Weise A., Becker H.M., Deitmer J.W. Enzymatic suppression of the membrane conductance associated with the glutamine transporter SNAT3 expressed in Xenopus oocytes by carbonic anhydrase II. J. Gen. Physiol. 2007, 130:203-215.
    • (2007) J. Gen. Physiol. , vol.130 , pp. 203-215
    • Weise, A.1    Becker, H.M.2    Deitmer, J.W.3
  • 324
    • 37249085641 scopus 로고    scopus 로고
    • The sodium-bicarbonate cotransporter NBCe1 supports glutamine efflux via SNAT3 (SLC38A3) co-expressed in Xenopus oocytes
    • Wendel C., Becker H.M., Deitmer J.W. The sodium-bicarbonate cotransporter NBCe1 supports glutamine efflux via SNAT3 (SLC38A3) co-expressed in Xenopus oocytes. Pflugers Arch. 2008, 455:885-893.
    • (2008) Pflugers Arch. , vol.455 , pp. 885-893
    • Wendel, C.1    Becker, H.M.2    Deitmer, J.W.3
  • 325
    • 17944373014 scopus 로고    scopus 로고
    • Human hypertension caused by mutations in WNK kinases
    • Wilson F.H., et al. Human hypertension caused by mutations in WNK kinases. Science 2001, 293:1107-1112.
    • (2001) Science , vol.293 , pp. 1107-1112
    • Wilson, F.H.1
  • 326
    • 0026529671 scopus 로고
    • Role of Lys 558 and Lys 869 in substrate and inhibitor binding to the murine band 3 protein: a study of the effects of site-directed mutagenesis of the band 3 protein expressed in the oocytes of Xenopus laevis
    • Wood P.G., Muller H., Sovak M., Passow H. Role of Lys 558 and Lys 869 in substrate and inhibitor binding to the murine band 3 protein: a study of the effects of site-directed mutagenesis of the band 3 protein expressed in the oocytes of Xenopus laevis. J. Membr. Biol. 1992, 127:139-148.
    • (1992) J. Membr. Biol. , vol.127 , pp. 139-148
    • Wood, P.G.1    Muller, H.2    Sovak, M.3    Passow, H.4
  • 327
    • 0036783553 scopus 로고    scopus 로고
    • Molecular and functional characterization of the Slc26A6 anion exchanger, functional comparison to Slc26a1
    • Xie Q., Welch R., Mercado A., Romero M.F., Mount D.B. Molecular and functional characterization of the Slc26A6 anion exchanger, functional comparison to Slc26a1. Am. J. Physiol. Renal Physiol. 2002, 283:F826-F838.
    • (2002) Am. J. Physiol. Renal Physiol. , vol.283
    • Xie, Q.1    Welch, R.2    Mercado, A.3    Romero, M.F.4    Mount, D.B.5
  • 328
    • 56649086776 scopus 로고    scopus 로고
    • Deletion of the chloride transporter Slc26a9 causes loss of tubulovesicles in parietal cells and impairs acid secretion in the stomach
    • Xu J., et al. Deletion of the chloride transporter Slc26a9 causes loss of tubulovesicles in parietal cells and impairs acid secretion in the stomach. Proc. Natl. Acad. Sci. U. S. A. 2008, 105:17955-17960.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 17955-17960
    • Xu, J.1
  • 329
    • 0037214012 scopus 로고    scopus 로고
    • - cotransporter NBC4 in rat kidney and characterization of a novel NBC4 variant
    • - cotransporter NBC4 in rat kidney and characterization of a novel NBC4 variant. Am. J. Physiol. Renal. Physiol 2003, 284:F41-F50.
    • (2003) Am. J. Physiol. Renal. Physiol , vol.284
    • Xu, J.1
  • 330
    • 0032415115 scopus 로고    scopus 로고
    • Intestinal inflammation reduces expression of DRA, a transporter responsible for congenital chloride diarrhea
    • Yang H., et al. Intestinal inflammation reduces expression of DRA, a transporter responsible for congenital chloride diarrhea. Am. J. Physiol. 1998, 275:G1445-G1453.
    • (1998) Am. J. Physiol. , vol.275
    • Yang, H.1
  • 331
    • 0027936966 scopus 로고
    • Molecular cloning, expression, and chromosomal localization of two isoforms of the AE3 anion exchanger from human heart
    • Yannoukakos D., Stuart-Tilley A., Fernandez H.A., Fey P., Duyk G., Alper S.L. Molecular cloning, expression, and chromosomal localization of two isoforms of the AE3 anion exchanger from human heart. Circ. Res. 1994, 75:603-614.
    • (1994) Circ. Res. , vol.75 , pp. 603-614
    • Yannoukakos, D.1    Stuart-tilley, A.2    Fernandez, H.A.3    Fey, P.4    Duyk, G.5    Alper, S.L.6
  • 332
    • 84882485661 scopus 로고    scopus 로고
    • Introduction: History of Red Cell Membrane Research
    • WILEY-VCH Verlag GmbH & Co, Weinheim, Y. Yawata (Ed.)
    • Yawata Y. Introduction: History of Red Cell Membrane Research. Cell Membrane: The Red Blood Cell as a Model 2003, 1-25. WILEY-VCH Verlag GmbH & Co, Weinheim. Y. Yawata (Ed.).
    • (2003) Cell Membrane: The Red Blood Cell as a Model , pp. 1-25
    • Yawata, Y.1
  • 333
    • 47149095245 scopus 로고    scopus 로고
    • Heterogeneity in the processing defect of SLC26A4 mutants
    • Yoon J.S., et al. Heterogeneity in the processing defect of SLC26A4 mutants. J. Med. Genet. 2008, 45:411-419.
    • (2008) J. Med. Genet. , vol.45 , pp. 411-419
    • Yoon, J.S.1
  • 334
    • 0034663669 scopus 로고    scopus 로고
    • Red-cell glycophorin A-band 3 interactions associated with the movement of band 3 to the cell surface
    • Young M.T., Beckmann R., Toye A.M., Tanner M.J. Red-cell glycophorin A-band 3 interactions associated with the movement of band 3 to the cell surface. Biochem. J. 2000, 350(Pt 1):53-60.
    • (2000) Biochem. J. , vol.350 , Issue.PT 1 , pp. 53-60
    • Young, M.T.1    Beckmann, R.2    Toye, A.M.3    Tanner, M.J.4
  • 335
    • 33744981140 scopus 로고    scopus 로고
    • Prestin is expressed on the whole outer hair cell basolateral surface
    • Yu N., Zhu M.L., Zhao H.B. Prestin is expressed on the whole outer hair cell basolateral surface. Brain Res. 2006, 1095:51-88.
    • (2006) Brain Res. , vol.1095 , pp. 51-88
    • Yu, N.1    Zhu, M.L.2    Zhao, H.B.3
  • 336
    • 0034329189 scopus 로고    scopus 로고
    • Crystallographic structure and functional interpretation of the cytoplasmic domain of erythrocyte membrane band 3
    • Zhang D., Kiyatkin A., Bolin J.T., Low P.S. Crystallographic structure and functional interpretation of the cytoplasmic domain of erythrocyte membrane band 3. Blood 2000, 96:2925-2933.
    • (2000) Blood , vol.96 , pp. 2925-2933
    • Zhang, D.1    Kiyatkin, A.2    Bolin, J.T.3    Low, P.S.4
  • 337
    • 33745977784 scopus 로고    scopus 로고
    • Analysis of the oligomeric structure of the motor protein prestin
    • Zheng J., et al. Analysis of the oligomeric structure of the motor protein prestin. J. Biol. Chem. 2006, 281:19916-19924.
    • (2006) J. Biol. Chem. , vol.281 , pp. 19916-19924
    • Zheng, J.1
  • 338
    • 0037326334 scopus 로고    scopus 로고
    • Genomic characterization and expression of mouse prestin, the motor protein of outer hair cells
    • Zheng J., Long K.B., Matsuda K.B., Madison L.D., Ryan A.D., Dallos P.D. Genomic characterization and expression of mouse prestin, the motor protein of outer hair cells. Mamm. Genome. 2003, 14:87-96.
    • (2003) Mamm. Genome. , vol.14 , pp. 87-96
    • Zheng, J.1    Long, K.B.2    Matsuda, K.B.3    Madison, L.D.4    Ryan, A.D.5    Dallos, P.D.6
  • 339
    • 0035800198 scopus 로고    scopus 로고
    • Prestin topology: localization of protein epitopes in relation to the plasma membrane
    • Zheng J., Long K.B., Shen W., Madison L.D., Dallos P. Prestin topology: localization of protein epitopes in relation to the plasma membrane. Neuroreport 2001, 12:1929-1935.
    • (2001) Neuroreport , vol.12 , pp. 1929-1935
    • Zheng, J.1    Long, K.B.2    Shen, W.3    Madison, L.D.4    Dallos, P.5
  • 340
  • 341
    • 0037474222 scopus 로고    scopus 로고
    • Novel topology in C-terminal region of the human plasma membrane anion exchanger, AE1
    • Zhu Q., Lee D.W., Casey J.R. Novel topology in C-terminal region of the human plasma membrane anion exchanger, AE1. J. Biol. Chem. 2003, 278:3112-3120.
    • (2003) J. Biol. Chem. , vol.278 , pp. 3112-3120
    • Zhu, Q.1    Lee, D.W.2    Casey, J.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.