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Volumn 72, Issue 7, 2015, Pages 1377-1403

Full-open and closed CFTR channels, with lateral tunnels from the cytoplasm and an alternative position of the F508 region, as revealed by molecular dynamics

Author keywords

ABC exporters; CFTR; Chloride channel; Molecular dynamics; Molecular modeling

Indexed keywords

AMINO ACID; CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR; MUTANT PROTEIN;

EID: 84928493859     PISSN: 1420682X     EISSN: 14209071     Source Type: Journal    
DOI: 10.1007/s00018-014-1749-2     Document Type: Article
Times cited : (71)

References (104)
  • 1
    • 84893088864 scopus 로고    scopus 로고
    • Functional architecture of the CFTR chloride channel
    • 1:CAS:528:DC%2BC2cXht1Oqsbo%3D 24341413
    • Linsdell P (2014) Functional architecture of the CFTR chloride channel. Mol Membr Biol 31:1-16
    • (2014) Mol Membr Biol , vol.31 , pp. 1-16
    • Linsdell, P.1
  • 2
    • 84901605375 scopus 로고    scopus 로고
    • Understanding how cystic fibrosis mutations disrupt CFTR function: From single molecules to animal models
    • 1:CAS:528:DC%2BC2cXntFygu7Y%3D 24727426
    • Wang Y, Wrennall J, Cai Z, Li H, Sheppard DN (2014) Understanding how cystic fibrosis mutations disrupt CFTR function: from single molecules to animal models. Int J Biochem Cell Biol 52:47-57
    • (2014) Int J Biochem Cell Biol , vol.52 , pp. 47-57
    • Wang, Y.1    Wrennall, J.2    Cai, Z.3    Li, H.4    Sheppard, D.N.5
  • 3
    • 84879000844 scopus 로고    scopus 로고
    • Cystic fibrosis transmembrane regulator correctors and potentiators
    • 23818513
    • Rowe SM, Verkman AS (2013) Cystic fibrosis transmembrane regulator correctors and potentiators. Cold Spring Harb Perspect Med 3(7):a009761
    • (2013) Cold Spring Harb Perspect Med , vol.3 , Issue.7
    • Rowe, S.M.1    Verkman, A.S.2
  • 4
    • 34548853133 scopus 로고    scopus 로고
    • Structure and mechanism of ABC transporter proteins
    • 1:CAS:528:DC%2BD2sXhtFSltb3L 17723295
    • Hollenstein K, Dawson JP, Locker KP (2007) Structure and mechanism of ABC transporter proteins. Curr Opin Struct Biol 17:412-418
    • (2007) Curr Opin Struct Biol , vol.17 , pp. 412-418
    • Hollenstein, K.1    Dawson, J.P.2    Locker, K.P.3
  • 5
    • 84880065252 scopus 로고    scopus 로고
    • Two salts bridges differentially contribute to the maintenance of cystic fibrosis transmembrane conductance regulator (CFTR) channel function
    • 3711338 1:CAS:528:DC%2BC3sXhtV2rurnF 23709221
    • Cui G, Freeman CS, Knotts T, Prince CZ, Kuang C, McCarty NA (2013) Two salts bridges differentially contribute to the maintenance of cystic fibrosis transmembrane conductance regulator (CFTR) channel function. J Biol Chem 288:20758-20767
    • (2013) J Biol Chem , vol.288 , pp. 20758-20767
    • Cui, G.1    Freeman, C.S.2    Knotts, T.3    Prince, C.Z.4    Kuang, C.5    McCarty, N.A.6
  • 6
    • 50249090046 scopus 로고    scopus 로고
    • Atomic model of human cystic fibrosis transmembrane conductance regulator: Membrane-spanning domains and coupling interfaces
    • 1:CAS:528:DC%2BD1cXhtVansr3L 18597042
    • Mornon J-P, Lehn P, Callebaut I (2008) Atomic model of human cystic fibrosis transmembrane conductance regulator: membrane-spanning domains and coupling interfaces. Cell Mol Life Sci 65:2594-2612
    • (2008) Cell Mol Life Sci , vol.65 , pp. 2594-2612
    • Mornon, J.-P.1    Lehn, P.2    Callebaut, I.3
  • 7
    • 42149120706 scopus 로고    scopus 로고
    • Phenylalanine-508 mediates a cytoplasmic-membrane domain contact in the CFTR 3D structure crucial to assembly and channel function
    • 2265173 1:CAS:528:DC%2BD1cXjtlKksbw%3D 18305154
    • Serohijos AW, Hegedus T, Aleksandrov AA, He L, Cui L, Dokholyan NV et al (2008) Phenylalanine-508 mediates a cytoplasmic-membrane domain contact in the CFTR 3D structure crucial to assembly and channel function. Proc Natl Acad Sci USA 105:3256-3261
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 3256-3261
    • Serohijos, A.W.1    Hegedus, T.2    Aleksandrov, A.A.3    He, L.4    Cui, L.5    Dokholyan, N.V.6
  • 8
    • 33748644877 scopus 로고    scopus 로고
    • Structure of a bacterial multidrug ABC transporter
    • 1:CAS:528:DC%2BD28XpsVansLY%3D 16943773
    • Dawson RJ, Locher KP (2006) Structure of a bacterial multidrug ABC transporter. Nature 443:180-185
    • (2006) Nature , vol.443 , pp. 180-185
    • Dawson, R.J.1    Locher, K.P.2
  • 9
    • 84888050424 scopus 로고    scopus 로고
    • CFTR: Effect of ICL2 and ICL4 amino acids in close spatial proximity on the current properties of the channel
    • 1:CAS:528:DC%2BC3sXktlCksrk%3D 23478129
    • Billet A, Mornon JP, Jollivet M, Lehn P, Callebaut I, Becq F (2013) CFTR: effect of ICL2 and ICL4 amino acids in close spatial proximity on the current properties of the channel. J Cyst Fibros 12:737-745
    • (2013) J Cyst Fibros , vol.12 , pp. 737-745
    • Billet, A.1    Mornon, J.P.2    Jollivet, M.3    Lehn, P.4    Callebaut, I.5    Becq, F.6
  • 10
    • 70349847830 scopus 로고    scopus 로고
    • Molecular models of the open and closed states of the whole human CFTR protein
    • 1:CAS:528:DC%2BD1MXht1Cmtr%2FN 19707853
    • Mornon JP, Lehn P, Callebaut I (2009) Molecular models of the open and closed states of the whole human CFTR protein. Cell Mol Life Sci 66:3469-3486
    • (2009) Cell Mol Life Sci , vol.66 , pp. 3469-3486
    • Mornon, J.P.1    Lehn, P.2    Callebaut, I.3
  • 11
    • 37649004412 scopus 로고    scopus 로고
    • Flexibility in the ABC transporter MsbA: Alternating access with a twist
    • 1:CAS:528:DC%2BD2sXhsVSru7bO
    • Ward A, Reyes CL, Yu J, Roth CB, Chang G (2007) Flexibility in the ABC transporter MsbA: alternating access with a twist. Proc Natl Aca Sci USA 104:19005-19010
    • (2007) Proc Natl Aca Sci USA , vol.104 , pp. 19005-19010
    • Ward, A.1    Reyes, C.L.2    Yu, J.3    Roth, C.B.4    Chang, G.5
  • 12
    • 57049124822 scopus 로고    scopus 로고
    • Structural insights into ABC transporter mechanism
    • 2643341 1:CAS:528:DC%2BD1cXhsVOisr%2FO 18948194
    • Oldham ML, Davidson AL, Chen J (2008) Structural insights into ABC transporter mechanism. Curr Opin Struct Biol 18:726-733
    • (2008) Curr Opin Struct Biol , vol.18 , pp. 726-733
    • Oldham, M.L.1    Davidson, A.L.2    Chen, J.3
  • 13
    • 84856629737 scopus 로고    scopus 로고
    • CFTR: Folding, misfolding and correcting the Δf508 conformational defect
    • 3643519 1:CAS:528:DC%2BC38Xit1aqsbk%3D 22138491
    • Lukacs GL, Verkman AS (2012) CFTR: folding, misfolding and correcting the ΔF508 conformational defect. Trends Mol Med. 18:81-91
    • (2012) Trends Mol Med , vol.18 , pp. 81-91
    • Lukacs, G.L.1    Verkman, A.S.2
  • 14
    • 65249147217 scopus 로고    scopus 로고
    • Cooperative assembly and misfolding of CFTR domains in vivo
    • 2663924 1:CAS:528:DC%2BD1MXotVyqs70%3D 19176754
    • Du K, Lukacs GL (2009) Cooperative assembly and misfolding of CFTR domains in vivo. Mol Biol Cell 20:1903-1915
    • (2009) Mol Biol Cell , vol.20 , pp. 1903-1915
    • Du, K.1    Lukacs, G.L.2
  • 15
    • 11444266284 scopus 로고    scopus 로고
    • The DeltaF508 cystic fibrosis mutation impairs domain-domain interactions and arrests post-translational folding of CFTR
    • 1:CAS:528:DC%2BD2MXhtVWlsbw%3D 15619635
    • Du K, Sharma M, Lukacs GL (2005) The DeltaF508 cystic fibrosis mutation impairs domain-domain interactions and arrests post-translational folding of CFTR. Nat Struct Mol Biol 12:17-25
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 17-25
    • Du, K.1    Sharma, M.2    Lukacs, G.L.3
  • 16
    • 77957302946 scopus 로고    scopus 로고
    • Thermal unfolding studies show the disease causing F508del mutation in CFTR thermodynamically destabilizes nucleotide-binding domain 1
    • 2998726 1:CAS:528:DC%2BC3cXhsFCntb3E 20687133
    • Protasevich I, Yang Z, Wang C, Atwell S, Zhao X, Emtage S et al (2010) Thermal unfolding studies show the disease causing F508del mutation in CFTR thermodynamically destabilizes nucleotide-binding domain 1. Protein Sci 19:1917-1931
    • (2010) Protein Sci , vol.19 , pp. 1917-1931
    • Protasevich, I.1    Yang, Z.2    Wang, C.3    Atwell, S.4    Zhao, X.5    Emtage, S.6
  • 17
    • 77957309337 scopus 로고    scopus 로고
    • Integrated biophysical studies implicate partial unfolding of NBD1 of CFTR in the molecular pathogenesis of F508del cystic fibrosis
    • 2998727 1:CAS:528:DC%2BC3cXhsFCntb3F 20687163
    • Wang C, Protasevich I, Yang Z, Seehausen D, Skalak T, Zhao X et al (2010) Integrated biophysical studies implicate partial unfolding of NBD1 of CFTR in the molecular pathogenesis of F508del cystic fibrosis. Protein Sci 19:1932-1947
    • (2010) Protein Sci , vol.19 , pp. 1932-1947
    • Wang, C.1    Protasevich, I.2    Yang, Z.3    Seehausen, D.4    Skalak, T.5    Zhao, X.6
  • 18
    • 84862909346 scopus 로고    scopus 로고
    • Requirements for efficient correction of Δf508 CFTR revealed by analyses of evolved sequences
    • 3266553 1:CAS:528:DC%2BC38XhtFKgsL8%3D 22265409
    • Mendoza JL, Schmidt A, Li Q, Nuvaga E, Barrett T, Bridges RJ et al (2012) Requirements for efficient correction of ΔF508 CFTR revealed by analyses of evolved sequences. Cell 148:164-174
    • (2012) Cell , vol.148 , pp. 164-174
    • Mendoza, J.L.1    Schmidt, A.2    Li, Q.3    Nuvaga, E.4    Barrett, T.5    Bridges, R.J.6
  • 19
    • 84862908028 scopus 로고    scopus 로고
    • Correction of both NBD1 energetics and domain interface is required to restore Δf508 CFTR folding and function
    • 3431169 1:CAS:528:DC%2BC38XhtFKgsL4%3D 22265408
    • Rabeh WM, Bossard F, Xu H, Okiyoneda T, Bagdany M, Mulvihill CM et al (2012) Correction of both NBD1 energetics and domain interface is required to restore ΔF508 CFTR folding and function. Cell 148:150-163
    • (2012) Cell , vol.148 , pp. 150-163
    • Rabeh, W.M.1    Bossard, F.2    Xu, H.3    Okiyoneda, T.4    Bagdany, M.5    Mulvihill, C.M.6
  • 20
    • 70350236733 scopus 로고    scopus 로고
    • Cystic fibrosis transmembrane conductance regulator: Using differential reactivity toward channel-permeant and channel-impermeant thiol-reactive probes to test a molecular model for the pore
    • 2765204 1:CAS:528:DC%2BD1MXhtFynsb%2FL 19754156
    • Alexander C, Ivetac A, Liu X, Norimatsu Y, Serrano JR, Landstrom A et al (2009) Cystic fibrosis transmembrane conductance regulator: using differential reactivity toward channel-permeant and channel-impermeant thiol-reactive probes to test a molecular model for the pore. Biochemistry 48:10078-10088
    • (2009) Biochemistry , vol.48 , pp. 10078-10088
    • Alexander, C.1    Ivetac, A.2    Liu, X.3    Norimatsu, Y.4    Serrano, J.R.5    Landstrom, A.6
  • 21
    • 84858633600 scopus 로고    scopus 로고
    • Cystic fibrosis transmembrane conductance regulator: A molecular model defines the architecture of the anion conduction path and locates a "bottleneck" in the pore
    • 3316148 1:CAS:528:DC%2BC38XisFalsb4%3D 22352759
    • Norimatsu Y, Ivetac A, Alexander C, Kirkham J, O'Donnell N, Dawson DC et al (2012) Cystic fibrosis transmembrane conductance regulator: a molecular model defines the architecture of the anion conduction path and locates a "bottleneck" in the pore. Biochemistry 51:2199-2212
    • (2012) Biochemistry , vol.51 , pp. 2199-2212
    • Norimatsu, Y.1    Ivetac, A.2    Alexander, C.3    Kirkham, J.4    O'Donnell, N.5    Dawson, D.C.6
  • 22
    • 84864258150 scopus 로고    scopus 로고
    • New model of cystic fibrosis transmembrane conductance regulator proposes active channel-like conformation
    • 1:CAS:528:DC%2BC38Xptlyltb8%3D 22747419
    • Dalton J, Kalid O, Schushan M, Ben-Ta lN, Villà-Freixa J (2012) New model of cystic fibrosis transmembrane conductance regulator proposes active channel-like conformation. J Chem Inf Model 52:1842-1853
    • (2012) J Chem Inf Model , vol.52 , pp. 1842-1853
    • Dalton, J.1    Kalid, O.2    Schushan, M.3    Ben-Ta, L.4    Villà-Freixa, J.5
  • 23
    • 84872304431 scopus 로고    scopus 로고
    • The power stroke driven by ATP binding in CFTR as studied by molecular dynamics simulations
    • 1:CAS:528:DC%2BC38XhslylurnI 23214920
    • Furukawa-Hagiya T, Furuta T, Chiba S, Sohma Y, Sakurai M (2013) The power stroke driven by ATP binding in CFTR as studied by molecular dynamics simulations. J Phys Chem B 117:83-93
    • (2013) J Phys Chem B , vol.117 , pp. 83-93
    • Furukawa-Hagiya, T.1    Furuta, T.2    Chiba, S.3    Sohma, Y.4    Sakurai, M.5
  • 24
    • 63449139456 scopus 로고    scopus 로고
    • Structure of P-glycoprotein reveals a molecular basis for poly-specific drug binding
    • 2720052 1:CAS:528:DC%2BD1MXjs1Kgtro%3D 19325113
    • Aller SG, Yu J, Ward A, Weng Y, Chittaboina S, Zhuo R et al (2009) Structure of P-glycoprotein reveals a molecular basis for poly-specific drug binding. Science 323:1718-1722
    • (2009) Science , vol.323 , pp. 1718-1722
    • Aller, S.G.1    Yu, J.2    Ward, A.3    Weng, Y.4    Chittaboina, S.5    Zhuo, R.6
  • 25
    • 84884699027 scopus 로고    scopus 로고
    • Modeling the conformational changes underlying channel opening in CFTR
    • 3785483 1:CAS:528:DC%2BC3sXhsFOntLfI 24086355
    • Rahman K, Cui G, Harvey S, McCarty N (2013) Modeling the conformational changes underlying channel opening in CFTR. PLoS ONE 8:e74574
    • (2013) PLoS ONE , vol.8
    • Rahman, K.1    Cui, G.2    Harvey, S.3    McCarty, N.4
  • 26
    • 84882338908 scopus 로고    scopus 로고
    • Structures of P-glycoprotein reveal its conformational flexibility and an epitope on the nucleotide-binding domain
    • 3746859 1:CAS:528:DC%2BC3sXhtlCrtbzE 23901103
    • Ward AB, Szewczyk P, Grimard V, Lee CW, Martinez L, Doshi R et al (2013) Structures of P-glycoprotein reveal its conformational flexibility and an epitope on the nucleotide-binding domain. Proc Natl Acad Sci USA 110:13386-13391
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. 13386-13391
    • Ward, A.B.1    Szewczyk, P.2    Grimard, V.3    Lee, C.W.4    Martinez, L.5    Doshi, R.6
  • 27
    • 84867883248 scopus 로고    scopus 로고
    • Crystal structure of the multidrug transporter P-glycoprotein from Caenorhabditis elegans
    • 3482266 1:CAS:528:DC%2BC38Xhtlymu7%2FN 23000902
    • Jin MS, Oldham ML, Zhang Q, Chen J (2012) Crystal structure of the multidrug transporter P-glycoprotein from Caenorhabditis elegans. Nature 490:566-569
    • (2012) Nature , vol.490 , pp. 566-569
    • Jin, M.S.1    Oldham, M.L.2    Zhang, Q.3    Chen, J.4
  • 28
    • 84896512558 scopus 로고    scopus 로고
    • Structural basis for gating mechanisms of a eukaryotic P-glycoprotein homolog
    • 3964115 1:CAS:528:DC%2BC2cXjtl2msbs%3D 24591620
    • Kodan A, Yamaguchi T, Nakatsu T, Sakiyama K, Hipolito C, Fujioka A et al (2014) Structural basis for gating mechanisms of a eukaryotic P-glycoprotein homolog. Proc Natl Acad Sci USA 111:4049-4054
    • (2014) Proc Natl Acad Sci USA , vol.111 , pp. 4049-4054
    • Kodan, A.1    Yamaguchi, T.2    Nakatsu, T.3    Sakiyama, K.4    Hipolito, C.5    Fujioka, A.6
  • 29
    • 84879002569 scopus 로고    scopus 로고
    • Structures of ABCB10, a human ATP-binding cassette transporter in apo- and nucleotide-bound states
    • 3683770 1:CAS:528:DC%2BC3sXhtFOrt7bL 23716676
    • Shintre CA, Pike AC, Li Q, Kim JI, Barr AJ, Goubin S et al (2013) Structures of ABCB10, a human ATP-binding cassette transporter in apo- and nucleotide-bound states. Proc Natl Acad Sci USA 110:9710-9715
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. 9710-9715
    • Shintre, C.A.1    Pike, A.C.2    Li, Q.3    Kim, J.I.4    Barr, A.J.5    Goubin, S.6
  • 30
    • 84896800834 scopus 로고    scopus 로고
    • Crystal structures of nucleotide-free and glutathione-bound mitochondrial ABC transporter Atm1
    • 1:CAS:528:DC%2BC2cXjsVegs7s%3D 24604199
    • Srinivasan V, Pierik AJ, Lill R (2014) Crystal structures of nucleotide-free and glutathione-bound mitochondrial ABC transporter Atm1. Science 343:1137-1140
    • (2014) Science , vol.343 , pp. 1137-1140
    • Srinivasan, V.1    Pierik, A.J.2    Lill, R.3
  • 31
    • 84896803955 scopus 로고    scopus 로고
    • Structural basis for heavy metal detoxification by an Atm1-type ABC exporter
    • 4151877 1:CAS:528:DC%2BC2cXjsVegs7o%3D 24604198
    • Lee JY, Yang JG, Zhitnitsky D, Lewinson O, Rees DC (2014) Structural basis for heavy metal detoxification by an Atm1-type ABC exporter. Science 343:1133-1136
    • (2014) Science , vol.343 , pp. 1133-1136
    • Lee, J.Y.1    Yang, J.G.2    Zhitnitsky, D.3    Lewinson, O.4    Rees, D.C.5
  • 32
    • 84861310612 scopus 로고    scopus 로고
    • Crystal structure of a heterodimeric ABC transporter in its inward-facing conformation
    • 1:CAS:528:DC%2BC38XksVegtLs%3D 22447242
    • Hohl M, Briand C, Grütter MG, Seeger MA (2012) Crystal structure of a heterodimeric ABC transporter in its inward-facing conformation. Nat Struct Mol Biol 19:395-402
    • (2012) Nat Struct Mol Biol , vol.19 , pp. 395-402
    • Hohl, M.1    Briand, C.2    Grütter, M.G.3    Seeger, M.A.4
  • 33
    • 0141513675 scopus 로고    scopus 로고
    • Prolonged nonhydrolytic interaction of nucleotide with CFTR's NH2-terminal nucleotide binding domain and its role in channel gating
    • 2234483 1:CAS:528:DC%2BD3sXnsleht78%3D 12939393
    • Basso C, Vergani P, Nairn AC, Gadsby DC (2003) Prolonged nonhydrolytic interaction of nucleotide with CFTR's NH2-terminal nucleotide binding domain and its role in channel gating. J Gen Physiol 122:333-348
    • (2003) J Gen Physiol , vol.122 , pp. 333-348
    • Basso, C.1    Vergani, P.2    Nairn, A.C.3    Gadsby, D.C.4
  • 34
    • 79958076650 scopus 로고    scopus 로고
    • Mutant cycles at CFTR's non-canonical ATP-binding site support little interface separation during gating
    • 3105517 1:CAS:528:DC%2BC3MXos1KmtrY%3D 21576373
    • Szollosi A, Muallem DR, Csanády L, Vergani P (2011) Mutant cycles at CFTR's non-canonical ATP-binding site support little interface separation during gating. J Gen Physiol 137:549-562
    • (2011) J Gen Physiol , vol.137 , pp. 549-562
    • Szollosi, A.1    Muallem, D.R.2    Csanády, L.3    Vergani, P.4
  • 35
    • 84903478669 scopus 로고    scopus 로고
    • Structure of an antibacterial peptide ATP-binding cassette transporter in a novel outward occluded state
    • 4078857 1:CAS:528:DC%2BC2cXpsFCjtr0%3D 24920594
    • Choudhury HG, Tong Z, Mathavan I, Li Y, Iwata S, Zirah S et al (2014) Structure of an antibacterial peptide ATP-binding cassette transporter in a novel outward occluded state. Proc Natl Acad Sci USA 111:9145-9150
    • (2014) Proc Natl Acad Sci USA , vol.111 , pp. 9145-9150
    • Choudhury, H.G.1    Tong, Z.2    Mathavan, I.3    Li, Y.4    Iwata, S.5    Zirah, S.6
  • 36
    • 0030690133 scopus 로고    scopus 로고
    • Deciphering protein sequence information through hydrophobic cluster analysis (HCA): Current status and perspectives
    • 1:CAS:528:DyaK2sXms1Clurs%3D 9351466
    • Callebaut I, Labesse G, Durand P, Poupon A, Canard L, Chomilier J et al (1997) Deciphering protein sequence information through hydrophobic cluster analysis (HCA): current status and perspectives. Cell Mol Life Sci 53:621-645
    • (1997) Cell Mol Life Sci , vol.53 , pp. 621-645
    • Callebaut, I.1    Labesse, G.2    Durand, P.3    Poupon, A.4    Canard, L.5    Chomilier, J.6
  • 37
    • 0023657949 scopus 로고
    • Hydrophobic cluster analysis: An efficient new way to compare and analyse amino acid sequences
    • 1:CAS:528:DyaL1cXjsVCntg%3D%3D 3678489
    • Gaboriaud C, Bissery V, Benchetrit T, Mornon JP (1987) Hydrophobic cluster analysis: an efficient new way to compare and analyse amino acid sequences. FEBS Lett 224:149-155
    • (1987) FEBS Lett , vol.224 , pp. 149-155
    • Gaboriaud, C.1    Bissery, V.2    Benchetrit, T.3    Mornon, J.P.4
  • 38
    • 0842330688 scopus 로고    scopus 로고
    • Nucleotide-binding domains of human cystic fibrosis transmembrane conductance regulator: Detailed sequence analysis and three-dimensional modeling of the heterodimer
    • 1:CAS:528:DC%2BD2cXjt1yhtLo%3D 14745501
    • Callebaut I, Eudes R, Mornon JP, Lehn P (2004) Nucleotide-binding domains of human cystic fibrosis transmembrane conductance regulator: detailed sequence analysis and three-dimensional modeling of the heterodimer. Cell Mol Life Sci 61:230-242
    • (2004) Cell Mol Life Sci , vol.61 , pp. 230-242
    • Callebaut, I.1    Eudes, R.2    Mornon, J.P.3    Lehn, P.4
  • 39
    • 10744230777 scopus 로고    scopus 로고
    • Structure of nucleotide-binding domain 1 of the cystic fibrosis transmembrane conductance regulator
    • 1271750 1:CAS:528:DC%2BD2cXhtVeqs7c%3D 14685259
    • Lewis HA, Buchanan SG, Burley SK, Conners K, Dickey M, Dorwart M et al (2004) Structure of nucleotide-binding domain 1 of the cystic fibrosis transmembrane conductance regulator. EMBO J 23:282-293
    • (2004) EMBO J , vol.23 , pp. 282-293
    • Lewis, H.A.1    Buchanan, S.G.2    Burley, S.K.3    Conners, K.4    Dickey, M.5    Dorwart, M.6
  • 41
    • 0000243829 scopus 로고
    • PROCHECK - A program to check the stereochemical quality of protein structures
    • 1:CAS:528:DyaK3sXit12lurY%3D
    • Laskowski R, MacArthur M, Moss D, Thornton J (1993) PROCHECK - a program to check the stereochemical quality of protein structures. J App Cryst 26:283-291
    • (1993) J App Cryst , vol.26 , pp. 283-291
    • Laskowski, R.1    MacArthur, M.2    Moss, D.3    Thornton, J.4
  • 42
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • 1:CAS:528:DyaK1cXhvFaks70%3D 9504803
    • Guex N, Peitsch MC (1997) SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 18:2714-2723
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 43
    • 4444221565 scopus 로고    scopus 로고
    • UCSF chimera - A visualization system for exploratory research and analysis
    • 1:CAS:528:DC%2BD2cXmvVOhsbs%3D 15264254
    • Pettersen E, Goddard T, Huang C, Couch G, Greenblatt D, Meng E et al (2004) UCSF chimera - a visualization system for exploratory research and analysis. J Comput Chem 25:1605-1612
    • (2004) J Comput Chem , vol.25 , pp. 1605-1612
    • Pettersen, E.1    Goddard, T.2    Huang, C.3    Couch, G.4    Greenblatt, D.5    Meng, E.6
  • 44
    • 0029878720 scopus 로고    scopus 로고
    • VMD - Visual molecular dynamics
    • 1:CAS:528:DyaK28Xis12nsrg%3D 8744570
    • Humphrey W, Dalke A, Schulten K (1996) VMD - visual molecular dynamics. J Mol Graph 14:33-38
    • (1996) J Mol Graph , vol.14 , pp. 33-38
    • Humphrey, W.1    Dalke, A.2    Schulten, K.3
  • 45
    • 75249088440 scopus 로고    scopus 로고
    • Roll: A new algorithm for the detection of protein pockets and cavities with a rolling probe sphere
    • 19846440
    • Yu J, Zhou Y, Tanaka I, Yao M (2010) Roll: a new algorithm for the detection of protein pockets and cavities with a rolling probe sphere. Bioinformatics 26:46-52
    • (2010) Bioinformatics , vol.26 , pp. 46-52
    • Yu, J.1    Zhou, Y.2    Tanaka, I.3    Yao, M.4
  • 46
    • 84861060898 scopus 로고    scopus 로고
    • OPM database and PPM web server: Resources for positioning of proteins in membranes
    • 3245162 1:CAS:528:DC%2BC3MXhs12hurzJ 21890895
    • Lomize M, Pogozheva I, Joo H, Mosberg H, Lomize A (2012) OPM database and PPM web server: resources for positioning of proteins in membranes. Nucleic Acids Res 40:D370-D376
    • (2012) Nucleic Acids Res , vol.40 , pp. D370-D376
    • Lomize, M.1    Pogozheva, I.2    Joo, H.3    Mosberg, H.4    Lomize, A.5
  • 49
    • 0041784950 scopus 로고    scopus 로고
    • All-hydrogen empirical potential for molecular modeling and dynamics studies of proteins using the CHARMM22 force field
    • 1:CAS:528:DyaK1cXivVOlsb4%3D 24889800
    • MacKerell AJ, Bashford D, Bellott M, Dunbrack RJ, Evanseck J, Field M et al (1998) All-hydrogen empirical potential for molecular modeling and dynamics studies of proteins using the CHARMM22 force field. J Phys Chem B 102:3586-3613
    • (1998) J Phys Chem B , vol.102 , pp. 3586-3613
    • MacKerell, A.J.1    Bashford, D.2    Bellott, M.3    Dunbrack, R.J.4    Evanseck, J.5    Field, M.6
  • 50
    • 3142714765 scopus 로고    scopus 로고
    • Extending the treatment of backbone energetics in protein force fields: Limitations of gas-phase quantum mechanics in reproducing protein conformational distributions in molecular dynamics simulations
    • 1:CAS:528:DC%2BD2cXlsVOgt7c%3D
    • MacKerell AJ, Feig M, Brooks CI (2004) Extending the treatment of backbone energetics in protein force fields: limitations of gas-phase quantum mechanics in reproducing protein conformational distributions in molecular dynamics simulations. J Comp Chem 25:1400-1415
    • (2004) J Comp Chem , vol.25 , pp. 1400-1415
    • MacKerell, A.J.1    Feig, M.2    Brooks, C.I.3
  • 51
    • 0034250744 scopus 로고    scopus 로고
    • An improved empirical potential energy function for molecular simulations of phospholipids
    • 1:CAS:528:DC%2BD3cXkvVWgtL4%3D
    • Feller S, MacKerell AJ (2000) An improved empirical potential energy function for molecular simulations of phospholipids. J Phys Chem B. 104:7510-7515
    • (2000) J Phys Chem B , vol.104 , pp. 7510-7515
    • Feller, S.1    MacKerell, A.J.2
  • 52
    • 0004016501 scopus 로고
    • Comparison of simple potential functions for simulating liquid water
    • 1:CAS:528:DyaL3sXksF2htL4%3D
    • Jorgensen W, Chandrasekhar J, Madura J, Impey R, Klein M (1983) Comparison of simple potential functions for simulating liquid water. J Chem Phys 79:926-935
    • (1983) J Chem Phys , vol.79 , pp. 926-935
    • Jorgensen, W.1    Chandrasekhar, J.2    Madura, J.3    Impey, R.4    Klein, M.5
  • 53
    • 33646940952 scopus 로고
    • Numerical integration of the cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes
    • 1:CAS:528:DyaE2sXktVGhsL4%3D
    • Ryckaert J-P, Ciccotti G, Berendsen H (1977) Numerical integration of the cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes. J Comp Phys 23:327-341
    • (1977) J Comp Phys , vol.23 , pp. 327-341
    • Ryckaert, J.-P.1    Ciccotti, G.2    Berendsen, H.3
  • 54
    • 33846823909 scopus 로고
    • Particle mesh Ewald, an N·log(N) method for Ewald sums in large systems
    • 1:CAS:528:DyaK3sXks1Ohsr0%3D
    • Darden T, York D, Pedersen L (1993) Particle mesh Ewald, an N·log(N) method for Ewald sums in large systems. J Chem Phys 98:10089-10092
    • (1993) J Chem Phys , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 55
    • 36449007836 scopus 로고
    • Constant pressure molecular dynamics simulation: The Langevin piston method
    • 1:CAS:528:DyaK2MXotVentLo%3D
    • Feller S, Zhang Y, Pastor R, Brooks B (1995) Constant pressure molecular dynamics simulation: the Langevin piston method. J Chem Phys 103:4613-4621
    • (1995) J Chem Phys , vol.103 , pp. 4613-4621
    • Feller, S.1    Zhang, Y.2    Pastor, R.3    Brooks, B.4
  • 56
    • 84862874979 scopus 로고    scopus 로고
    • Thermal instability of Δf508 cystic fibrosis transmembrane conductance regulator (CFTR) channel function: Protection by single suppressor mutations and inhibiting channel activity
    • 3402225 1:CAS:528:DC%2BC38Xot1amtr4%3D 22680785
    • Liu X, O'Donnell N, Landstrom A, Skach WR, Dawson DC (2012) Thermal instability of ΔF508 cystic fibrosis transmembrane conductance regulator (CFTR) channel function: protection by single suppressor mutations and inhibiting channel activity. Biochemistry 51:5113-5124
    • (2012) Biochemistry , vol.51 , pp. 5113-5124
    • Liu, X.1    O'Donnell, N.2    Landstrom, A.3    Skach, W.R.4    Dawson, D.C.5
  • 57
    • 77956237499 scopus 로고    scopus 로고
    • Dual roles of the sixth transmembrane segment of the CFTR chloride channel in gating and permeation
    • 2931150 1:CAS:528:DC%2BC3cXhtF2rtrnI 20805575
    • Bai Y, Li M, Hwang T (2010) Dual roles of the sixth transmembrane segment of the CFTR chloride channel in gating and permeation. J Gen Physiol 136:293-309
    • (2010) J Gen Physiol , vol.136 , pp. 293-309
    • Bai, Y.1    Li, M.2    Hwang, T.3
  • 58
    • 0033605158 scopus 로고    scopus 로고
    • Cystic fibrosis-associated mutations at arginine 347 alter the pore architecture of CFTR. Evidence for disruption of a salt bridge
    • 1:CAS:528:DyaK1MXhsFalsb0%3D 10026154
    • Cotten JF, Welsh MJ (1999) Cystic fibrosis-associated mutations at arginine 347 alter the pore architecture of 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
  • 59
    • 0028264188 scopus 로고
    • Amino acid residues lining the chloride channel of the cystic fibrosis transmembrane conductance regulator
    • 1:CAS:528:DyaK2cXkt12mtrs%3D 7515047
    • Akabas MH, Kaufmann C, Cook TA, Archdeacon P (1994) Amino acid residues lining the chloride channel of the cystic fibrosis transmembrane conductance regulator. J Biol Chem 269:14865-14868
    • (1994) J Biol Chem , vol.269 , pp. 14865-14868
    • Akabas, M.H.1    Kaufmann, C.2    Cook, T.A.3    Archdeacon, P.4
  • 60
    • 67349171421 scopus 로고    scopus 로고
    • Novel residues lining the CFTR chloride channel pore identified by functional modification of introduced cysteines
    • 1:CAS:528:DC%2BD1MXlslGgtbw%3D 19381710
    • Fatehi M, Linsdell P (2009) Novel residues lining the CFTR chloride channel pore identified by functional modification of introduced cysteines. J Membr Biol 228:151-164
    • (2009) J Membr Biol , vol.228 , pp. 151-164
    • Fatehi, M.1    Linsdell, P.2
  • 61
    • 84874150515 scopus 로고    scopus 로고
    • Cysteine scanning of CFTR's first transmembrane segment reveals its plausible roles in gating and permeation
    • 3576531 1:CAS:528:DC%2BC3sXivFOqtLg%3D 23442957
    • Gao X, Bai Y, Hwang TC (2013) Cysteine scanning of CFTR's first transmembrane segment reveals its plausible roles in gating and permeation. Biophys J 104:786-797
    • (2013) Biophys J , vol.104 , pp. 786-797
    • Gao, X.1    Bai, Y.2    Hwang, T.C.3
  • 62
    • 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
    • 1:CAS:528:DC%2BD2cXhtFeis73I 15504721
    • Ge N, Muise CN, 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.N.2    Gong, X.3    Linsdell, P.4
  • 63
    • 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
    • 1:CAS:528:DC%2BD2MXitVCitrs%3D 15634668
    • 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
  • 64
    • 79961146667 scopus 로고    scopus 로고
    • Alignment of transmembrane regions in the cystic fibrosis transmembrane conductance regulator chloride channel pore
    • 3149817 1:CAS:528:DC%2BC3MXhtV2qtrnL 21746847
    • Wang W, El Hiani Y, Linsdell P (2011) Alignment of transmembrane regions in the cystic fibrosis transmembrane conductance regulator chloride channel pore. J Gen Physiol 138:165-178
    • (2011) J Gen Physiol , vol.138 , pp. 165-178
    • Wang, W.1    El Hiani, Y.2    Linsdell, P.3
  • 65
    • 84896690825 scopus 로고    scopus 로고
    • Relative contribution of different transmembrane segments to the CFTR chloride channel pore
    • 1:CAS:528:DC%2BC3sXht12isr%2FE 23955087
    • Wang W, El Hiani Y, Rubaiy HN, Linsdell P (2014) Relative contribution of different transmembrane segments to the CFTR chloride channel pore. Pflugers Arch 466:477-490
    • (2014) Pflugers Arch , vol.466 , pp. 477-490
    • Wang, W.1    El Hiani, Y.2    Rubaiy, H.N.3    Linsdell, P.4
  • 66
    • 80054724207 scopus 로고    scopus 로고
    • Functional arrangement of the 12th transmembrane region in the CFTR chloride channel pore based on functional investigation of a cysteine-less CFTR variant
    • Quian F, El Hiani Y, Linsdell P (2011) Functional arrangement of the 12th transmembrane region in the CFTR chloride channel pore based on functional investigation of a cysteine-less CFTR variant. Eur J Physiol. 462:559-571
    • (2011) Eur J Physiol , vol.462 , pp. 559-571
    • Quian, F.1    El Hiani, Y.2    Linsdell, P.3
  • 67
    • 80555127440 scopus 로고    scopus 로고
    • Structural basis for the channel function of a degraded ABC transporter, CFTR (ABCC7)
    • 3206304 1:CAS:528:DC%2BC3MXhsFCrsLvE 22042986
    • Bai Y, Li M, Hwang T (2011) Structural basis for the channel function of a degraded ABC transporter, CFTR (ABCC7). J Gen Physiol 138:495-507
    • (2011) J Gen Physiol , vol.138 , pp. 495-507
    • Bai, Y.1    Li, M.2    Hwang, T.3
  • 68
    • 0032190615 scopus 로고    scopus 로고
    • Non-pore lining amino acid side chains influence anion selectivity of the human CFTR Cl-channel expressed in mammalian cell lines
    • 2231193 1:CAS:528:DyaK1cXnt1Ortb8%3D 9729613
    • Linsdell P, Zheng SX, Hanrahan JW (1998) Non-pore lining amino acid side chains influence anion selectivity of the human CFTR Cl-channel expressed in mammalian cell lines. J Physiol 512:1-16
    • (1998) J Physiol , vol.512 , pp. 1-16
    • Linsdell, P.1    Zheng, S.X.2    Hanrahan, J.W.3
  • 69
    • 84862614574 scopus 로고    scopus 로고
    • Differential contribution of TM6 and TM12 to the pore of CFTR identified by three sulfonylurea-based blockers
    • 1:CAS:528:DC%2BC38XitVGgs74%3D 22160394
    • Cui G, Song B, Turki HW, McCarty NA (2012) Differential contribution of TM6 and TM12 to the pore of CFTR identified by three sulfonylurea-based blockers. Pflugers Arch 463:405-418
    • (2012) Pflugers Arch , vol.463 , pp. 405-418
    • Cui, G.1    Song, B.2    Turki, H.W.3    McCarty, N.A.4
  • 70
    • 84907902317 scopus 로고    scopus 로고
    • Cystic fibrosis transmembrane conductance regulator chloride channel blockers: Pharmacological, biophysical and physiological relevance
    • 3942540 24600512
    • Linsdell P (2014) Cystic fibrosis transmembrane conductance regulator chloride channel blockers: pharmacological, biophysical and physiological relevance. World J Biol Chem 5:26-39
    • (2014) World J Biol Chem , vol.5 , pp. 26-39
    • Linsdell, P.1
  • 71
    • 77649161249 scopus 로고    scopus 로고
    • Regulation of conductance by the number of fixed positive charges in the intracellular vestibule of the CFTR chloride channel pore
    • 2828907 1:CAS:528:DC%2BC3cXjvF2jsLw%3D 20142516
    • Zhou JJ, Li MS, Qi J, Linsdell P (2010) Regulation of conductance by the number of fixed positive charges in the intracellular vestibule of the CFTR chloride channel pore. J Gen Physiol 135:229-245
    • (2010) J Gen Physiol , vol.135 , pp. 229-245
    • Zhou, J.J.1    Li, M.S.2    Qi, J.3    Linsdell, P.4
  • 72
    • 84867631978 scopus 로고    scopus 로고
    • Tuning of CFTR chloride channel function by location of positive charges within the pore
    • 3475386 23083715
    • El Hiani Y, Linsdell P (2012) Tuning of CFTR chloride channel function by location of positive charges within the pore. Biophys J 103:1719-1726
    • (2012) Biophys J , vol.103 , pp. 1719-1726
    • El Hiani, Y.1    Linsdell, P.2
  • 73
    • 0037266979 scopus 로고    scopus 로고
    • Extent of the selectivity filter conferred by the sixth transmembrane region in the CFTR chloride channel pore
    • 1:CAS:528:DC%2BD3sXkslahurg%3D 12745925
    • Gupta J, Lindsell P (2003) Extent of the selectivity filter conferred by the sixth transmembrane region in the CFTR chloride channel pore. Mol Membr Biol 20:45-52
    • (2003) Mol Membr Biol , vol.20 , pp. 45-52
    • Gupta, J.1    Lindsell, P.2
  • 74
    • 34247493249 scopus 로고    scopus 로고
    • Identification of a second blocker binding site at the cytoplasmic mouth of the cystic fibrosis transmembrane conductance regulator chloride channel pore
    • 1:CAS:528:DC%2BD2sXlslSis78%3D 17293558
    • St Aubin CN, Zhou JJ, Linsdell P (2007) Identification of a second blocker binding site at the cytoplasmic mouth of the cystic fibrosis transmembrane conductance regulator chloride channel pore. Mol Pharmacol 71:1360-1368
    • (2007) Mol Pharmacol , vol.71 , pp. 1360-1368
    • St Aubin, C.N.1    Zhou, J.J.2    Linsdell, P.3
  • 75
    • 35148857724 scopus 로고    scopus 로고
    • CFTR inhibition by glibenclamide requires a positive charge in cytoplasmic loop three
    • 1:CAS:528:DC%2BD2sXhtFGrsr3J 17582383
    • Melin P, Hosy E, Vivaudou M, Becq F (2007) CFTR inhibition by glibenclamide requires a positive charge in cytoplasmic loop three. Biochim Biophys Acta 1768:2438-2446
    • (2007) Biochim Biophys Acta , vol.1768 , pp. 2438-2446
    • Melin, P.1    Hosy, E.2    Vivaudou, M.3    Becq, F.4
  • 76
    • 33645533055 scopus 로고    scopus 로고
    • The role of cystic fibrosis transmembrane conductance regulator phenylalanine 508 side chain in ion channel gating
    • 1779664 1:CAS:528:DC%2BD28XksV2jtr8%3D 16484308
    • Cui L, Aleksandrov L, Hou YX, Gentzsch M, Chen JH, Riordan JR et al (2006) The role of cystic fibrosis transmembrane conductance regulator phenylalanine 508 side chain in ion channel gating. J Physiol 572:347-358
    • (2006) J Physiol , vol.572 , pp. 347-358
    • Cui, L.1    Aleksandrov, L.2    Hou, Y.X.3    Gentzsch, M.4    Chen, J.H.5    Riordan, J.R.6
  • 77
    • 84860271643 scopus 로고    scopus 로고
    • Allosteric modulation balances thermodynamic stability and restores function of Δf508 CFTR
    • 3891843 1:CAS:528:DC%2BC38XkvFWisL4%3D 22406676
    • Aleksandrov A, Kota P, Cui L, Jensen T, Alekseev A, Reyes S et al (2012) Allosteric modulation balances thermodynamic stability and restores function of ΔF508 CFTR. J Mol Biol 419:41-60
    • (2012) J Mol Biol , vol.419 , pp. 41-60
    • Aleksandrov, A.1    Kota, P.2    Cui, L.3    Jensen, T.4    Alekseev, A.5    Reyes, S.6
  • 78
    • 33846630895 scopus 로고    scopus 로고
    • A generalized analysis of hydrophobic and loop clusters within globular protein sequences
    • 1774571 17210072
    • Eudes R, Le Tuan K, Delettré J, Mornon JP, Callebaut I (2007) A generalized analysis of hydrophobic and loop clusters within globular protein sequences. BMC Struct Biol 7:2
    • (2007) BMC Struct Biol , vol.7 , pp. 2
    • Eudes, R.1    Le Tuan, K.2    Delettré, J.3    Mornon, J.P.4    Callebaut, I.5
  • 79
    • 84885022205 scopus 로고    scopus 로고
    • Defining the disease liability of variants in the cystic fibrosis transmembrane conductance regulator gene
    • 1:CAS:528:DC%2BC3sXhtlWku7fK 23974870
    • Sosnay P, Siklosi K, Van Goor F, Kaniecki K, Yu H, Sharma N et al (2013) Defining the disease liability of variants in the cystic fibrosis transmembrane conductance regulator gene. Nat Genet 45:1160-1167
    • (2013) Nat Genet , vol.45 , pp. 1160-1167
    • Sosnay, P.1    Siklosi, K.2    Van Goor, F.3    Kaniecki, K.4    Yu, H.5    Sharma, N.6
  • 80
    • 0035865354 scopus 로고    scopus 로고
    • Relationship between anion binding and anion permeability revealed by mutagenesis within the cystic fibrosis transmembrane conductance regulator chloride channel pore
    • 2278455 1:CAS:528:DC%2BD3MXitlSlt70%3D 11179391
    • Linsdell P (2001) Relationship between anion binding and anion permeability revealed by mutagenesis within the cystic fibrosis transmembrane conductance regulator chloride channel pore. J Physiol 531:51-66
    • (2001) J Physiol , vol.531 , pp. 51-66
    • Linsdell, P.1
  • 81
    • 0034084793 scopus 로고    scopus 로고
    • Molecular determinants of anion selectivity in the cystic fibrosis transmembrane conductance regulator chloride channel pore
    • 1300881 1:CAS:528:DC%2BD3cXjvFOhu7k%3D 10827976
    • 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
  • 82
    • 84864564117 scopus 로고    scopus 로고
    • Perspectives on the structure-function of ABC transporters: The switch and constant contact models
    • 1:CAS:528:DC%2BC38XhtFKnsrbP 22765920
    • George A, Jones P (2012) Perspectives on the structure-function of ABC transporters: the switch and constant contact models. Prog Biophys Mol Biol 109:95-107
    • (2012) Prog Biophys Mol Biol , vol.109 , pp. 95-107
    • George, A.1    Jones, P.2
  • 83
    • 67349185408 scopus 로고    scopus 로고
    • Ion channels versus ion pumps: The principal difference, in principle
    • 2742554 1:CAS:528:DC%2BD1MXjvV2ksrk%3D 19339978
    • Gadsby DC (2009) Ion channels versus ion pumps: the principal difference, in principle. Nat Rev Mol Cell Biol 10:344-352
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 344-352
    • Gadsby, D.C.1
  • 84
    • 42049096734 scopus 로고    scopus 로고
    • CLC-0 and CFTR: Chloride channels evolved from transporters
    • 1:CAS:528:DC%2BD1cXls1Khs7o%3D 18391167
    • Chen T, Hwang T (2008) CLC-0 and CFTR: chloride channels evolved from transporters. Physiol Rev 88:351-387
    • (2008) Physiol Rev , vol.88 , pp. 351-387
    • Chen, T.1    Hwang, T.2
  • 85
    • 75749112587 scopus 로고    scopus 로고
    • CFTR: Break a pump, make a channel
    • 2824264 1:CAS:528:DC%2BC3cXht1aqsLg%3D 20080601
    • Miller C (2010) CFTR: break a pump, make a channel. Proc Natl Acad Sci USA 107:959-960
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 959-960
    • Miller, C.1
  • 86
    • 0038374988 scopus 로고    scopus 로고
    • Crystal structures of the ATPase subunit of the glucose ABC transporter from Sulfolobus solfataricus: Nucleotide-free and nucleotide-bound conformations
    • 1:CAS:528:DC%2BD3sXkvVaqur0%3D 12823973
    • Verdon G, Albers SV, Dijkstra BW, Driessen AJ, Thunnissen AM (2003) Crystal structures of the ATPase subunit of the glucose ABC transporter from Sulfolobus solfataricus: nucleotide-free and nucleotide-bound conformations. J Mol Biol 330:343-358
    • (2003) J Mol Biol , vol.330 , pp. 343-358
    • Verdon, G.1    Albers, S.V.2    Dijkstra, B.W.3    Driessen, A.J.4    Thunnissen, A.M.5
  • 87
    • 84905040016 scopus 로고    scopus 로고
    • Structural basis for allosteric cross-talk between the asymmetric nucleotide binding sites of a heterodimeric ABC exporter
    • 4121816 1:CAS:528:DC%2BC2cXhtFyqtLnJ 25030449
    • Hohl M, Hürlimann LM, Böhm S, Schöppe J, Grütter MG, Bordignon E et al (2014) Structural basis for allosteric cross-talk between the asymmetric nucleotide binding sites of a heterodimeric ABC exporter. Proc Natl Acad Sci USA 111:11025-11030
    • (2014) Proc Natl Acad Sci USA , vol.111 , pp. 11025-11030
    • Hohl, M.1    Hürlimann, L.M.2    Böhm, S.3    Schöppe, J.4    Grütter, M.G.5    Bordignon, E.6
  • 88
    • 82755176172 scopus 로고    scopus 로고
    • The cystic fibrosis transmembrane conductance regulator (CFTR): Three-dimensional structure and localization of a channel gate
    • 3234965 1:CAS:528:DC%2BC3MXhsFKjs7%2FO 21931164
    • Rosenberg MF, O'Ryan LP, Hughes G, Zhao Z, Aleksandrov LA, Riordan JR et al (2011) The cystic fibrosis transmembrane conductance regulator (CFTR): three-dimensional structure and localization of a channel gate. J Biol Chem 286:42647-42654
    • (2011) J Biol Chem , vol.286 , pp. 42647-42654
    • Rosenberg, M.F.1    O'Ryan, L.P.2    Hughes, G.3    Zhao, Z.4    Aleksandrov, L.A.5    Riordan, J.R.6
  • 89
    • 84861116440 scopus 로고    scopus 로고
    • Role of the juxtamembrane region of cytoplasmic loop 3 in the gating and conductance of the cystic fibrosis transmembrane conductance regulator chloride channel
    • 3381012 22545782
    • El Hiani Y, Linsdell P (2012) Role of the juxtamembrane region of cytoplasmic loop 3 in the gating and conductance of the cystic fibrosis transmembrane conductance regulator chloride channel. Biochemistry 51:3971-3981
    • (2012) Biochemistry , vol.51 , pp. 3971-3981
    • El Hiani, Y.1    Linsdell, P.2
  • 90
    • 33748310520 scopus 로고    scopus 로고
    • Structural asymmetry of AcrB trimer suggests a peristaltic pump mechanism
    • 1:CAS:528:DC%2BD28XoslOntbo%3D 16946072
    • Seeger MA, Schiefner A, Eicher T, Verrey F, Diederichs K, Pos KM (2006) Structural asymmetry of AcrB trimer suggests a peristaltic pump mechanism. Science 313:1295-1298
    • (2006) Science , vol.313 , pp. 1295-1298
    • Seeger, M.A.1    Schiefner, A.2    Eicher, T.3    Verrey, F.4    Diederichs, K.5    Pos, K.M.6
  • 91
    • 80051959810 scopus 로고    scopus 로고
    • Preferential use of unobstructed lateral portals as the access route to the pore of human ATP-gated ion channels (P2X receptors)
    • 3158179 1:CAS:528:DC%2BC3MXhtV2ms7fP 21808018
    • Samways D, Khakh B, Dutertre S, Egan T (2011) Preferential use of unobstructed lateral portals as the access route to the pore of human ATP-gated ion channels (P2X receptors). Proc Natl Acad Sci USA 108:13800-13805
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 13800-13805
    • Samways, D.1    Khakh, B.2    Dutertre, S.3    Egan, T.4
  • 92
    • 0032545321 scopus 로고    scopus 로고
    • Structure of the MscL homolog from Mycobacterium tuberculosis: A gated mechanosensitive ion channel
    • Chang G, Spencer RH, Lee A, Barclay MT, Rees DC (1996) Structure of the MscL homolog from Mycobacterium tuberculosis: a gated mechanosensitive ion channel. Science 282:2220-2226
    • (1996) Science , vol.282 , pp. 2220-2226
    • Chang, G.1    Spencer, R.H.2    Lee, A.3    Barclay, M.T.4    Rees, D.C.5
  • 93
    • 14544300522 scopus 로고    scopus 로고
    • CFTR channel opening by ATP-driven tight dimerization of its nucleotide-binding domains
    • 2756053 1:CAS:528:DC%2BD2MXhsFOrtbs%3D 15729345
    • Vergani P, Lockless SW, Nairn AC, Gadsby DC (2005) CFTR channel opening by ATP-driven tight dimerization of its nucleotide-binding domains. Nature 433:876-880
    • (2005) Nature , vol.433 , pp. 876-880
    • Vergani, P.1    Lockless, S.W.2    Nairn, A.C.3    Gadsby, D.C.4
  • 94
    • 0028265949 scopus 로고
    • Effetc of ATP concentration on CFTR Cl- channels: A kinetic analysis of channel regulation
    • 1275860 1:CAS:528:DyaK2cXivFagtbc%3D 7520292
    • Winter MC, Sheppard DN, Carson MR, Welsh MJ (1994) Effetc of ATP concentration on CFTR Cl- channels: a kinetic analysis of channel regulation. Biophys J 66:1398-1403
    • (1994) Biophys J , vol.66 , pp. 1398-1403
    • Winter, M.C.1    Sheppard, D.N.2    Carson, M.R.3    Welsh, M.J.4
  • 95
    • 84870847213 scopus 로고    scopus 로고
    • Nonequilibrium gating of CFTR on an equilibrium theme
    • 1:CAS:528:DC%2BC3sXhsVagtbs%3D 23223629
    • Jih K, Hwang T (2012) Nonequilibrium gating of CFTR on an equilibrium theme. Physiology 27:351-361
    • (2012) Physiology , vol.27 , pp. 351-361
    • Jih, K.1    Hwang, T.2
  • 96
    • 43549091314 scopus 로고    scopus 로고
    • Mutation at arginine 352 alters the pore architecture of CFTR
    • 2474774 1:CAS:528:DC%2BD1cXls1Kks7w%3D 18421494
    • Cui G, Zhang ZR, O'Brien AR, Song B, McCarty NA (2008) Mutation at arginine 352 alters the pore architecture of CFTR. J Membr Biol 222:91-106
    • (2008) J Membr Biol , vol.222 , pp. 91-106
    • Cui, G.1    Zhang, Z.R.2    O'Brien, A.R.3    Song, B.4    McCarty, N.A.5
  • 97
    • 77649256457 scopus 로고    scopus 로고
    • ATP-independent CFTR channel gating and allosteric modulation by phosphorylation
    • 2840504 1:CAS:528:DC%2BC3cXjtFyls7s%3D 20133716
    • Wang W, Wu J, Bernard K, Li G, Wang G, Bevensee M et al (2010) ATP-independent CFTR channel gating and allosteric modulation by phosphorylation. Proc Natl Acad Sci USA 107:3888-3893
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 3888-3893
    • Wang, W.1    Wu, J.2    Bernard, K.3    Li, G.4    Wang, G.5    Bevensee, M.6
  • 98
    • 84907610568 scopus 로고    scopus 로고
    • Metal bridges illuminate transmembrane domain movements during gating of the cystic fibrosis transmembrane conductance regulator chloride channel
    • in press
    • El Hiani Y, Linsdell P (2014) Metal bridges illuminate transmembrane domain movements during gating of the cystic fibrosis transmembrane conductance regulator chloride channel. J Biol Chem (in press)
    • (2014) J Biol Chem
    • El Hiani, Y.1    Linsdell, P.2
  • 99
    • 78349305451 scopus 로고    scopus 로고
    • Evolutionary origin of secondary structures: π-helices as cryptic but widespread insertional variations of α-helices that enhance protein functionality
    • 2981643 1:CAS:528:DC%2BC3cXhsVaitrnK 20888342
    • Cooley R, Arp D, Karplus P (2010) Evolutionary origin of secondary structures: π-helices as cryptic but widespread insertional variations of α-helices that enhance protein functionality. J Mol Biol 404:232-246
    • (2010) J Mol Biol , vol.404 , pp. 232-246
    • Cooley, R.1    Arp, D.2    Karplus, P.3
  • 100
    • 78649930507 scopus 로고    scopus 로고
    • The elusive π-helix
    • 1:CAS:528:DC%2BC3cXhsFCqur%2FP 20828621
    • Riek R, Graham R (2011) The elusive π-helix. J Struct Biol 173:153-160
    • (2011) J Struct Biol , vol.173 , pp. 153-160
    • Riek, R.1    Graham, R.2
  • 101
    • 84861971438 scopus 로고    scopus 로고
    • Phenylalanine 368 of multidrug resistance-associated protein 4 (MRP4/ABCC4) plays a crucial role in substrate-specific transport activity
    • 1:CAS:528:DC%2BC38XmsVert7g%3D 22542979
    • Wittgen H, van den Heuvel J, Krieger E, Schaftenaar G, Russel F, Koenderink J (2012) Phenylalanine 368 of multidrug resistance-associated protein 4 (MRP4/ABCC4) plays a crucial role in substrate-specific transport activity. Biochem Pharmacol 84:366-373
    • (2012) Biochem Pharmacol , vol.84 , pp. 366-373
    • Wittgen, H.1    Van Den Heuvel, J.2    Krieger, E.3    Schaftenaar, G.4    Russel, F.5    Koenderink, J.6
  • 102
    • 78449252630 scopus 로고    scopus 로고
    • Intragenic suppressing mutations correct the folding and intracellular traffic of misfolded mutants of Yor1p, a eukaryotic drug transporter
    • 2978558 1:CAS:528:DC%2BC3cXhsVWgsr7I 20837481
    • Pagant S, Halliday JJ, Kougentakis C, Miller EA (2010) Intragenic suppressing mutations correct the folding and intracellular traffic of misfolded mutants of Yor1p, a eukaryotic drug transporter. J Biol Chem 285:36304-36314
    • (2010) J Biol Chem , vol.285 , pp. 36304-36314
    • Pagant, S.1    Halliday, J.J.2    Kougentakis, C.3    Miller, E.A.4
  • 103
    • 84880506420 scopus 로고    scopus 로고
    • Effects of the gout-causing Q141K polymorphism and a CFTR Δf508 mimicking mutation on the processing and stability of the ABCG2 protein
    • 23800412
    • Sarankó H, Tordai H, Telbisz Á, Özvegy-Laczka C, Erdo{combining double acute accent}s G, Sarkadi B et al (2013) Effects of the gout-causing Q141K polymorphism and a CFTR ΔF508 mimicking mutation on the processing and stability of the ABCG2 protein. Biochem Biophys Res Commun 437:140-145
    • (2013) Biochem Biophys Res Commun , vol.437 , pp. 140-145
    • Sarankó, H.1    Tordai, H.2    Telbisz, Á.3    Özvegy-Laczka, C.4    Erdos, G.5    Sarkadi, B.6
  • 104
    • 84901689529 scopus 로고    scopus 로고
    • A "SYDE" effect of hierarchical phosphorylation: Possible relevance to the cystic fibrosis basic defect
    • 1:CAS:528:DC%2BC2cXjt1SqsbY%3D 24566881
    • Venerando A, Cesaro L, Marin O, Donella-Deana A, Pinna LA (2014) A "SYDE" effect of hierarchical phosphorylation: possible relevance to the cystic fibrosis basic defect. Cell Mol Life Sci 71:2193-2196
    • (2014) Cell Mol Life Sci , vol.71 , pp. 2193-2196
    • Venerando, A.1    Cesaro, L.2    Marin, O.3    Donella-Deana, A.4    Pinna, L.A.5


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