메뉴 건너뛰기




Volumn 79, Issue 1 SUPPL. 1, 1999, Pages

CFTR: Mechanism of anion conduction

Author keywords

[No Author keywords available]

Indexed keywords

AMINOBENZOIC ACID; ANION; ANION CHANNEL; CHLORIDE ION; CYSTEINE; IODIDE ION; STILBENEDISULFONIC ACID; SULFONYLUREA DERIVATIVE; THIOCYANATE; TRANSMEMBRANE CONDUCTANCE REGULATOR;

EID: 0032934694     PISSN: 00319333     EISSN: None     Source Type: Journal    
DOI: 10.1152/physrev.1999.79.1.S47     Document Type: Review
Times cited : (122)

References (163)
  • 2
    • 0345312370 scopus 로고    scopus 로고
    • Identification of channel-lining residues in the M6 membrane-spanning segment of CFTR and the position of the anion-selectivity filter
    • AKABAS, M. H., AND M. CHEUNG. Identification of channel-lining residues in the M6 membrane-spanning segment of CFTR and the position of the anion-selectivity filter (Abstract). Biophys. J. 70: A71, 1996.
    • (1996) Biophys. J. , vol.70
    • Akabas, M.H.1    Cheung, M.2
  • 3
    • 0028264188 scopus 로고
    • Amino acid residues lining the chloride channel of the cystic fibrosis transmembrane conductance regulator
    • AKABAS, M. H., C. KAUFMANN, T. A. COOK, AND P. ARCHDEACON. Amino acid residues lining the chloride channel of the cystic fibrosis transmembrane conductance regulator. J. Biol. Chem. 269: 14865-14868, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14865-14868
    • Akabas, M.H.1    Kaufmann, C.2    Cook, T.A.3    Archdeacon, P.4
  • 4
    • 0026471029 scopus 로고
    • Molecular determinants of channel function
    • ANDERSEN, O. S., AND R. E. D. KOEPPE. Molecular determinants of channel function. Physiol. Rev. 72, Suppl: S89-S158, 1992.
    • (1992) Physiol. Rev. , vol.72 , Issue.SUPPL.
    • Andersen, O.S.1    Koeppe, R.E.D.2
  • 5
    • 0025931429 scopus 로고
    • Nucleoside triphosphates are required to open the CFTR chloride channel
    • ANDERSON, M. P., H. A. BERGER, D. P. RICH, R. J. GREGORY, A. E. SMITH, AND M. J. WELSH. Nucleoside triphosphates are required to open the CFTR chloride channel. Cell 67: 775-784, 1991.
    • (1991) Cell , vol.67 , pp. 775-784
    • Anderson, M.P.1    Berger, H.A.2    Rich, D.P.3    Gregory, R.J.4    Smith, A.E.5    Welsh, M.J.6
  • 7
    • 0343470793 scopus 로고
    • Reflections on selectivity
    • Bethesda, MD: Am. Physiol. Soc.
    • ARMSTRONG, C. M. Reflections on selectivity. In: Membrane Transport: People and Ideas. Bethesda, MD: Am. Physiol. Soc., 1989, p. 261-273.
    • (1989) Membrane Transport: People and Ideas , pp. 261-273
    • Armstrong, C.M.1
  • 8
    • 0042643164 scopus 로고
    • Hydration of the halide negative ions in the gas phase. II. Comparison of hydration energies for the alkali positive and halide negative ions
    • ARSHADI, M., R. YAMDAGNI, AND P. KEBARLE. Hydration of the halide negative ions in the gas phase. II. Comparison of hydration energies for the alkali positive and halide negative ions. J. Phys. Chem. 74: 1475-1482, 1970.
    • (1970) J. Phys. Chem. , vol.74 , pp. 1475-1482
    • Arshadi, M.1    Yamdagni, R.2    Kebarle, P.3
  • 10
    • 0026532895 scopus 로고
    • Purification and functional reconstitution of the cystic fibrosis transmembrane conductance regulator (CFTR)
    • BEAR, C. E., C. H. LI, N. KARTNER, R. J. BRIDGES, T. J. JENSEN, M. RAMJEESINGH, AND J. R. RIORDAN. Purification and functional reconstitution of the cystic fibrosis transmembrane conductance regulator (CFTR). Cell 68: 809-818, 1992.
    • (1992) Cell , vol.68 , pp. 809-818
    • Bear, C.E.1    Li, C.H.2    Kartner, N.3    Bridges, R.J.4    Jensen, T.J.5    Ramjeesingh, M.6    Riordan, J.R.7
  • 11
    • 0015424492 scopus 로고
    • Negative conductance caused by entry of sodium and cesium ions into the potassium channels of squid axons
    • BEZANILLA, F., AND C. M. ARMSTRONG. Negative conductance caused by entry of sodium and cesium ions into the potassium channels of squid axons. J. Gen. Physiol. 60: 588-608, 1972.
    • (1972) J. Gen. Physiol. , vol.60 , pp. 588-608
    • Bezanilla, F.1    Armstrong, C.M.2
  • 13
    • 0023162271 scopus 로고
    • Mechanism of anion permeation through channels gated by glycine and gamma-aminobutyric acid in mouse cultured spinal neurones
    • BORMANN, J., O. P. HAMILL, AND B. SAKMANN. Mechanism of anion permeation through channels gated by glycine and gamma-aminobutyric acid in mouse cultured spinal neurones. J. Physiol. (Lond.) 385: 243-286, 1987.
    • (1987) J. Physiol. (Lond.) , vol.385 , pp. 243-286
    • Bormann, J.1    Hamill, O.P.2    Sakmann, B.3
  • 14
    • 0028223284 scopus 로고
    • Infrared spectroscopic detection of light-induced change in chloride-arginine interaction in halorhodopsin
    • BRAIMAN, M. S., T. J. WALTER, AND D. M. BRIERCHECK. Infrared spectroscopic detection of light-induced change in chloride-arginine interaction in halorhodopsin. Biochemistry 33: 1629-1635, 1994.
    • (1994) Biochemistry , vol.33 , pp. 1629-1635
    • Braiman, M.S.1    Walter, T.J.2    Briercheck, D.M.3
  • 16
    • 37049055868 scopus 로고
    • A theory of ion-solvent interaction
    • BUCKINGHAM, A. D. A theory of ion-solvent interaction. Faraday Discuss. Chem. Soc. 24: 151-157, 1957.
    • (1957) Faraday Discuss. Chem. Soc. , vol.24 , pp. 151-157
    • Buckingham, A.D.1
  • 18
    • 0026727807 scopus 로고
    • Control by asparagine residues of calcium permeability and magnesium blockade in the NMDA receptor
    • BURNASHEV, N., R. SCHOEPFER, H. MONYER, J. P. RUPPERSBERG, W. GUNTHER, P. H. SEEBURG, AND B. SAKMANN. Control by asparagine residues of calcium permeability and magnesium blockade in the NMDA receptor. Science 257: 1415-1419, 1992.
    • (1992) Science , vol.257 , pp. 1415-1419
    • Burnashev, N.1    Schoepfer, R.2    Monyer, H.3    Ruppersberg, J.P.4    Gunther, W.5    Seeburg, P.H.6    Sakmann, B.7
  • 19
    • 2542550010 scopus 로고    scopus 로고
    • Dimensions and ion selectivity of recombinant AMPA and kainate receptor channels and their dependence on Q/R site residues
    • BURNASHEV, N., A. VILLARROEL, AND B. SAKMANN. Dimensions and ion selectivity of recombinant AMPA and kainate receptor channels and their dependence on Q/R site residues. J. Physiol. (Lond.) 496: 165-173, 1996.
    • (1996) J. Physiol. (Lond.) , vol.496 , pp. 165-173
    • Burnashev, N.1    Villarroel, A.2    Sakmann, B.3
  • 20
    • 0029063956 scopus 로고
    • Alternate translation initiation codons can create functional forms of cystic fibrosis transmembrane conductance regulator
    • CARROLL, T. P., M. M. MORALES, S. B. FULMER, S. S. ALLEN, T. R. FLOTTE, G. R. CUTTING, AND W. B. GUGGINO. Alternate translation initiation codons can create functional forms of cystic fibrosis transmembrane conductance regulator. J. Biol. Chem. 270: 11941-11946, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11941-11946
    • Carroll, T.P.1    Morales, M.M.2    Fulmer, S.B.3    Allen, S.S.4    Flotte, T.R.5    Cutting, G.R.6    Guggino, W.B.7
  • 21
    • 0030799617 scopus 로고    scopus 로고
    • Permeation through the calcium release channel of cardiac muscle
    • CHEN, D., L. XU, A. TRIPATHY, G. MEISSNER, AND B. EISENBERG. Permeation through the calcium release channel of cardiac muscle. Biophys. J. 73: 1337-1354, 1997.
    • (1997) Biophys. J. , vol.73 , pp. 1337-1354
    • Chen, D.1    Xu, L.2    Tripathy, A.3    Meissner, G.4    Eisenberg, B.5
  • 22
    • 0030893916 scopus 로고    scopus 로고
    • Locating the anion-selectivity filter of the cystic fibrosis transmembrane conductance regulator (CFTR) chloride channel
    • CHEUNG, M., AND M. H. AKABAS. Locating the anion-selectivity filter of the cystic fibrosis transmembrane conductance regulator (CFTR) chloride channel. J. Gen. Physiol. 109: 289-299, 1997.
    • (1997) J. Gen. Physiol. , vol.109 , pp. 289-299
    • Cheung, M.1    Akabas, M.H.2
  • 23
    • 0016821356 scopus 로고
    • Identification of chloride-binding sites in hemoglobin by nuclear-magnetic-resonance quadrupole-relaxation studies of hemoglobin digests
    • CHIANCONE, E., J. E. NORNE, S. FORSEN, J. BONAVENTURA, M. BRUNORI, E. ANTONINI, AND J. WYMAN. Identification of chloride-binding sites in hemoglobin by nuclear-magnetic-resonance quadrupole-relaxation studies of hemoglobin digests. Eur. J. Biochem. 55: 385-390, 1975.
    • (1975) Eur. J. Biochem. , vol.55 , pp. 385-390
    • Chiancone, E.1    Norne, J.E.2    Forsen, S.3    Bonaventura, J.4    Brunori, M.5    Antonini, E.6    Wyman, J.7
  • 24
    • 0017386385 scopus 로고
    • Relaxation studies on complex formation of macrocyclic and open chain antibiotics with monovalent cations
    • CHOCK, P. B., F. EGGERS, M. EIGEN, AND R. WINKLER. Relaxation studies on complex formation of macrocyclic and open chain antibiotics with monovalent cations. Biophys.Chem. 6: 239-251, 1977.
    • (1977) Biophys.chem. , vol.6 , pp. 239-251
    • Chock, P.B.1    Eggers, F.2    Eigen, M.3    Winkler, R.4
  • 25
    • 0028999046 scopus 로고
    • Sticky ions in biological systems
    • COLLINS, K. D. Sticky ions in biological systems. Proc. Natl. Acad. Sci. USA 92: 5553-5557, 1995.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 5553-5557
    • Collins, K.D.1
  • 26
    • 0031029477 scopus 로고    scopus 로고
    • Charge density-dependent strength of hydration and biological structure
    • COLLINS, K. D. Charge density-dependent strength of hydration and biological structure. Biophys. J. 72: 65-76, 1997.
    • (1997) Biophys. J. , vol.72 , pp. 65-76
    • Collins, K.D.1
  • 27
    • 0022147096 scopus 로고
    • The Hofmeister effect and the behaviour of water at interfaces
    • COLLINS, K. D., AND M. W. WASHABAUGH. The Hofmeister effect and the behaviour of water at interfaces. Q. Rev. Biophys. 18: 323-422, 1985.
    • (1985) Q. Rev. Biophys. , vol.18 , pp. 323-422
    • Collins, K.D.1    Washabaugh, M.W.2
  • 29
    • 0029835571 scopus 로고    scopus 로고
    • Effect of cystic fibrosis-associated mutations in the fourth intracellular loop of cystic fibrosis transmembrane conductance regulator
    • COTTEN, J. F., L. S. OSTEDGAARD, M. R. CARSON, AND M. J. WELSH. Effect of cystic fibrosis-associated mutations in the fourth intracellular loop of cystic fibrosis transmembrane conductance regulator. J. Biol. Chem. 271: 21279-21284, 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 21279-21284
    • Cotten, J.F.1    Ostedgaard, L.S.2    Carson, M.R.3    Welsh, M.J.4
  • 30
    • 84971074097 scopus 로고
    • Solvation of ions. XIX. Thermodynamic properties for transfer of single ions between protic and aprotic solvents
    • COX, B. G., G. R. HEDWIG, A. J. PARKER, AND D. W. WATTS. Solvation of ions. XIX. Thermodynamic properties for transfer of single ions between protic and aprotic solvents. Aust. J. Chem. 27: 477-501, 1974.
    • (1974) Aust. J. Chem. , vol.27 , pp. 477-501
    • Cox, B.G.1    Hedwig, G.R.2    Parker, A.J.3    Watts, D.W.4
  • 31
    • 0015382864 scopus 로고
    • Temperature dependence of chloride, bromide, iodide, thiocyanate and salicylate transport in human red cells
    • DALMARK, M., AND J. O. WIETH. Temperature dependence of chloride, bromide, iodide, thiocyanate and salicylate transport in human red cells. J. Physiol. (Lond.) 224: 583-610, 1972.
    • (1972) J. Physiol. (Lond.) , vol.224 , pp. 583-610
    • Dalmark, M.1    Wieth, J.O.2
  • 32
    • 0031992163 scopus 로고    scopus 로고
    • Ion channel selectivity through stepwise changes in binding affinity
    • DANG, T. X., AND E. W. MCCLESKEY. Ion channel selectivity through stepwise changes in binding affinity. J. Gen. Physiol. 111: 185-193, 1998.
    • (1998) J. Gen. Physiol. , vol.111 , pp. 185-193
    • Dang, T.X.1    McCleskey, E.W.2
  • 33
    • 0025013784 scopus 로고
    • Diffusion and kinetic approaches to describe permeation in ionic channels
    • DANI, J. A., AND D. G. LEVITT. Diffusion and kinetic approaches to describe permeation in ionic channels. J. Theor. Biol. 146: 289-301, 1990.
    • (1990) J. Theor. Biol. , vol.146 , pp. 289-301
    • Dani, J.A.1    Levitt, D.G.2
  • 34
    • 0020691096 scopus 로고
    • Lyotropic anions. Na channel gating and Ca electrode response
    • DANI, J. A., J. A. SANCHEZ, AND B. HILLE. Lyotropic anions. Na channel gating and Ca electrode response. J. Gen. Physiol. 81:255-281, 1983.
    • (1983) J. Gen. Physiol. , vol.81 , pp. 255-281
    • Dani, J.A.1    Sanchez, J.A.2    Hille, B.3
  • 35
    • 33847798511 scopus 로고
    • Ionic solvation by aprotic solvents. Gas phase solvation of the alkali ions by acetonitrile
    • DAVIDSON, W. R., AND P. KEBARLE. Ionic solvation by aprotic solvents. Gas phase solvation of the alkali ions by acetonitrile. J. Am. Chem. Soc. 98: 6125-6133, 1976.
    • (1976) J. Am. Chem. Soc. , vol.98 , pp. 6125-6133
    • Davidson, W.R.1    Kebarle, P.2
  • 36
    • 0344915210 scopus 로고
    • Thermodynamic aspects of radiotracer flow
    • edited by L. G. Colombetti. Boca Raton, FL: CRC
    • DAWSON, D. C. Thermodynamic aspects of radiotracer flow. In: Biological Transport of Radiotracers, edited by L. G. Colombetti. Boca Raton, FL: CRC, 1982, p. 79-95.
    • (1982) Biological Transport of Radiotracers , pp. 79-95
    • Dawson, D.C.1
  • 38
    • 0001994556 scopus 로고    scopus 로고
    • Permeability and conductance in ion channels: A primer
    • edited by T. F. Andreoli, J. F. Hoffman, D. D. Fanestil, and S. G. Schultz. New York: Plenum
    • DAWSON, D. C. Permeability and conductance in ion channels: a primer. In: Molecular Biology of Membrane Transport Disorders, edited by T. F. Andreoli, J. F. Hoffman, D. D. Fanestil, and S. G. Schultz. New York: Plenum, 1996, p. 87-109.
    • (1996) Molecular Biology of Membrane Transport Disorders , pp. 87-109
    • Dawson, D.C.1
  • 39
    • 0014439655 scopus 로고
    • Biological membranes: The physical basis of ion and nonelectrolyte selectivity
    • DIAMOND, J. M., AND E. M. WRIGHT. Biological membranes: the physical basis of ion and nonelectrolyte selectivity. Annu. Rev. Physiol. 31: 581-646, 1969.
    • (1969) Annu. Rev. Physiol. , vol.31 , pp. 581-646
    • Diamond, J.M.1    Wright, E.M.2
  • 40
    • 0003125357 scopus 로고
    • Kinetics and mechanism of reactions of main group metal ions with biological carriers
    • DIEBLER, H., M. EIGEN, G. ILGENFRITZ, G. MAAB, AND R. WINKLER. Kinetics and mechanism of reactions of main group metal ions with biological carriers. Pure Appl. Chem. 20: 93-115, 1969.
    • (1969) Pure Appl. Chem. , vol.20 , pp. 93-115
    • Diebler, H.1    Eigen, M.2    Ilgenfritz, G.3    Maab, G.4    Winkler, R.5
  • 41
    • 79960798772 scopus 로고
    • Design of anion receptors: Applications
    • DIETRICH, B. Design of anion receptors: applications. Pure Appl. Chem. 65: 1457-1464, 1993.
    • (1993) Pure Appl. Chem. , vol.65 , pp. 1457-1464
    • Dietrich, B.1
  • 43
    • 0030050164 scopus 로고    scopus 로고
    • A semi-microscopic Monte Carlo study of permeation energetics in a gramicidin-like channel: The origin of cation selectivity
    • DORMAN, V., M. B. PARTENSKII, AND P. C. JORDAN. A semi-microscopic Monte Carlo study of permeation energetics in a gramicidin-like channel: the origin of cation selectivity. Biophys. J. 70: 121-134, 1996.
    • (1996) Biophys. J. , vol.70 , pp. 121-134
    • Dorman, V.1    Partenskii, M.B.2    Jordan, P.C.3
  • 46
    • 0024208537 scopus 로고
    • - channels in colonic carcinoma cells (HT29) as revealed by 5-nitro-2-(3-phenylpropylamino)benzoic acid (NPPB)
    • - channels in colonic carcinoma cells (HT29) as revealed by 5-nitro-2-(3-phenylpropylamino)benzoic acid (NPPB). Biochim. Biophys. Acta 946: 135-142, 1988.
    • (1988) Biochim. Biophys. Acta , vol.946 , pp. 135-142
    • Dreinhofer, J.1    Gogelein, H.2    Greger, R.3
  • 47
    • 84986409778 scopus 로고
    • Anion-receptor molecules: Synthesis of a chiral and functionalized binding subunit, a bicyclic guanidinium group derived from L-or D-asparagine
    • ECHAVARREN, A., A. GALAN, J. DE MENDOZA, AND A. SALMERÓN. Anion-receptor molecules: synthesis of a chiral and functionalized binding subunit, a bicyclic guanidinium group derived from L-or D-asparagine. Helv. Chim. Acta 71: 685-693, 1988.
    • (1988) Helv. Chim. Acta , vol.71 , pp. 685-693
    • Echavarren, A.1    Galan, A.2    De Mendoza, J.3    Salmerón, A.4
  • 49
    • 0015075770 scopus 로고
    • Carriers and specificity in membranes. II. Characteristics of carriers. Alkali ion carriers: Specificity, architecture, and mechanisms: An essay
    • EIGEN, M., AND R. WINKLER. Carriers and specificity in membranes. II. Characteristics of carriers. Alkali ion carriers: specificity, architecture, and mechanisms: an essay. Neurosci. Res. Prog. Bull. 9: 330-338, 1971.
    • (1971) Neurosci. Res. Prog. Bull. , vol.9 , pp. 330-338
    • Eigen, M.1    Winkler, R.2
  • 50
    • 0021070747 scopus 로고
    • Ionic selectivity revisited: The role of kinetic and equilibrium processes in ion permeation through channels
    • EISENMAN, G., AND R. HORN. Ionic selectivity revisited: the role of kinetic and equilibrium processes in ion permeation through channels. J. Membr. Biol. 76: 197-225, 1983.
    • (1983) J. Membr. Biol. , vol.76 , pp. 197-225
    • Eisenman, G.1    Horn, R.2
  • 51
    • 0002933759 scopus 로고
    • Some applications of modern rate theory to physiological systems
    • EYRING, H., R. LUMRY, AND J. W. WOODBURY. Some applications of modern rate theory to physiological systems. Rec. Chem. Prog. 10: 100-114, 1949.
    • (1949) Rec. Chem. Prog. , vol.10 , pp. 100-114
    • Eyring, H.1    Lumry, R.2    Woodbury, J.W.3
  • 52
    • 0031468569 scopus 로고    scopus 로고
    • Pore-forming segments in voltage-gated chloride channels
    • FAHLKE, C., H. T. YU, C. L. BECK, T. H. RHODES, AND A. L. GEORGE, JR. Pore-forming segments in voltage-gated chloride channels. Nature 390: 529-532, 1997.
    • (1997) Nature , vol.390 , pp. 529-532
    • Fahlke, C.1    Yu, H.T.2    Beck, C.L.3    Rhodes, T.H.4    George A.L., Jr.5
  • 53
    • 0025336465 scopus 로고
    • An NMR study of anion binding to yeast phosphoglycerate kinase
    • FAIRBROTHER, W. J., H. C. GRAHAM, AND R. J. WILLIAMS. An NMR study of anion binding to yeast phosphoglycerate kinase. Eur. J. Biochem. 190: 161-169, 1990.
    • (1990) Eur. J. Biochem. , vol.190 , pp. 161-169
    • Fairbrother, W.J.1    Graham, H.C.2    Williams, R.J.3
  • 54
    • 0027326059 scopus 로고
    • Anion permeation in GABA-and glycine-gated channels of mammalian cultured hippocampal neurons
    • FATIMA-SHAD, K., AND P. H. BARRY. Anion permeation in GABA-and glycine-gated channels of mammalian cultured hippocampal neurons. Proc. R. Soc. Lond. B Biol. Sci. 253: 69-75, 1993.
    • (1993) Proc. R. Soc. Lond. B Biol. Sci. , vol.253 , pp. 69-75
    • Fatima-Shad, K.1    Barry, P.H.2
  • 55
    • 0014308722 scopus 로고
    • Permeability and electrical properties of thin lipid membranes
    • FINKELSTEIN, A., AND A. CASS. Permeability and electrical properties of thin lipid membranes. J. Gen. Physiol. 52, Suppl.: 145-173, 1968.
    • (1968) J. Gen. Physiol. , vol.52 , Issue.SUPPL. , pp. 145-173
    • Finkelstein, A.1    Cass, A.2
  • 56
    • 0027191065 scopus 로고
    • CFTR and outward rectifying chloride channels are distinct proteins with a regulatory relationship
    • GABRIEL, S. E., L. L. CLARKE, R. C. BOUCHER, AND M. J. STUTTS. CFTR and outward rectifying chloride channels are distinct proteins with a regulatory relationship. Nature 363: 263-268, 1993.
    • (1993) Nature , vol.363 , pp. 263-268
    • Gabriel, S.E.1    Clarke, L.L.2    Boucher, R.C.3    Stutts, M.J.4
  • 57
    • 0026656037 scopus 로고
    • Mutations in the channel domain of a neuronal nicotinic receptor convert ion selectivity from cationic to anionic
    • GALZI, J. L., A. DEVILLERS-THIERY, N. HUSSY, S. BERTRAND, J. P. CHANGEUX, AND D. BERTRAND. Mutations in the channel domain of a neuronal nicotinic receptor convert ion selectivity from cationic to anionic. Nature 359: 500-505, 1992.
    • (1992) Nature , vol.359 , pp. 500-505
    • Galzi, J.L.1    Devillers-Thiery, A.2    Hussy, N.3    Bertrand, S.4    Changeux, J.P.5    Bertrand, D.6
  • 60
    • 0030989580 scopus 로고    scopus 로고
    • CFTR-independent ATP release from epithelial cells triggered by mechanical stimuli
    • GRYGORCZYK, R., AND J. W. HANRAHAN. CFTR-independent ATP release from epithelial cells triggered by mechanical stimuli. Am. J. Physiol. 272 (Cell Physiol. 41): C1058-C1066, 1997.
    • (1997) Am. J. Physiol. 272 (Cell Physiol. 41) , vol.272
    • Grygorczyk, R.1    Hanrahan, J.W.2
  • 61
    • 0027464248 scopus 로고
    • Outwardly rectifying chloride channels and CF: A divorce and remarriage
    • GUGGINO, W. B. Outwardly rectifying chloride channels and CF: a divorce and remarriage. J. Bioenerg. Biomembr. 25: 27-35, 1993.
    • (1993) J. Bioenerg. Biomembr. , vol.25 , pp. 27-35
    • Guggino, W.B.1
  • 62
    • 0015964491 scopus 로고
    • Mechanism of anion permeation through the muscle fibre membrane of an elasmobranch fish, Taeniura lymma
    • HAGIWARA, S., AND K. TAKAHASHI. Mechanism of anion permeation through the muscle fibre membrane of an elasmobranch fish, Taeniura lymma. J. Physiol. (Lond.) 238: 109-127, 1974.
    • (1974) J. Physiol. (Lond.) , vol.238 , pp. 109-127
    • Hagiwara, S.1    Takahashi, K.2
  • 63
    • 0026503391 scopus 로고
    • Anion permeation in an apical membrane chloride channel of a secretory epithelial cell
    • HALM, D. R., AND R. A. FRIZZELL. Anion permeation in an apical membrane chloride channel of a secretory epithelial cell. J. Gen. Physiol. 99: 339-366, 1992.
    • (1992) J. Gen. Physiol. , vol.99 , pp. 339-366
    • Halm, D.R.1    Frizzell, R.A.2
  • 64
    • 0004152926 scopus 로고
    • Anion interaction in frog muscle
    • Harris, E. J. Anion interaction in frog muscle. J. Physiol. (Lond.) 141: 351-365, 1958.
    • (1958) J. Physiol. (Lond.) , vol.141 , pp. 351-365
    • Harris, E.J.1
  • 68
    • 0018117903 scopus 로고
    • Potassium channels as multi-ion single-file pores
    • HILLE, B., AND W. SCHWARZ. Potassium channels as multi-ion single-file pores. J. Gen. Physiol. 72: 409-442, 1978.
    • (1978) J. Gen. Physiol. , vol.72 , pp. 409-442
    • Hille, B.1    Schwarz, W.2
  • 70
    • 0029860763 scopus 로고    scopus 로고
    • On the use of thiol-modifying agents to determine channel topology
    • HOLMGREN, M., Y. LIU, Y. XU, AND G. YELLEN. On the use of thiol-modifying agents to determine channel topology. Neuropharmacology 35: 797-804, 1996.
    • (1996) Neuropharmacology , vol.35 , pp. 797-804
    • Holmgren, M.1    Liu, Y.2    Xu, Y.3    Yellen, G.4
  • 71
    • 0000612738 scopus 로고
    • Effect of nitrate and other anions on the membrane resistance of frog skeletal muscle
    • HUTTER, O. F., AND S. M. PADSHA. Effect of nitrate and other anions on the membrane resistance of frog skeletal muscle. J. Physiol. (Lond.) 146: 117-132, 1959.
    • (1959) J. Physiol. (Lond.) , vol.146 , pp. 117-132
    • Hutter, O.F.1    Padsha, S.M.2
  • 72
    • 0028340159 scopus 로고
    • Regulation of the gating of cystic fibrosis transmembrane conductance regulator Cl channels by phosphorylation and
    • HWANG, T. C., G. NAGEL, A. C. NAIRN, AND D. C. GADSBY. Regulation of the gating of cystic fibrosis transmembrane conductance regulator Cl channels by phosphorylation and ATP hydrolysis. Proc. Natl. Acad. Sci. USA 91: 4698-4702, 1994.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 4698-4702
    • Hwang, T.C.1    Nagel, G.2    Nairn, A.C.3    Gadsby, D.C.4    Hydrolysis, A.T.P.5
  • 73
    • 0003766353 scopus 로고
    • Halides and halogen atoms as hydrogen-bond acceptors
    • New York: Springer-Verlag
    • JEFFERY, G. A., AND W. SAENGER. Halides and halogen atoms as hydrogen-bond acceptors. In: Hydrogen Bonding in Biological Structures. New York: Springer-Verlag, 1991, p. 161-163.
    • (1991) Hydrogen Bonding in Biological Structures , pp. 161-163
    • Jeffery, G.A.1    Saenger, W.2
  • 75
    • 0015221771 scopus 로고
    • Presence of arginine residues at the strong, hydrophobic anion binding sites of bovine serum albumin
    • JONAS, A., AND G. WEBER. Presence of arginine residues at the strong, hydrophobic anion binding sites of bovine serum albumin. Biochemistry 10: 1335-1339, 1971.
    • (1971) Biochemistry , vol.10 , pp. 1335-1339
    • Jonas, A.1    Weber, G.2
  • 76
    • 0015237788 scopus 로고
    • Strong binding of hydrophobic anions by bovine serum albumin peptides covalently linked to lysozyme
    • JONAS, A., AND G. WEBER. Strong binding of hydrophobic anions by bovine serum albumin peptides covalently linked to lysozyme. Biochemistry 10: 4492-4496, 1971.
    • (1971) Biochemistry , vol.10 , pp. 4492-4496
    • Jonas, A.1    Weber, G.2
  • 77
    • 0026695805 scopus 로고
    • High-resolution X-ray study of deoxyhemoglobin Rothschild 37 beta Trp-Arg: A mutation that creates an intersubunit chloride-binding site
    • KAVANAUGH, J. S., P. H. ROGERS, D. A. CASE, AND A. ARNONE. High-resolution X-ray study of deoxyhemoglobin Rothschild 37 beta Trp-Arg: a mutation that creates an intersubunit chloride-binding site. Biochemistry 31: 4111-4121, 1992.
    • (1992) Biochemistry , vol.31 , pp. 4111-4121
    • Kavanaugh, J.S.1    Rogers, P.H.2    Case, D.A.3    Arnone, A.4
  • 78
    • 0028322962 scopus 로고
    • Chloride acts as a novel negative heterotropic effector of hemoglobin Rothschild (beta 37 Trp→Arg) in solution
    • KELLY, R. M., H. L. HUI, AND R. W. NOBLE. Chloride acts as a novel negative heterotropic effector of hemoglobin Rothschild (beta 37 Trp→Arg) in solution. Biochemistry 33: 4363-4367, 1994.
    • (1994) Biochemistry , vol.33 , pp. 4363-4367
    • Kelly, R.M.1    Hui, H.L.2    Noble, R.W.3
  • 79
    • 0017639586 scopus 로고
    • Novel sulfhydryl reagents
    • KENYON, G. L., AND T. W. BRUCE. Novel sulfhydryl reagents. Methods Enzymol. 47: 407-430, 1977.
    • (1977) Methods Enzymol. , vol.47 , pp. 407-430
    • Kenyon, G.L.1    Bruce, T.W.2
  • 83
    • 0026011344 scopus 로고
    • Ion channel formation by synthetic transmembrane segments of the inhibitory glycine receptor - A model study
    • LANGOSCH, D., K. HARTUNG, E. GRELL, E. BAMBERG, AND H. BETZ. Ion channel formation by synthetic transmembrane segments of the inhibitory glycine receptor - a model study. Biochim. Biophys. Acta 1063: 36-44, 1991.
    • (1991) Biochim. Biophys. Acta , vol.1063 , pp. 36-44
    • Langosch, D.1    Hartung, K.2    Grell, E.3    Bamberg, E.4    Betz, H.5
  • 84
    • 0028016521 scopus 로고
    • Decreased agonist affinity and chloride conductance of mutant glycine receptors associated with human hereditary hyperekplexia
    • LANGOSCH, D., B. LAUBE, N. RUNDSTROM, V. SCHMIEDEN, J. BORMANN, AND H. BETZ. Decreased agonist affinity and chloride conductance of mutant glycine receptors associated with human hereditary hyperekplexia. EMBO J. 13: 4223-4228, 1994.
    • (1994) EMBO J. , vol.13 , pp. 4223-4228
    • Langosch, D.1    Laube, B.2    Rundstrom, N.3    Schmieden, V.4    Bormann, J.5    Betz, H.6
  • 85
    • 0015788893 scopus 로고
    • Ion transport through pores: A rate-theory analysis
    • LÄUGER, P. Ion transport through pores: a rate-theory analysis. Biochim. Biophys. Acta 311: 423-441, 1973.
    • (1973) Biochim. Biophys. Acta , vol.311 , pp. 423-441
    • Läuger, P.1
  • 86
    • 0023907575 scopus 로고
    • Synthetic amphiphilic peptide models for protein ion channels
    • LEAR, J. D., Z. R. WASSERMAN, AND W. F. DEGRADO. Synthetic amphiphilic peptide models for protein ion channels. Science 240: 1177-1181, 1988.
    • (1988) Science , vol.240 , pp. 1177-1181
    • Lear, J.D.1    Wasserman, Z.R.2    Degrado, W.F.3
  • 88
    • 0020104695 scopus 로고
    • Comparison of Nernst-Planck and reaction-rate models for multiply occupied channels
    • LEVITT, D. G. Comparison of Nernst-Planck and reaction-rate models for multiply occupied channels. Biophys. J. 37: 575-587, 1982.
    • (1982) Biophys. J. , vol.37 , pp. 575-587
    • Levitt, D.G.1
  • 89
    • 0022522698 scopus 로고
    • Interpretation of biological ion channel flux data-reaction-rate versus continuum theory
    • LEVITT, D. G. Interpretation of biological ion channel flux data-reaction-rate versus continuum theory. Annu. Rev. Biophys. Chem. 15: 29-57, 1986.
    • (1986) Annu. Rev. Biophys. Chem. , vol.15 , pp. 29-57
    • Levitt, D.G.1
  • 91
    • 0021063982 scopus 로고
    • Acetylcholine receptor channel ionic selectivity: Ions experience an aqueous environment
    • LEWIS, C. A., AND C. F. STEVENS. Acetylcholine receptor channel ionic selectivity: ions experience an aqueous environment. Proc. Natl. Acad. Sci. USA 80: 6110-6113, 1983.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 6110-6113
    • Lewis, C.A.1    Stevens, C.F.2
  • 92
    • 0029736743 scopus 로고    scopus 로고
    • Flickery block of single CFTR chloride channels by intracellular anions and osmolytes
    • LINSDELL, P., AND J. W. HANRAHAN. Flickery block of single CFTR chloride channels by intracellular anions and osmolytes. Am. J. Physiol. 271 (Cell Physiol. 40): C628-C634, 1996.
    • (1996) Am. J. Physiol. 271 (Cell Physiol. 40) , vol.271
    • Linsdell, P.1    Hanrahan, J.W.2
  • 93
    • 0029861859 scopus 로고    scopus 로고
    • - channels expressed in a mammalian cell line and its regulation by a critical pore residue
    • - channels expressed in a mammalian cell line and its regulation by a critical pore residue. J. Physiol. (Lond.) 496: 687-693, 1996.
    • (1996) J. Physiol. (Lond.) , vol.496 , pp. 687-693
    • Linsdell, P.1    Hanrahan, J.W.2
  • 94
    • 0031954021 scopus 로고    scopus 로고
    • Adenosine triphosphate-dependent asymmetry of anion permeation in the cystic fibrosis transmembrane conductance regulator chloride channel
    • LINSDELL, P., AND J. W. HANRAHAN. Adenosine triphosphate-dependent asymmetry of anion permeation in the cystic fibrosis transmembrane conductance regulator chloride channel. J. Gen. Physiol. 111: 1-14, 1998.
    • (1998) J. Gen. Physiol. , vol.111 , pp. 1-14
    • Linsdell, P.1    Hanrahan, J.W.2
  • 95
    • 0030886246 scopus 로고    scopus 로고
    • Multi-ion mechanism for ion permeation and block in the cystic fibrosis transmembrane conductance regulator chloride channel
    • LINSDELL, P., J. A. TABCHARANI, AND J. W. HANRAHAN. Multi-ion mechanism for ion permeation and block in the cystic fibrosis transmembrane conductance regulator chloride channel. J. Gen. Physiol. 110: 365-377, 1997.
    • (1997) J. Gen. Physiol. , vol.110 , pp. 365-377
    • Linsdell, P.1    Tabcharani, J.A.2    Hanrahan, J.W.3
  • 97
    • 0344101523 scopus 로고    scopus 로고
    • Possible contribution of the peptide backbone to CFTR anion selectivity
    • LINSDELL, P., S.-X. ZHENG, AND J. W. HANRAHAN. Possible contribution of the peptide backbone to CFTR anion selectivity (Abstract). Pediatr. Pulmonol. Suppl. 14: 214, 1997.
    • (1997) Pediatr. Pulmonol. Suppl. , vol.14 , pp. 214
    • Linsdell, P.1    Zheng, S.-X.2    Hanrahan, J.W.3
  • 98
    • 0029012475 scopus 로고
    • Pore loops: An emerging theme in ion channel structure
    • MACKINNON, R. Pore loops: an emerging theme in ion channel structure. Neuron 14: 889-892, 1995.
    • (1995) Neuron , vol.14 , pp. 889-892
    • Mackinnon, R.1
  • 100
    • 0000914532 scopus 로고
    • Solvation of halide anions in dimethyl sulfoxide. Factors involved in enhanced reactivity of negative ions in dipolar aprotic solvents
    • MAGNERA, T. F., G. CALDWELL, J. SUNNER, S. IKUTA, AND P. KEBARLE. Solvation of halide anions in dimethyl sulfoxide. Factors involved in enhanced reactivity of negative ions in dipolar aprotic solvents. J. Am. Chem. Soc. 106: 6140-6146, 1984.
    • (1984) J. Am. Chem. Soc. , vol.106 , pp. 6140-6146
    • Magnera, T.F.1    Caldwell, G.2    Sunner, J.3    Ikuta, S.4    Kebarle, P.5
  • 102
    • 0028133296 scopus 로고
    • A simple empirical model describing the thermodynamics of hydration of ions of widely varying charges, sizes, and shapes
    • MARCUS, Y. A simple empirical model describing the thermodynamics of hydration of ions of widely varying charges, sizes, and shapes. Biophys. Chem. 51: 111-127, 1994.
    • (1994) Biophys. Chem. , vol.51 , pp. 111-127
    • Marcus, Y.1
  • 105
    • 0028111941 scopus 로고
    • Novel pore-lining residues in CFTR that govern permeation and open-channel block
    • MCDONOUGH, S., N. DAVIDSON, H. A. LESTER, AND N. A. MCCARTY. Novel pore-lining residues in CFTR that govern permeation and open-channel block. Neuron 13: 623-634, 1994.
    • (1994) Neuron , vol.13 , pp. 623-634
    • McDonough, S.1    Davidson, N.2    Lester, H.A.3    McCarty, N.A.4
  • 106
    • 0002145089 scopus 로고
    • Single-channel enzymology
    • edited by C. Miller. New York: Plenum
    • MODCZYDLOWSKI, E. Single-channel enzymology. In: Ion Channel Reconstitution, edited by C. Miller. New York: Plenum, 1986, p. 75-113.
    • (1986) Ion Channel Reconstitution , pp. 75-113
    • Modczydlowski, E.1
  • 107
    • 0029870552 scopus 로고    scopus 로고
    • Novel missense mutation (G314R) in a cystic fibrosis patient with hepatic failure
    • NASR, S. Z., T. V. STRONG, M. K. MANSOURA, D. C. DAWSON, AND F. S. COLLINS. Novel missense mutation (G314R) in a cystic fibrosis patient with hepatic failure. Hum. Mutat. 7: 151-154, 1996.
    • (1996) Hum. Mutat. , vol.7 , pp. 151-154
    • Nasr, S.Z.1    Strong, T.V.2    Mansoura, M.K.3    Dawson, D.C.4    Collins, F.S.5
  • 109
    • 0003381942 scopus 로고
    • Anion binding properties of human serum albumin from halide ion quadrupole relaxation
    • NORNE, J. E., S. G. HJALMARSSON, B. LINDMAN, AND M. ZEPPEZAUER. Anion binding properties of human serum albumin from halide ion quadrupole relaxation. Biochemistry 14: 3401-3408, 1975.
    • (1975) Biochemistry , vol.14 , pp. 3401-3408
    • Norne, J.E.1    Hjalmarsson, S.G.2    Lindman, B.3    Zeppezauer, M.4
  • 111
    • 0028058184 scopus 로고
    • Identification of an ion channel-forming motif in the primary structure of CFTR, the cystic fibrosis chloride channel
    • OBLATT-MONTAL, M., G. L. REDDY, T. IWAMOTO, J. M. TOMICH, AND M. MONTAL. Identification of an ion channel-forming motif in the primary structure of CFTR, the cystic fibrosis chloride channel. Proc. Natl. Acad. Sci. USA 91: 1495-1499, 1994.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 1495-1499
    • Oblatt-Montal, M.1    Reddy, G.L.2    Iwamoto, T.3    Tomich, J.M.4    Montal, M.5
  • 112
    • 0027443122 scopus 로고
    • On the mechanism of rectification of the isoproterenol-activated chloride current in guinea-pig ventricular myocytes
    • OVERHOLT, J. L., M. E. HOBERT, AND R. D. HARVEY. On the mechanism of rectification of the isoproterenol-activated chloride current in guinea-pig ventricular myocytes. J. Gen. Physiol. 102: 871-895, 1993.
    • (1993) J. Gen. Physiol. , vol.102 , pp. 871-895
    • Overholt, J.L.1    Hobert, M.E.2    Harvey, R.D.3
  • 113
  • 114
    • 0014707218 scopus 로고
    • Thiocyanate binding with modified bovine plasma albumins
    • PANDE, C. S., AND R. H. MCMENAMY. Thiocyanate binding with modified bovine plasma albumins. Arch. Biochem. Biophys. 136: 260-267, 1970.
    • (1970) Arch. Biochem. Biophys. , vol.136 , pp. 260-267
    • Pande, C.S.1    McMenamy, R.H.2
  • 115
    • 0028068829 scopus 로고
    • Influence of a channel-forming peptide on energy barriers to ion permeation, viewed from a continuum dielectric perspective
    • PARTENSKII, M. B., V. DORMAN, AND P. C. JORDAN. Influence of a channel-forming peptide on energy barriers to ion permeation, viewed from a continuum dielectric perspective. Biophys. J. 67: 1429-1438, 1994.
    • (1994) Biophys. J. , vol.67 , pp. 1429-1438
    • Partenskii, M.B.1    Dorman, V.2    Jordan, P.C.3
  • 116
    • 0020700816 scopus 로고
    • Chloride impermeability in cystic fibrosis
    • QUINTON, P. M. Chloride impermeability in cystic fibrosis. Nature 301: 421-422, 1983.
    • (1983) Nature , vol.301 , pp. 421-422
    • Quinton, P.M.1
  • 118
    • 0024375716 scopus 로고
    • Defective epithelial ion transport in cystic fibrosis
    • QUINTON, P. M. Defective epithelial ion transport in cystic fibrosis. Clin. Chem. 35: 726-730, 1989.
    • (1989) Clin. Chem. , vol.35 , pp. 726-730
    • Quinton, P.M.1
  • 119
    • 0025349031 scopus 로고
    • Cystic fibrosis: A disease in electrolyte transport
    • QUINTON, P. M. Cystic fibrosis: a disease in electrolyte transport. FASEB J. 4: 2709-2717, 1990.
    • (1990) FASEB J. , vol.4 , pp. 2709-2717
    • Quinton, P.M.1
  • 120
    • 33845280446 scopus 로고
    • Comparing the polarities of the amino acids: Side-chain distribution coefficients between the vapor phase, cyclohexane, 1-octanol, and neutral aqueous solution
    • RADZICKA, A., AND R. WOLFENDEN. Comparing the polarities of the amino acids: side-chain distribution coefficients between the vapor phase, cyclohexane, 1-octanol, and neutral aqueous solution. Biochemistry 27: 1664-1670, 1988.
    • (1988) Biochemistry , vol.27 , pp. 1664-1670
    • Radzicka, A.1    Wolfenden, R.2
  • 121
    • 0027255102 scopus 로고
    • Synthetic peptides and four-helix bundle proteins as model systems for the pore-forming structure of channel proteins. II. Transmembrane segment M2 of the brain glycine receptor is a plausible candidate for the pore-lining structure
    • REDDY, G. L., T. IWAMOTO, J. M. TOMICH, AND M. MONTAL. Synthetic peptides and four-helix bundle proteins as model systems for the pore-forming structure of channel proteins. II. Transmembrane segment M2 of the brain glycine receptor is a plausible candidate for the pore-lining structure. J. Biol. Chem. 268: 14608-14615, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 14608-14615
    • Reddy, G.L.1    Iwamoto, T.2    Tomich, J.M.3    Montal, M.4
  • 124
    • 0019203714 scopus 로고
    • Ion conductance and ion selectivity of potassium channels in snail neurones
    • REUTER, H., AND C. F. STEVENS. Ion conductance and ion selectivity of potassium channels in snail neurones. J. Membr. Biol. 57: 103-118, 1980.
    • (1980) J. Membr. Biol. , vol.57 , pp. 103-118
    • Reuter, H.1    Stevens, C.F.2
  • 127
    • 0027197879 scopus 로고
    • Effect of chloride on oxygen binding to crystals of hemoglobin Rothschild (beta 37 Trp→Arg) in the T quaternary structure
    • RIVETTI, C., A. MOZZARELLI, G. L. ROSSI, L. D. KWIATKOWSKI, A. M. WIERZBA, AND R. W. NOBLE. Effect of chloride on oxygen binding to crystals of hemoglobin Rothschild (beta 37 Trp→Arg) in the T quaternary structure. Biochemistry 32: 6411-6418, 1993.
    • (1993) Biochemistry , vol.32 , pp. 6411-6418
    • Rivetti, C.1    Mozzarelli, A.2    Rossi, G.L.3    Kwiatkowski, L.D.4    Wierzba, A.M.5    Noble, R.W.6
  • 129
    • 0029040316 scopus 로고
    • Chemical reconstitution of a chloride pump inactivated by a single point mutation
    • RUDIGER, M., U. HAUPTS, K. GERWERT, AND D. OESTERHELT. Chemical reconstitution of a chloride pump inactivated by a single point mutation. EMBO J. 14: 1599-1606, 1995.
    • (1995) EMBO J. , vol.14 , pp. 1599-1606
    • Rudiger, M.1    Haupts, U.2    Gerwert, K.3    Oesterhelt, D.4
  • 131
    • 0028854587 scopus 로고
    • Extended dipolar chain model for ion channels: Electrostriction effects and the translocational energy barrier
    • SANCHO, M., M. B. PARTENSKII, V. DORMAN, AND P. C. JORDAN. Extended dipolar chain model for ion channels: electrostriction effects and the translocational energy barrier. Biophys. J. 68: 427-433, 1995.
    • (1995) Biophys. J. , vol.68 , pp. 427-433
    • Sancho, M.1    Partenskii, M.B.2    Dorman, V.3    Jordan, P.C.4
  • 132
    • 84956394277 scopus 로고
    • Physical chemistry of protein solutions. Part VII: The binding of some small anions to serum albumin
    • SCATCHARD, G., J. S. COLEMAN, AND A. L. SHEN. Physical chemistry of protein solutions. Part VII: the binding of some small anions to serum albumin. J. Am. Chem. Soc. 79: 12-20, 1956.
    • (1956) J. Am. Chem. Soc. , vol.79 , pp. 12-20
    • Scatchard, G.1    Coleman, J.S.2    Shen, A.L.3
  • 133
    • 33947482491 scopus 로고
    • The physical chemistry of protein solutions. Part XII: The effects of temperature and hydroxide ion on the binding of small anions to human serum albumin
    • SCATCHARD, G., AND W. T. YAP. The physical chemistry of protein solutions. Part XII: the effects of temperature and hydroxide ion on the binding of small anions to human serum albumin. J. Am. Chem. Soc. 86: 3434-3438, 1964.
    • (1964) J. Am. Chem. Soc. , vol.86 , pp. 3434-3438
    • Scatchard, G.1    Yap, W.T.2
  • 135
    • 0028980536 scopus 로고
    • CFTR regulates outwardly rectifying chloride channels through an autocrine mechanism involving ATP
    • SCHWIEBERT, E. M., M. E. EGAN, T. H. HWANG, S. B. FULMER, S. S. ALLEN, G. R. CUTTING, AND W. B. GUGGINO. CFTR regulates outwardly rectifying chloride channels through an autocrine mechanism involving ATP. Cell 81: 1063-1073, 1995.
    • (1995) Cell , vol.81 , pp. 1063-1073
    • Schwiebert, E.M.1    Egan, M.E.2    Hwang, T.H.3    Fulmer, S.B.4    Allen, S.S.5    Cutting, G.R.6    Guggino, W.B.7
  • 138
    • 15844397666 scopus 로고    scopus 로고
    • Contribution of proline residues in the membrane-spanning domains of cystic fibrosis transmembrane conductance regulator to chloride channel function
    • SHEPPARD, D. N., S. M. TRAVIS, H. ISHIHARA, AND M. J. WELSH. Contribution of proline residues in the membrane-spanning domains of cystic fibrosis transmembrane conductance regulator to chloride channel function. J. Biol. Chem. 271: 14995-15001, 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 14995-15001
    • Sheppard, D.N.1    Travis, S.M.2    Ishihara, H.3    Welsh, M.J.4
  • 139
    • 0026759418 scopus 로고
    • + channel regulators on cystic fibrosis transmembrane conductance regulator chloride currents
    • + channel regulators on cystic fibrosis transmembrane conductance regulator chloride currents. J. Gen. Physiol. 100: 573-591, 1992.
    • (1992) J. Gen. Physiol. , vol.100 , pp. 573-591
    • Sheppard, D.N.1    Welsh, M.J.2
  • 140
    • 17544374096 scopus 로고    scopus 로고
    • Disease-associated mutations in the fourth cytoplasmic loop of cystic fibrosis transmembrane conductance regulator compromise biosynthetic processing and chloride channel activity
    • SIEBERT, F. S., P. LINSDELL, T. W. LOO, J. W. HANRAHAN, D. M. CLARKE, AND J. S. RIORDON. Disease-associated mutations in the fourth cytoplasmic loop of cystic fibrosis transmembrane conductance regulator compromise biosynthetic processing and chloride channel activity. J. Biol. Chem. 271: 15139-15145, 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15139-15145
    • Siebert, F.S.1    Linsdell, P.2    Loo, T.W.3    Hanrahan, J.W.4    Clarke, D.M.5    Riordon, J.S.6
  • 141
    • 0027364318 scopus 로고
    • Functional roles of the nucleotide-binding folds in the activation of the cystic fibrosis transmembrane conductance regulator
    • SMIT, L. S., D. J. WILKINSON, M. K. MANSOURA, F. S. COLLINS, AND D. C. DAWSON. Functional roles of the nucleotide-binding folds in the activation of the cystic fibrosis transmembrane conductance regulator. Proc. Natl. Acad. Sci. USA 90: 9963-9967, 1993.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 9963-9967
    • Smit, L.S.1    Wilkinson, D.J.2    Mansoura, M.K.3    Collins, F.S.4    Dawson, D.C.5
  • 145
    • 0026629383 scopus 로고
    • The cystic fibrosis transmembrane conductance regulator chloride channel. Iodide block and permeation
    • TABCHARANI, J. A., X. B. CHANG, J. R. RIORDAN, AND J. W. HANRAHAN. The cystic fibrosis transmembrane conductance regulator chloride channel. Iodide block and permeation. Biophys. J. 62: 1-4, 1992.
    • (1992) Biophys. J. , vol.62 , pp. 1-4
    • Tabcharani, J.A.1    Chang, X.B.2    Riordan, J.R.3    Hanrahan, J.W.4
  • 146
    • 0030964656 scopus 로고    scopus 로고
    • Halide permeation in wild-type and mutant cystic fibrosis transmembrane conductance regulator chloride channels
    • TABCHARANI, J. A., P. LINSDELL, AND J. W. HANRAHAN. Halide permeation in wild-type and mutant cystic fibrosis transmembrane conductance regulator chloride channels. J. Gen. Physiol. 110: 341-354, 1997.
    • (1997) J. Gen. Physiol. , vol.110 , pp. 341-354
    • Tabcharani, J.A.1    Linsdell, P.2    Hanrahan, J.W.3
  • 148
    • 0014986234 scopus 로고
    • Anion interaction at the inhibitory post-synaptic membrane of the crayfish neuromuscular junction
    • TAKEUCHI, A., AND N. TAKEUCHI. Anion interaction at the inhibitory post-synaptic membrane of the crayfish neuromuscular junction. J. Physiol. (Lond.) 212: 337-351, 1971.
    • (1971) J. Physiol. (Lond.) , vol.212 , pp. 337-351
    • Takeuchi, A.1    Takeuchi, N.2
  • 149
    • 84980107151 scopus 로고
    • The distinction by means of tracers between active transport and diffusion
    • USSING, H. H. The distinction by means of tracers between active transport and diffusion. Acta Physiol. Scand. 19: 43-56, 1949.
    • (1949) Acta Physiol. Scand. , vol.19 , pp. 43-56
    • Ussing, H.H.1
  • 150
    • 0002420060 scopus 로고
    • Some aspects of the application of tracers in permeability studies
    • USSING, H. H. Some aspects of the application of tracers in permeability studies. Adv. Enzymol. 13: 21-65, 1952.
    • (1952) Adv. Enzymol. , vol.13 , pp. 21-65
    • Ussing, H.H.1
  • 151
    • 0011199354 scopus 로고
    • Interpretation of tracer fluxes
    • edited by G. Giebisch, D. C. Testeson, and H. H. Ussing. Berlin: Springer-Verlag
    • USSING, H. H. Interpretation of tracer fluxes. In: Membrane Transport in Biology, edited by G. Giebisch, D. C. Testeson, and H. H. Ussing. Berlin: Springer-Verlag, 1978, p. 115-140.
    • (1978) Membrane Transport in Biology , pp. 115-140
    • Ussing, H.H.1
  • 152
    • 0023612184 scopus 로고
    • Chloride-thiocyanate interactions in frog muscle anion-conducting channels at pH 5
    • VAUGHAN, P. C. Chloride-thiocyanate interactions in frog muscle anion-conducting channels at pH 5. Pflügers Arch. 410: 153-158, 1987.
    • (1987) Pflügers Arch. , vol.410 , pp. 153-158
    • Vaughan, P.C.1
  • 155
    • 0028285064 scopus 로고
    • Anion-protein interactions during halorhodopsin pumping: Halide binding at the protonated Schiff base
    • WALTER, T. J., AND M. S. BRAIMAN. Anion-protein interactions during halorhodopsin pumping: halide binding at the protonated Schiff base. Biochemistry 33: 1724-1733, 1994.
    • (1994) Biochemistry , vol.33 , pp. 1724-1733
    • Walter, T.J.1    Braiman, M.S.2
  • 156
    • 0023028803 scopus 로고
    • The systematic characterization by aqueous column chromatography of solutes which affect protein stability
    • WASHABAUGH, M. W., AND K. D. COLLINS. The systematic characterization by aqueous column chromatography of solutes which affect protein stability. J. Biol. Chem. 261: 12477-12485, 1986.
    • (1986) J. Biol. Chem. , vol.261 , pp. 12477-12485
    • Washabaugh, M.W.1    Collins, K.D.2
  • 158
    • 0030045751 scopus 로고    scopus 로고
    • CFTR: The nucleotide binding folds regulate the accessibility and stability of the activated state
    • WILKINSON, D. J., M. K. MANSOURA, P. Y. WATSON, L. S. SMIT, F. S. COLLINS, AND D. C. DAWSON. CFTR: the nucleotide binding folds regulate the accessibility and stability of the activated state. J. Gen. Physiol. 107: 103-119, 1996.
    • (1996) J. Gen. Physiol. , vol.107 , pp. 103-119
    • Wilkinson, D.J.1    Mansoura, M.K.2    Watson, P.Y.3    Smit, L.S.4    Collins, F.S.5    Dawson, D.C.6
  • 160
    • 84949812020 scopus 로고
    • Erying rate theory model of the current-voltage relationships of ion channels in excitable membranes
    • edited by J. Hirschfelder. New York: Wiley
    • WOODBURY, J. W. Erying rate theory model of the current-voltage relationships of ion channels in excitable membranes. In: Chemical Dynamics: Papers in Honor of Henry Erying, edited by J. Hirschfelder. New York: Wiley, 1971, p. 601-617.
    • (1971) Chemical Dynamics: Papers in Honor of Henry Erying , pp. 601-617
    • Woodbury, J.W.1
  • 161
    • 0015879604 scopus 로고
    • Ionic blockage of sodium channels in nerve
    • WOODHULL, A. M. Ionic blockage of sodium channels in nerve. J. Gen. Physiol. 61: 687-708, 1973.
    • (1973) J. Gen. Physiol. , vol.61 , pp. 687-708
    • Woodhull, A.M.1
  • 162
    • 0017619677 scopus 로고
    • Anion selectivity in biological systems
    • WRIGHT, E. M., AND J. M. DIAMOND. Anion selectivity in biological systems. Physiol. Rev. 57: 109-156, 1977.
    • (1977) Physiol. Rev. , vol.57 , pp. 109-156
    • Wright, E.M.1    Diamond, J.M.2
  • 163
    • 0030021584 scopus 로고    scopus 로고
    • Molecular basis of charge movement in voltage-gated sodium channels
    • YANG, N., A. L. GEORGE, JR., AND R. HORN. Molecular basis of charge movement in voltage-gated sodium channels. Neuron 16: 113-122, 1996.
    • (1996) Neuron. , vol.16 , pp. 113-122
    • Yang, N.1    George, A.L.2    Horn, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.