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Volumn 222, Issue 2, 2008, Pages 91-106

Mutations at arginine 352 alter the pore architecture of CFTR

Author keywords

Anion selectivity; Blocker; CFTR; Channel open state; Chloride channel; Salt bridge; Subconductance

Indexed keywords

ANION; ARGININE; GLIPIZIDE; TRANSMEMBRANE CONDUCTANCE REGULATOR;

EID: 43549091314     PISSN: 00222631     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00232-008-9105-9     Document Type: Article
Times cited : (45)

References (66)
  • 1
    • 34248173904 scopus 로고    scopus 로고
    • Specific recognition of saturated and 4,5-unsaturated hexuronate sugars by a periplasmic binding protein involved in pectin catabolism
    • Abbott DW, Boraston AB (2007) Specific recognition of saturated and 4,5-unsaturated hexuronate sugars by a periplasmic binding protein involved in pectin catabolism. J Mol Biol 369:759-770
    • (2007) J Mol Biol , vol.369 , pp. 759-770
    • Abbott, D.W.1    Boraston, A.B.2
  • 5
    • 0029126565 scopus 로고
    • Search for mutations in pancreatic sufficient cystic fibrosis Italian patients: Detection of 90% of molecular defects and identification of three novel mutations
    • Brancolini V, Cremonesi L, Belloni E, Pappalardo E, Bordoni R, Seia M, Rady M, Russo MP, Romeo G, Devoto M (1995) Search for mutations in pancreatic sufficient cystic fibrosis Italian patients: detection of 90% of molecular defects and identification of three novel mutations. Hum Genet 96:312-318
    • (1995) Hum Genet , vol.96 , pp. 312-318
    • Brancolini, V.1    Cremonesi, L.2    Belloni, E.3    Pappalardo, E.4    Bordoni, R.5    Seia, M.6    Rady, M.7    Russo, M.P.8    Romeo, G.9    Devoto, M.10
  • 6
    • 34948822308 scopus 로고    scopus 로고
    • Docking of the periplasmic FecB binding protein to the FecCD transmembrane proteins in the ferric citrate transport system of Escherichia coli
    • Braun V, Herrmann C (2007) Docking of the periplasmic FecB binding protein to the FecCD transmembrane proteins in the ferric citrate transport system of Escherichia coli. J Bacteriol 189:6913-6918
    • (2007) J Bacteriol , vol.189 , pp. 6913-6918
    • Braun, V.1    Herrmann, C.2
  • 7
    • 0034893723 scopus 로고    scopus 로고
    • A combined analysis of the cystic fibrosis transmembrane conductance regulator: Implications for structure and disease models
    • Chen JM, Cutler C, Jacques C, Boefu G, Denamur E, Lecointre G, Mercier B, Cramb G, Férec C (2001) A combined analysis of the cystic fibrosis transmembrane conductance regulator: implications for structure and disease models. Mol Biol Evol 18:1771-1788
    • (2001) Mol Biol Evol , vol.18 , pp. 1771-1788
    • Chen, J.M.1    Cutler, C.2    Jacques, C.3    Boefu, G.4    Denamur, E.5    Lecointre, G.6    Mercier, B.7    Cramb, G.8    Férec, C.9
  • 9
    • 0025987020 scopus 로고
    • Phosphorylation of the R domain by cAMP-dependent protein kinase regulates the CFTR chloride channel
    • Cheng SH, Rich DP, Marshall J, Gregory RJ, Welsh MW, Smith AE (1991) Phosphorylation of the R domain by cAMP-dependent protein kinase regulates the CFTR chloride channel. Cell 66:1027-1036
    • (1991) Cell , vol.66 , pp. 1027-1036
    • Cheng, S.H.1    Rich, D.P.2    Marshall, J.3    Gregory, R.J.4    Welsh, M.W.5    Smith, A.E.6
  • 10
    • 0030893916 scopus 로고    scopus 로고
    • Locating the anion-selectivity filter of the cystic fibrosis transmembrane conductance regulator (CFTR) chloride channel
    • Cheung M, Akabas MH (1997) Locating the anion-selectivity filter of the cystic fibrosis transmembrane conductance regulator (CFTR) chloride channel. J Gen Physiol 109:289-299
    • (1997) J Gen Physiol , vol.109 , pp. 289-299
    • Cheung, M.1    Akabas, M.H.2
  • 12
    • 0033605158 scopus 로고    scopus 로고
    • Cystic fibrosis-associated mutations at arginine 347 alter the pore architecture for CFTR: Evidence for disruption of a salt bridge
    • Cotten JF, Welsh MJ (1999) Cystic fibrosis-associated mutations at arginine 347 alter the pore architecture for CFTR: evidence for disruption of a salt bridge. J Biol Chem 274:5429-5435
    • (1999) J Biol Chem , vol.274 , pp. 5429-5435
    • Cotten, J.F.1    Welsh, M.J.2
  • 13
    • 10344247673 scopus 로고    scopus 로고
    • Salt bridges and gating in the COOH-terminal region of HCN2 and CNGA1 channels
    • Craven KB, Zagotta WN (2004) Salt bridges and gating in the COOH-terminal region of HCN2 and CNGA1 channels. J Gen Physiol 124:663-677
    • (2004) J Gen Physiol , vol.124 , pp. 663-677
    • Craven, K.B.1    Zagotta, W.N.2
  • 15
    • 0027018275 scopus 로고
    • Four new mutations of the CFTR gene (541delC, R347H, R352Q, E585X) detected by DGGE analysis in Italian CF patients, associated with different clinical phenotypes
    • Cremonesi L, Ferrari M, Belloni E, Magnani C, Seia M, Ronchetto P, Rady M, Russo MP, Romeo G, Devoto M (1992) Four new mutations of the CFTR gene (541delC, R347H, R352Q, E585X) detected by DGGE analysis in Italian CF patients, associated with different clinical phenotypes. Hum Mutat 1:314-319
    • (1992) Hum Mutat , vol.1 , pp. 314-319
    • Cremonesi, L.1    Ferrari, M.2    Belloni, E.3    Magnani, C.4    Seia, M.5    Ronchetto, P.6    Rady, M.7    Russo, M.P.8    Romeo, G.9    Devoto, M.10
  • 16
    • 0034953105 scopus 로고    scopus 로고
    • The human ATP-binding cassette (ABC) transporter superfamily
    • Dean M, Homon Y, Chimini G (2001) The human ATP-binding cassette (ABC) transporter superfamily. J Lipid Res 42:1007-1017
    • (2001) J Lipid Res , vol.42 , pp. 1007-1017
    • Dean, M.1    Homon, Y.2    Chimini, G.3
  • 17
    • 0031425728 scopus 로고    scopus 로고
    • CFTR: Domains, structure, and function
    • Devidas S, Guggino WB (1997) CFTR: domains, structure, and function. J Bioenerg Biomemb 29:443-451
    • (1997) J Bioenerg Biomemb , vol.29 , pp. 443-451
    • Devidas, S.1    Guggino, W.B.2
  • 19
    • 33645307384 scopus 로고    scopus 로고
    • The ABC protein turned chloride channel whose failure causes cystic fibrosis
    • Gadsby DC, Vergani P, Csanády L (2006) The ABC protein turned chloride channel whose failure causes cystic fibrosis. Nature 440:477-483
    • (2006) Nature , vol.440 , pp. 477-483
    • Gadsby, D.C.1    Vergani, P.2    Csanády, L.3
  • 20
    • 11244339684 scopus 로고    scopus 로고
    • Direct comparison of the functional roles played by different transmembrane regions in the cystic fibrosis transmembrane conductance regulator chloride channel pore
    • Ge N, Muise C, Gong X, Linsdell P (2004) Direct comparison of the functional roles played by different transmembrane regions in the cystic fibrosis transmembrane conductance regulator chloride channel pore. J Biol Chem 279:55283-55289
    • (2004) J Biol Chem , vol.279 , pp. 55283-55289
    • Ge, N.1    Muise, C.2    Gong, X.3    Linsdell, P.4
  • 21
    • 0035342450 scopus 로고    scopus 로고
    • Residue frequencies and pairing preferences at protein-protein interfaces
    • Glaser F, Steinberg DM, Vakser IA, Ben-Tal N (2001) Residue frequencies and pairing preferences at protein-protein interfaces. Proteins 43:89-102
    • (2001) Proteins , vol.43 , pp. 89-102
    • Glaser, F.1    Steinberg, D.M.2    Vakser, I.A.3    Ben-Tal, N.4
  • 22
    • 33745772850 scopus 로고    scopus 로고
    • New insights into cystic fibrosis: Molecular switches that regulate CFTR
    • Guggino WB, Stanton BA (2006) New insights into cystic fibrosis: molecular switches that regulate CFTR. Nat Rev Mol Cell Biol 7:426-436
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 426-436
    • Guggino, W.B.1    Stanton, B.A.2
  • 23
    • 0033608961 scopus 로고    scopus 로고
    • Arg352 is a major determinant of charge selectivity in the cystic fibrosis transmembrane conductance regulator chloride channel
    • Guinamard R, Akabas MH (1999) Arg352 is a major determinant of charge selectivity in the cystic fibrosis transmembrane conductance regulator chloride channel. Biochemistry 38:5528-5537
    • (1999) Biochemistry , vol.38 , pp. 5528-5537
    • Guinamard, R.1    Akabas, M.H.2
  • 24
    • 0028340159 scopus 로고
    • Regulation of the gating of cystic fibrosis transmembrane conductance regulator Cl channels by phosphorylation and ATP hydrolysis
    • Hwang T-C, Nagel G, Nairn AC, Gadsby DC (1994) 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) 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
  • 25
    • 0026087282 scopus 로고
    • The interaction between aspartic acid 237 and lysine 358 in the lactose carrier of Escherichia coli
    • King SC, Hansen CL, Wilson TH (1991) The interaction between aspartic acid 237 and lysine 358 in the lactose carrier of Escherichia coli. Biochim Biophys Acta 1062:177-186
    • (1991) Biochim Biophys Acta , vol.1062 , pp. 177-186
    • King, S.C.1    Hansen, C.L.2    Wilson, T.H.3
  • 26
    • 29344433036 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli SufC, an ABC-type ATPase component of the SUF iron-sulfur cluster assembly machinery
    • Kitaoka S, Wada K, Hasegawa Y, Minami Y, Fukuyama K, Takahashi Y (2006) Crystal structure of Escherichia coli SufC, an ABC-type ATPase component of the SUF iron-sulfur cluster assembly machinery. FEBS Lett 580:137-143
    • (2006) FEBS Lett , vol.580 , pp. 137-143
    • Kitaoka, S.1    Wada, K.2    Hasegawa, Y.3    Minami, Y.4    Fukuyama, K.5    Takahashi, Y.6
  • 27
    • 0034864534 scopus 로고    scopus 로고
    • Thiocyanate as a probe of the cystic fibrosis transmembrane conductance regulator chloride channel pore
    • Linsdell P (2001) Thiocyanate as a probe of the cystic fibrosis transmembrane conductance regulator chloride channel pore. Can J Physiol Pharmacol 79:573-579
    • (2001) Can J Physiol Pharmacol , vol.79 , pp. 573-579
    • Linsdell, P.1
  • 28
    • 15744390354 scopus 로고    scopus 로고
    • Location of a common inhibitor binding site in the cytoplasmic vestibule of the cystic fibrosis transmembrane conductance regulator chloride channel pore
    • Linsdell P (2005) Location of a common inhibitor binding site in the cytoplasmic vestibule of the cystic fibrosis transmembrane conductance regulator chloride channel pore. J Biol Chem 280:8945-8950
    • (2005) J Biol Chem , vol.280 , pp. 8945-8950
    • Linsdell, P.1
  • 29
    • 32544435783 scopus 로고    scopus 로고
    • Mechanism of chloride permeation in the cystic fibrosis transmembrane conductance regulator chloride channel
    • Linsdell P (2006) Mechanism of chloride permeation in the cystic fibrosis transmembrane conductance regulator chloride channel. Exp Physiol 91:123-129
    • (2006) Exp Physiol , vol.91 , pp. 123-129
    • Linsdell, P.1
  • 30
    • 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 496:687-693
    • (1996) J Physiol , vol.496 , pp. 687-693
    • Linsdell, P.1    Hanrahan, J.W.2
  • 31
    • 0029736743 scopus 로고    scopus 로고
    • Flickery block of single CFTR chloride channels by intracellular anions and osmolytes
    • Linsdell P, Hanrahan JW (1996b) Flickery block of single CFTR chloride channels by intracellular anions and osmolytes. Am J Physiol 271:C628-C634
    • (1996) Am J Physiol , vol.271
    • Linsdell, P.1    Hanrahan, J.W.2
  • 33
    • 0034084793 scopus 로고    scopus 로고
    • Molecular determinants of anion selectivity in the cystic fibrosis transmembrane conductance regulator chloride channel pore
    • Linsdell P, Evagelidis A, Hanrahan JW (2000) Molecular determinants of anion selectivity in the cystic fibrosis transmembrane conductance regulator chloride channel pore. Biophys J 78:2973-2982
    • (2000) Biophys J , vol.78 , pp. 2973-2982
    • Linsdell, P.1    Evagelidis, A.2    Hanrahan, J.W.3
  • 34
    • 0031668883 scopus 로고    scopus 로고
    • The spontaneous gating activity of OmpC porin is affected by mutations of a putative hydrogen bond network or of a salt bridge between the L3 loop and the barrel
    • Liu NZ, Delcour AH (1998) The spontaneous gating activity of OmpC porin is affected by mutations of a putative hydrogen bond network or of a salt bridge between the L3 loop and the barrel. Protein Eng 11:797-802
    • (1998) Protein Eng , vol.11 , pp. 797-802
    • Liu, N.Z.1    Delcour, A.H.2
  • 35
    • 10044283304 scopus 로고    scopus 로고
    • CFTR: A cysteine at position 338 in TM6 senses a positive electrostatic potential in the pore
    • Liu X, Zhang Z-R, Fuller MD, Billingsley J, McCarty NA, Dawson DC (2004) CFTR: a cysteine at position 338 in TM6 senses a positive electrostatic potential in the pore. Biophys J 87:3826-3841
    • (2004) Biophys J , vol.87 , pp. 3826-3841
    • Liu, X.1    Zhang, Z.-R.2    Fuller, M.D.3    Billingsley, J.4    McCarty, N.A.5    Dawson, D.C.6
  • 36
    • 0033898228 scopus 로고    scopus 로고
    • Permeation through the CFTR chloride channel
    • McCarty NA (2000) Permeation through the CFTR chloride channel. J Exp Biol 203:1947-1962
    • (2000) J Exp Biol , vol.203 , pp. 1947-1962
    • McCarty, N.A.1
  • 37
    • 0034785913 scopus 로고    scopus 로고
    • Identification of a region of strong discrimination in the pore of CFTR
    • McCarty NA, Zhang Z-R (2001) Identification of a region of strong discrimination in the pore of CFTR. Am J Physiol 281:L852-L867
    • (2001) Am J Physiol , vol.281
    • McCarty, N.A.1    Zhang, Z.-R.2
  • 38
    • 0028111941 scopus 로고
    • Novel pore-lining residues in CFTR that govern permeation and open-channel block
    • McDonough S, Davidson N, Lester HA, McCarty NA (1994) Novel pore-lining residues in CFTR that govern permeation and open-channel block. Neuron 13:623-634
    • (1994) Neuron , vol.13 , pp. 623-634
    • McDonough, S.1    Davidson, N.2    Lester, H.A.3    McCarty, N.A.4
  • 39
    • 0018094892 scopus 로고
    • Electrostatic effects in proteins
    • Perutz MF (1978) Electrostatic effects in proteins. Science 201:1187-1191
    • (1978) Science , vol.201 , pp. 1187-1191
    • Perutz, M.F.1
  • 40
    • 0030061670 scopus 로고    scopus 로고
    • Estimating single-channel kinetic parameters from idealized patch clamp data containing missed events
    • Qin F, Auerbach A, Sachs F (1996) Estimating single-channel kinetic parameters from idealized patch clamp data containing missed events. Biophys J 70:264-280
    • (1996) Biophys J , vol.70 , pp. 264-280
    • Qin, F.1    Auerbach, A.2    Sachs, F.3
  • 41
    • 0035807019 scopus 로고    scopus 로고
    • A monomer is the minimum function unit required for channel and ATPase activity of the cystic fibrosis transmembrane conductance regulator
    • Ramjeesingh M, Li C, Kogan I, Wang Y, Huan L-J, Bear CE (2001) A monomer is the minimum function unit required for channel and ATPase activity of the cystic fibrosis transmembrane conductance regulator. Biochemistry 40:10700-10706
    • (2001) Biochemistry , vol.40 , pp. 10700-10706
    • Ramjeesingh, M.1    Li, C.2    Kogan, I.3    Wang, Y.4    Huan, L.-J.5    Bear, C.E.6
  • 42
    • 0242637061 scopus 로고    scopus 로고
    • Stable dimeric assembly of the second membrane-spanning domain of CFTR (cystic fibrosis transmembrane conductance regulator) reconstitutes a chloride-selective pore
    • Ramjeesingh M, Ugwu F, Li C, Dhani S, Huan L-J, Wang Y, Bear CE (2003) Stable dimeric assembly of the second membrane-spanning domain of CFTR (cystic fibrosis transmembrane conductance regulator) reconstitutes a chloride-selective pore. Biochemistry 375:633-641
    • (2003) Biochemistry , vol.375 , pp. 633-641
    • Ramjeesingh, M.1    Ugwu, F.2    Li, C.3    Dhani, S.4    Huan, L.-J.5    Wang, Y.6    Bear, C.E.7
  • 45
    • 0025283002 scopus 로고
    • Electrostatic interactions in macromolecules: Theory and applications
    • Sharp KA, Honig B (1990) Electrostatic interactions in macromolecules: theory and applications. Annu Rev Biophys Biophys Chem 19:301-332
    • (1990) Annu Rev Biophys Biophys Chem , vol.19 , pp. 301-332
    • Sharp, K.A.1    Honig, B.2
  • 46
    • 0030847723 scopus 로고    scopus 로고
    • - channels expressed in a murine cell line
    • - channels expressed in a murine cell line. J Physiol 503:333-345
    • (1997) J Physiol , vol.503 , pp. 333-345
    • Sheppard, D.N.1    Robinson, K.A.2
  • 47
    • 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 100:573-592
    • (1992) J Gen Physiol , vol.100 , pp. 573-592
    • Sheppard, D.N.1    Welsh, M.J.2
  • 49
    • 15844397666 scopus 로고    scopus 로고
    • Contributions of proline residues in the membrane-spanning domains of the cystic fibrosis transmembrane conductance regulator to chloride channel function
    • Sheppard DN, Travis SM, Ishihara H, Welsh MJ (1996) Contributions of proline residues in the membrane-spanning domains of the cystic fibrosis transmembrane conductance regulator to chloride channel function. J Biol Chem 271:14995-15001
    • (1996) J Biol Chem , vol.271 , pp. 14995-15001
    • Sheppard, D.N.1    Travis, S.M.2    Ishihara, H.3    Welsh, M.J.4
  • 50
    • 0032795083 scopus 로고    scopus 로고
    • Cystic fibrosis transmembrane conductance regulator: Physical basis for lyotropic anion selectivity patterns
    • Smith SS, Steinle ED, Meyerhoff ME, Dawson DC (1999) Cystic fibrosis transmembrane conductance regulator: physical basis for lyotropic anion selectivity patterns. J Gen Physiol 114:799-817
    • (1999) J Gen Physiol , vol.114 , pp. 799-817
    • Smith, S.S.1    Steinle, E.D.2    Meyerhoff, M.E.3    Dawson, D.C.4
  • 52
    • 33750530196 scopus 로고    scopus 로고
    • Positive charges at the intracellular mouth of the pore regulate anion conduction in the CFTR chloride channel
    • St. Aubin CN, Linsdell P (2006) Positive charges at the intracellular mouth of the pore regulate anion conduction in the CFTR chloride channel. J Gen Physiol 128:535-545
    • (2006) J Gen Physiol , vol.128 , pp. 535-545
    • St. Aubin, C.N.1    Linsdell, P.2
  • 53
    • 27744606438 scopus 로고    scopus 로고
    • A salt-bridge motif involved in ligand binding and large-scale domain motions of the maltose-binding protein
    • Stockner T, Vogel HJ, Tieleman DP (2005) A salt-bridge motif involved in ligand binding and large-scale domain motions of the maltose-binding protein. Biophys J 89:3362-3371
    • (2005) Biophys J , vol.89 , pp. 3362-3371
    • Stockner, T.1    Vogel, H.J.2    Tieleman, D.P.3
  • 55
    • 0030964656 scopus 로고    scopus 로고
    • Halide permeation in wild-type and mutant cystic fibrosis transmembrane conductance regulator chloride channels
    • Tabcharani JA, Linsdell P, Hanrahan JW (1997) Halide permeation in wild-type and mutant cystic fibrosis transmembrane conductance regulator chloride channels. J Gen Physiol 110:341-351
    • (1997) J Gen Physiol , vol.110 , pp. 341-351
    • Tabcharani, J.A.1    Linsdell, P.2    Hanrahan, J.W.3
  • 56
    • 0033570916 scopus 로고    scopus 로고
    • An unstable transmembrane segment in the cystic fibrosis transmembrane conductance regulator
    • Tector M, Hartl FU (1999) An unstable transmembrane segment in the cystic fibrosis transmembrane conductance regulator. EMBO J 18:6290-6298
    • (1999) EMBO J , vol.18 , pp. 6290-6298
    • Tector, M.1    Hartl, F.U.2
  • 58
    • 0031019498 scopus 로고    scopus 로고
    • Stabilization of ion selectivity filter by pore loop pairs in an inwardly rectifying potassium channel
    • Yang J, Yu M, Jan YN, Jan LY (1997) Stabilization of ion selectivity filter by pore loop pairs in an inwardly rectifying potassium channel. Proc Natl Acad Sci USA 94:1568-1572
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 1568-1572
    • Yang, J.1    Yu, M.2    Jan, Y.N.3    Jan, L.Y.4
  • 59
    • 0034616134 scopus 로고    scopus 로고
    • The two halves of CFTR form a dual-pore ion channel
    • Yue H, Devidas S, Guggino WB (2000) The two halves of CFTR form a dual-pore ion channel. J Biol Chem 275:10030-10034
    • (2000) J Biol Chem , vol.275 , pp. 10030-10034
    • Yue, H.1    Devidas, S.2    Guggino, W.B.3
  • 61
    • 0033931302 scopus 로고    scopus 로고
    • Interaction between permeation and gating in a putative pore-domain mutant in CFTR
    • Zhang Z-R, McDonough SI, McCarty NA (2000) Interaction between permeation and gating in a putative pore-domain mutant in CFTR. Biophys J 79:298-313
    • (2000) Biophys J , vol.79 , pp. 298-313
    • Zhang, Z.-R.1    McDonough, S.I.2    McCarty, N.A.3
  • 62
    • 0036085876 scopus 로고    scopus 로고
    • Voltage-sensitive gating induced by a mutation in the fifth transmembrane domain of CFTR
    • Zhang Z-R, Zeltwanger S, Smith SS, Dawson DC, McCarty NA (2001) Voltage-sensitive gating induced by a mutation in the fifth transmembrane domain of CFTR. Am J Physiol 282:L135-L145
    • (2001) Am J Physiol , vol.282
    • Zhang, Z.-R.1    Zeltwanger, S.2    Smith, S.S.3    Dawson, D.C.4    McCarty, N.A.5
  • 63
    • 15744363180 scopus 로고    scopus 로고
    • Time-dependent interactions of glibenclamide with CFTR: Kinetically complex block of macroscopic currents
    • Zhang Z-R, Cui G, Zeltwanger S, McCarty NA (2004a) Time-dependent interactions of glibenclamide with CFTR: kinetically complex block of macroscopic currents. J Membr Biol 201:139-155
    • (2004) J Membr Biol , vol.201 , pp. 139-155
    • Zhang, Z.-R.1    Cui, G.2    Zeltwanger, S.3    McCarty, N.A.4
  • 64
    • 2942659790 scopus 로고    scopus 로고
    • Steady-state interactions of glibenclamide with CFTR: Evidence for multiple sites
    • Zhang Z-R, Zeltwanger S, McCarty NA (2004b) Steady-state interactions of glibenclamide with CFTR: evidence for multiple sites. J Membr Biol 199:15-28
    • (2004) J Membr Biol , vol.199 , pp. 15-28
    • Zhang, Z.-R.1    Zeltwanger, S.2    McCarty, N.A.3
  • 65
    • 12844277303 scopus 로고    scopus 로고
    • Determination of the functional unit of the cystic fibrosis transmembrane conductance regulator chloride channel: One polypeptide forms one pore
    • Zhang Z-R, Cui G, Liu X, Song B, Dawson DC, McCarty NA (2005a) Determination of the functional unit of the cystic fibrosis transmembrane conductance regulator chloride channel: one polypeptide forms one pore. J Biol Chem 280:458-468
    • (2005) J Biol Chem , vol.280 , pp. 458-468
    • Zhang, Z.-R.1    Cui, G.2    Liu, X.3    Song, B.4    Dawson, D.C.5    McCarty, N.A.6
  • 66
    • 29644442896 scopus 로고    scopus 로고
    • State-dependent chemical reactivity of an engineered cysteine reveals conformational changes in the outer vestibule of CFTR
    • Zhang Z-R, Song B, McCarty NA (2005b) State-dependent chemical reactivity of an engineered cysteine reveals conformational changes in the outer vestibule of CFTR. J Biol Chem 280:41997-42003
    • (2005) J Biol Chem , vol.280 , pp. 41997-42003
    • Zhang, Z.-R.1    Song, B.2    McCarty, N.A.3


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