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Volumn 27, Issue 6, 2012, Pages 351-361

Nonequilibrium gating of CFTR on an equilibrium Theme

Author keywords

[No Author keywords available]

Indexed keywords

ABC TRANSPORTER; CHLORIDE CHANNEL; CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR;

EID: 84870847213     PISSN: 15489213     EISSN: 15489221     Source Type: Journal    
DOI: 10.1152/physiol.00026.2012     Document Type: Review
Times cited : (34)

References (84)
  • 2
    • 0037042224 scopus 로고    scopus 로고
    • Nucleoside triphosphate pentose ring impact on CFTR gating and hydrolysis
    • Aleksandrov AA, Aleksandrov L, Riordan JR. Nucleoside triphosphate pentose ring impact on CFTR gating and hydrolysis. FEBS Lett 518: 183-188, 2002.
    • (2002) FEBS Lett , vol.518 , pp. 183-188
    • Aleksandrov, A.A.1    Aleksandrov, L.2    Riordan, J.R.3
  • 4
    • 0033759953 scopus 로고    scopus 로고
    • The non-hydrolytic pathway of cystic fibrosis transmembrane conductance regulator ion channel gating
    • Aleksandrov AA, Chang X, Aleksandrov L, Riordan JR. The non-hydrolytic pathway of cystic fibrosis transmembrane conductance regulator ion channel gating. J Physiol 528: 259-265, 2000.
    • (2000) J Physiol , vol.528 , pp. 259-265
    • Aleksandrov, A.A.1    Chang, X.2    Aleksandrov, L.3    Riordan, J.R.4
  • 5
    • 67649659825 scopus 로고    scopus 로고
    • Relationship between nucleotide binding and ion channel gating in cystic fibrosis transmembrane conductance regulator
    • Aleksandrov AA, Cui L, Riordan JR. Relationship between nucleotide binding and ion channel gating in cystic fibrosis transmembrane conductance regulator. J Physiol 587: 2875-2886, 2009.
    • (2009) J Physiol , vol.587 , pp. 2875-2886
    • Aleksandrov, A.A.1    Cui, L.2    Riordan, J.R.3
  • 6
    • 70350236733 scopus 로고    scopus 로고
    • Cystic fibrosis transmembrane conductance regulator: Using differential reactivity toward channelpermeant and channel-impermeant thiol-reactive probes to test a molecular model for the pore
    • Alexander C, Ivetac A, Liu X, Norimatsu Y, Serrano JR, Landstrom A, Sansom M, Dawson DC. Cystic fibrosis transmembrane conductance regulator: using differential reactivity toward channelpermeant and channel-impermeant thiol-reactive probes to test a molecular model for the pore. Biochemistry 48: 10078-10088, 2009.
    • (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    Sansom, M.7    Dawson, D.C.8
  • 8
    • 77956237499 scopus 로고    scopus 로고
    • Dual roles of the sixth transmembrane segment of the CFTR chloride channel in gating and permeation
    • Bai Y, Li M, Hwang TC. Dual roles of the sixth transmembrane segment of the CFTR chloride channel in gating and permeation. J Gen Physiol 136: 293-309, 2010.
    • (2010) J Gen Physiol , vol.136 , pp. 293-309
    • Bai, Y.1    Li, M.2    Hwang, T.C.3
  • 9
    • 80555127440 scopus 로고    scopus 로고
    • Structural basis for the channel function of a degraded ABC transporter, CFTR (ABCC7)
    • Bai Y, Li M, Hwang TC. Structural basis for the channel function of a degraded ABC transporter, CFTR (ABCC7). J Gen Physiol 138: 495-507, 2011.
    • (2011) J Gen Physiol , vol.138 , pp. 495-507
    • Bai, Y.1    Li, M.2    Hwang, T.C.3
  • 11
    • 0026532895 scopus 로고
    • Purification and functional reconstitution of the cystic fibrosis transmembrane conductance regulator (CFTR)
    • Bear CE, Li CH, Kartner N, Bridges RJ, Jensen TJ, Ramjeesingh M, Riordan JR. 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
  • 12
    • 17044383747 scopus 로고    scopus 로고
    • CFTR gating I: Characterization of the ATP-dependent gating of a phosphorylation-independent CFTR channel (DeltaR-CFTR)
    • Bompadre SG, Ai T, Cho JH, Wang X, Sohma Y, Li M, Hwang TC. CFTR gating I: characterization of the ATP-dependent gating of a phosphorylation-independent CFTR channel (DeltaR-CFTR). J Gen Physiol 125: 361-375, 2005.
    • (2005) J Gen Physiol , vol.125 , pp. 361-375
    • Bompadre, S.G.1    Ai, T.2    Cho, J.H.3    Wang, X.4    Sohma, Y.5    Li, M.6    Hwang, T.C.7
  • 14
    • 33947725805 scopus 로고    scopus 로고
    • G551D and G1349D, two CF-associated mutations in the signature sequences of CFTR, exhibit distinct gating defects
    • Bompadre SG, Sohma Y, Li M, Hwang TC. G551D and G1349D, two CF-associated mutations in the signature sequences of CFTR, exhibit distinct gating defects. J Gen Physiol 129: 285-298, 2007.
    • (2007) J Gen Physiol , vol.129 , pp. 285-298
    • Bompadre, S.G.1    Sohma, Y.2    Li, M.3    Hwang, T.C.4
  • 15
    • 79958088886 scopus 로고    scopus 로고
    • Targeting F508del-CFTR to develop rational new therapies for cystic fibrosis
    • Cai ZW, Liu J, Li HY, Sheppard DN. Targeting F508del-CFTR to develop rational new therapies for cystic fibrosis. Acta Pharmacol Sin 32: 693-701, 2011.
    • (2011) Acta Pharmacol Sin , vol.32 , pp. 693-701
    • Cai, Z.W.1    Liu, J.2    Li, H.Y.3    Sheppard, D.N.4
  • 16
    • 0028906612 scopus 로고
    • The two nucleotide-binding domains of cystic fibrosis transmembrane conductance regulator (CFTR) have distinct functions in controlling channel activity
    • Carson MR, Travis SM, Welsh MJ. The two nucleotide-binding domains of cystic fibrosis transmembrane conductance regulator (CFTR) have distinct functions in controlling channel activity. J Biol Chem 270: 1711-1717, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 1711-1717
    • Carson, M.R.1    Travis, S.M.2    Welsh, M.J.3
  • 17
    • 0042025073 scopus 로고    scopus 로고
    • N-terminal transmembrane domain of the SUR controls trafficking and gating of Kir6 channel subunits
    • Chan KW, Zhang H, Logothetis DE. N-terminal transmembrane domain of the SUR controls trafficking and gating of Kir6 channel subunits. EMBO J 22: 3833-3843, 2003.
    • (2003) EMBO J , vol.22 , pp. 3833-3843
    • Chan, K.W.1    Zhang, H.2    Logothetis, D.E.3
  • 18
    • 42049096734 scopus 로고    scopus 로고
    • CLC-0 and CFTR: Chloride channels evolved from transporters
    • Chen TY, Hwang TC. CLC-0 and CFTR: chloride channels evolved from transporters. Physiol Rev 88: 351-387, 2008.
    • (2008) Physiol Rev , vol.88 , pp. 351-387
    • Chen, T.Y.1    Hwang, T.C.2
  • 19
    • 0033230588 scopus 로고    scopus 로고
    • Coupled chemical and mechanical reaction steps in a processive Neurospora kinesin
    • Crevel I, Carter N, Schliwa M, Cross R. Coupled chemical and mechanical reaction steps in a processive Neurospora kinesin. EMBO J 18: 5863-5872, 1999.
    • (1999) EMBO J , vol.18 , pp. 5863-5872
    • Crevel, I.1    Carter, N.2    Schliwa, M.3    Cross, R.4
  • 20
    • 67749084300 scopus 로고    scopus 로고
    • Application of rate-equilibrium free energy relationship analysis to nonequilibrium ion channel gating mechanisms
    • Csanady L. Application of rate-equilibrium free energy relationship analysis to nonequilibrium ion channel gating mechanisms. J Gen Physiol 134: 129-136, 2009.
    • (2009) J Gen Physiol , vol.134 , pp. 129-136
    • Csanady, L.1
  • 21
    • 0033817333 scopus 로고    scopus 로고
    • Severed channels probe regulation of gating of cystic fibrosis transmembrane conductance regulator by its cytoplasmic domains
    • Csanady L, Chan KW, Seto-Young D, Kopsco DC, Nairn AC, Gadsby DC. Severed channels probe regulation of gating of cystic fibrosis transmembrane conductance regulator by its cytoplasmic domains. J Gen Physiol 116: 477-500, 2000.
    • (2000) J Gen Physiol , vol.116 , pp. 477-500
    • Csanady, L.1    Chan, K.W.2    Seto-Young, D.3    Kopsco, D.C.4    Nairn, A.C.5    Gadsby, D.C.6
  • 22
    • 33750499982 scopus 로고    scopus 로고
    • Thermodynamics of CFTR channel gating: A spreading conformational change initiates an irreversible gating cycle
    • Csanady L, Nairn AC, Gadsby DC. Thermodynamics of CFTR channel gating: a spreading conformational change initiates an irreversible gating cycle. J Gen Physiol 128: 523-533, 2006.
    • (2006) J Gen Physiol , vol.128 , pp. 523-533
    • Csanady, L.1    Nairn, A.C.2    Gadsby, D.C.3
  • 23
    • 75749153312 scopus 로고    scopus 로고
    • Strict coupling between CFTR's catalytic cycle and gating of its Cl ion pore revealed by distributions of open channel burst durations
    • Csanady L, Vergani P, Gadsby DC. Strict coupling between CFTR's catalytic cycle and gating of its Cl ion pore revealed by distributions of open channel burst durations. Proc Natl Acad Sci USA 107: 1241-1246, 2010.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 1241-1246
    • Csanady, L.1    Vergani, P.2    Gadsby, D.C.3
  • 25
    • 3943062954 scopus 로고    scopus 로고
    • ATP-binding cassette transporters in bacteria
    • Davidson AL, Chen J. ATP-binding cassette transporters in bacteria. Ann Rev Biochem 73: 241-268, 2004.
    • (2004) Ann Rev Biochem , vol.73 , pp. 241-268
    • Davidson, A.L.1    Chen, J.2
  • 26
    • 33748644877 scopus 로고    scopus 로고
    • Structure of a bacterial multidrug ABC transporter
    • Dawson RJ, Locher KP. Structure of a bacterial multidrug ABC transporter. Nature 443: 180-185, 2006.
    • (2006) Nature , vol.443 , pp. 180-185
    • Dawson, R.J.1    Locher, K.P.2
  • 27
    • 77957761417 scopus 로고    scopus 로고
    • Changes in accessibility of cytoplasmic substances to the pore associated with activation of the cystic fibrosis transmembrane conductance regulator chloride channel
    • El Hiani Y, Linsdell P. Changes in accessibility of cytoplasmic substances to the pore associated with activation of the cystic fibrosis transmembrane conductance regulator chloride channel. J Biol Chem 285: 32126-32140, 2010.
    • (2010) J Biol Chem , vol.285 , pp. 32126-32140
    • El Hiani, Y.1    Linsdell, P.2
  • 28
    • 78049362741 scopus 로고    scopus 로고
    • Structure of a eukaryotic CLC transporter defines an intermediate state in the transport cycle
    • Feng L, Campbell EB, Hsiung Y, MacKinnon R. Structure of a eukaryotic CLC transporter defines an intermediate state in the transport cycle. Science 330: 635-641, 2010.
    • (2010) Science , vol.330 , pp. 635-641
    • Feng, L.1    Campbell, E.B.2    Hsiung, Y.3    Mackinnon, R.4
  • 29
    • 0019194038 scopus 로고
    • The recognition of maltodextrins by Escherichia coli
    • Ferenci T. The recognition of maltodextrins by Escherichia coli. Eur J Biochem 108: 631-636, 1980.
    • (1980) Eur J Biochem , vol.108 , pp. 631-636
    • Ferenci, T.1
  • 30
    • 67349185408 scopus 로고    scopus 로고
    • Ion channels versus ion pumps: The principal difference, in principle
    • Gadsby DC. Ion channels versus ion pumps: the principal difference, in principle. Nat Rev Mol Cell Biol 10: 344-352, 2009.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 344-352
    • Gadsby, D.C.1
  • 31
    • 33645307384 scopus 로고    scopus 로고
    • The ABC protein turned chloride channel whose failure causes cystic fibrosis
    • Gadsby DC, Vergani P, Csanady L. The ABC protein turned chloride channel whose failure causes cystic fibrosis. Nature 440: 477-483, 2006.
    • (2006) Nature , vol.440 , pp. 477-483
    • Gadsby, D.C.1    Vergani, P.2    Csanady, L.3
  • 32
    • 0034724680 scopus 로고    scopus 로고
    • Comparison of the functional characteristics of the nucleotide binding domains of multidrug resistance protein 1
    • Gao M, Cui HR, Loe DW, Grant CE, Almquist KC, Cole SP, Deeley RG. Comparison of the functional characteristics of the nucleotide binding domains of multidrug resistance protein 1. J Biol Chem 275: 13098-13108, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 13098-13108
    • Gao, M.1    Cui, H.R.2    Loe, D.W.3    Grant, C.E.4    Almquist, K.C.5    Cole, S.P.6    Deeley, R.G.7
  • 33
    • 0035682189 scopus 로고    scopus 로고
    • Overview: ABC transporters and human disease
    • Gottesman MM, Ambudkar SV. Overview: ABC transporters and human disease. J Bioenerg Biomembr 33: 453-458, 2001.
    • (2001) J Bioenerg Biomembr , vol.33 , pp. 453-458
    • Gottesman, M.M.1    Ambudkar, S.V.2
  • 34
    • 0029117303 scopus 로고
    • Conformational states of CFTR associated with channel gating: The role ATP binding and hydrolysis
    • Gunderson KL, Kopito RR. Conformational states of CFTR associated with channel gating: the role ATP binding and hydrolysis. Cell 82: 231-239, 1995.
    • (1995) Cell , vol.82 , pp. 231-239
    • Gunderson, K.L.1    Kopito, R.R.2
  • 35
    • 0028070453 scopus 로고
    • Effects of pyrophosphate and nucleotide analogs suggest a role for ATP hydrolysis in cystic fibrosis transmembrane regulator channel gating
    • Gunderson KL, Kopito RR. Effects of pyrophosphate and nucleotide analogs suggest a role for ATP hydrolysis in cystic fibrosis transmembrane regulator channel gating. J Biol Chem 269: 19349-19353, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 19349-19353
    • Gunderson, K.L.1    Kopito, R.R.2
  • 36
    • 84860417445 scopus 로고    scopus 로고
    • ATP hydrolysis at one of the two sites in ABC transporters initiates transport related conformational transitions
    • Gyimesi G, Ramachandran S, Kota P, Dokholyan NV, Sarkadi B, Hegedus T. ATP hydrolysis at one of the two sites in ABC transporters initiates transport related conformational transitions. Biochim Biophys Acta 1808: 2954-2964, 2011.
    • (2011) Biochim Biophys Acta , vol.1808 , pp. 2954-2964
    • Gyimesi, G.1    Ramachandran, S.2    Kota, P.3    Dokholyan, N.V.4    Sarkadi, B.5    Hegedus, T.6
  • 37
    • 84861310612 scopus 로고    scopus 로고
    • Crystal structure of a heterodimeric ABC transporter in its inward-facing conformation
    • Hohl M, Briand C, Grutter MG, Seeger MA. Crystal structure of a heterodimeric ABC transporter in its inward-facing conformation. Nature Struct Mol Biol 19: 395-402, 2012.
    • (2012) Nature Struct Mol Biol , vol.19 , pp. 395-402
    • Hohl, M.1    Briand, C.2    Grutter, M.G.3    Seeger, M.A.4
  • 38
    • 33947154878 scopus 로고    scopus 로고
    • Structure of an ABC transporter in complex with its binding protein
    • Hollenstein K, Frei DC, Locher KP. Structure of an ABC transporter in complex with its binding protein. Nature 446: 213-216, 2007.
    • (2007) Nature , vol.446 , pp. 213-216
    • Hollenstein, K.1    Frei, D.C.2    Locher, K.P.3
  • 39
    • 0034617097 scopus 로고    scopus 로고
    • Allosteric interactions between the two non-equivalent nucleotide binding domains of multidrug resistance protein MRP1
    • Hou Y, Cui L, Riordan JR, Chang X. Allosteric interactions between the two non-equivalent nucleotide binding domains of multidrug resistance protein MRP1. J Biol Chem 275: 20280-20287, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 20280-20287
    • Hou, Y.1    Cui, L.2    Riordan, J.R.3    Chang, X.4
  • 40
    • 34548671159 scopus 로고    scopus 로고
    • Asymmetry in the structure of the ABC transporter-binding protein complex BtuCD-BtuF
    • Hvorup RN, Goetz BA, Niederer M, Hollenstein K, Perozo E, Locher KP. Asymmetry in the structure of the ABC transporter-binding protein complex BtuCD-BtuF. Science 317: 1387-1390, 2007.
    • (2007) Science , vol.317 , pp. 1387-1390
    • Hvorup, R.N.1    Goetz, B.A.2    Niederer, M.3    Hollenstein, K.4    Perozo, E.5    Locher, K.P.6
  • 41
    • 0028340159 scopus 로고
    • Regulation of the gating of cystic fibrosis transmembrane conductance regulator Cl channels by phosphorylation and ATP hydrolysis
    • Hwang TC, Nagel G, Nairn AC, Gadsby DC. 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
  • 42
    • 65749102092 scopus 로고    scopus 로고
    • Gating of the CFTR Cl channel by ATP-driven nucleotide-binding domain dimerisation
    • Hwang TC, Sheppard DN. Gating of the CFTR Cl channel by ATP-driven nucleotide-binding domain dimerisation. J Physiol 587: 2151-2161, 2009.
    • (2009) J Physiol , vol.587 , pp. 2151-2161
    • Hwang, T.C.1    Sheppard, D.N.2
  • 43
    • 0030668944 scopus 로고    scopus 로고
    • Block by MOPS reveals a conformation change in the CFTR pore produced by ATP hydrolysis
    • Ishihara H, Welsh MJ. Block by MOPS reveals a conformation change in the CFTR pore produced by ATP hydrolysis. Am J Physiol Cell Physiol 273: C1278-C1289, 1997.
    • (1997) Am J Physiol Cell Physiol , vol.273
    • Ishihara, H.1    Welsh, M.J.2
  • 44
    • 33947284958 scopus 로고    scopus 로고
    • Dynamics and function in a bacterial ABC transporter: Simulation studies of the BtuCDF system and its components
    • Ivetac A, Campbell JD, Sansom MS. Dynamics and function in a bacterial ABC transporter: simulation studies of the BtuCDF system and its components. Biochemistry 46: 2767-2778, 2007.
    • (2007) Biochemistry , vol.46 , pp. 2767-2778
    • Ivetac, A.1    Campbell, J.D.2    Sansom, M.S.3
  • 45
    • 0022628717 scopus 로고
    • Kinetics of unliganded acetylcholine receptor channel gating
    • Jackson MB. Kinetics of unliganded acetylcholine receptor channel gating. Biophys J 49: 663-672, 1986.
    • (1986) Biophys J , vol.49 , pp. 663-672
    • Jackson, M.B.1
  • 46
    • 84861167188 scopus 로고    scopus 로고
    • Identification of a novel post-hydrolytic state in CFTR gating
    • Jih KY, Sohma Y, Li M, Hwang TC. Identification of a novel post-hydrolytic state in CFTR gating. J Gen Physiol 139: 359-370, 2012.
    • (2012) J Gen Physiol , vol.139 , pp. 359-370
    • Jih, K.Y.1    Sohma, Y.2    Li, M.3    Hwang, T.C.4
  • 47
    • 84870795585 scopus 로고    scopus 로고
    • Nonintegral stoichiometry in CFTR gating revealed by a pore-lining mutation
    • Jih KY, Sohma Y, Hwang TC. Nonintegral stoichiometry in CFTR gating revealed by a pore-lining mutation. J Gen Physiol 140: 347-359, 2012.
    • (2012) J Gen Physiol , vol.140 , pp. 347-359
    • Jih, K.Y.1    Sohma, Y.2    Hwang, T.C.3
  • 48
    • 60549097035 scopus 로고    scopus 로고
    • Alternating access in maltose transporter mediated by rigid-body rotations
    • Khare D, Oldham ML, Orelle C, Davidson AL, Chen J. Alternating access in maltose transporter mediated by rigid-body rotations. Mol Cell 33: 528-536, 2009.
    • (2009) Mol Cell , vol.33 , pp. 528-536
    • Khare, D.1    Oldham, M.L.2    Orelle, C.3    Davidson, A.L.4    Chen, J.5
  • 51
    • 0037052565 scopus 로고    scopus 로고
    • The E. coli BtuCD structure: A framework for ABC transporter architecture and mechanism
    • Locher KP, Lee AT, Rees DC. The E. coli BtuCD structure: a framework for ABC transporter architecture and mechanism. Science 296: 1091-1098, 2002.
    • (2002) Science , vol.296 , pp. 1091-1098
    • Locher, K.P.1    Lee, A.T.2    Rees, D.C.3
  • 52
    • 0033601321 scopus 로고    scopus 로고
    • ATP binding properties of the nucleotide-binding folds of SUR1
    • Matsuo M, Kioka N, Amachi T, Ueda K. ATP binding properties of the nucleotide-binding folds of SUR1. J Biol Chem 274: 37479-37482,1999.
    • (1999) J Biol Chem , vol.274 , pp. 37479-37482
    • Matsuo, M.1    Kioka, N.2    Amachi, T.3    Ueda, K.4
  • 53
    • 33750222000 scopus 로고    scopus 로고
    • In vivo phosphorylation of CFTR promotes formation of a nucleotidebinding domain heterodimer
    • Mense M, Vergani P, White DM, Altberg G, Nairn AC, Gadsby DC. In vivo phosphorylation of CFTR promotes formation of a nucleotidebinding domain heterodimer. EMBO J 25: 4728-4739, 2006.
    • (2006) EMBO J , vol.25 , pp. 4728-4739
    • Mense, M.1    Vergani, P.2    White, D.M.3    Altberg, G.4    Nairn, A.C.5    Gadsby, D.C.6
  • 54
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: A plausible model
    • Monod J, Wyman J, Changeux JP. On the nature of allosteric transitions: a plausible model. J Mol Biol 12: 88-118, 1965.
    • (1965) J Mol Biol , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, J.2    Changeux, J.P.3
  • 55
    • 0036843663 scopus 로고    scopus 로고
    • The significance of molecular slips in transport systems
    • Nelson N, Sacher A, Nelson H. The significance of molecular slips in transport systems. Nature Rev Mol Cell Biol 3: 876-881, 2002.
    • (2002) Nature Rev Mol Cell Biol , vol.3 , pp. 876-881
    • Nelson, N.1    Sacher, A.2    Nelson, H.3
  • 56
    • 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
    • Norimatsu Y, Ivetac A, Alexander C, Kirkham J, O'Donnell N, Dawson DC, Sansom MS. 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.
    • (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    Sansom, M.S.7
  • 57
    • 36549018568 scopus 로고    scopus 로고
    • Crystal structure of a catalytic intermediate of the maltose transporter
    • Oldham ML, Khare D, Quiocho FA, Davidson AL, Chen J. Crystal structure of a catalytic intermediate of the maltose transporter. Nature 450: 515-521, 2007.
    • (2007) Nature , vol.450 , pp. 515-521
    • Oldham, M.L.1    Khare, D.2    Quiocho, F.A.3    Davidson, A.L.4    Chen, J.5
  • 58
    • 0035896542 scopus 로고    scopus 로고
    • Regulation of the cystic fibrosis transmembrane conductance regulator Cl channel by its R domain
    • Ostedgaard LS, Baldursson O, Welsh MJ. Regulation of the cystic fibrosis transmembrane conductance regulator Cl channel by its R domain. J Biol Chem 276: 7689-7692, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 7689-7692
    • Ostedgaard, L.S.1    Baldursson, O.2    Welsh, M.J.3
  • 59
    • 33846601303 scopus 로고    scopus 로고
    • An inward-facing conformation of a putative metalchelate-type ABC transporter
    • Pinkett HW, Lee AT, Lum P, Locher KP, Rees DC. An inward-facing conformation of a putative metalchelate-type ABC transporter. Science 315: 373-377, 2007.
    • (2007) Science , vol.315 , pp. 373-377
    • Pinkett, H.W.1    Lee, A.T.2    Lum, P.3    Locher, K.P.4    Rees, D.C.5
  • 60
    • 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
    • Qian F, El Hiani Y, Linsdell P. Functional arrangement of the 12th transmembrane region in the CFTR chloride channel pore based on functional investigation of a cysteine-less CFTR variant. Pflügers Arch 462: 559-571, 2011.
    • (2011) Pflügers Arch , vol.462 , pp. 559-571
    • Qian, F.1    El Hiani, Y.2    Linsdell, P.3
  • 63
    • 0025270712 scopus 로고
    • Steady-state coupling of ion-channel conformations to a transmembrane ion gradient
    • Richard EA, Miller C. Steady-state coupling of ion-channel conformations to a transmembrane ion gradient. Science 247: 1208-1210, 1990.
    • (1990) Science , vol.247 , pp. 1208-1210
    • Richard, E.A.1    Miller, C.2
  • 66
    • 40949121607 scopus 로고    scopus 로고
    • ABC multidrug transporters: Structure, function and role in chemoresistance
    • Sharom FJ. ABC multidrug transporters: structure, function and role in chemoresistance. Pharmacogenomics 9: 105-127, 2008.
    • (2008) Pharmacogenomics , vol.9 , pp. 105-127
    • Sharom, F.J.1
  • 67
    • 79951822357 scopus 로고    scopus 로고
    • Cystic fibrosis: CFTR correctors to the rescue
    • Sheppard DN. Cystic fibrosis: CFTR correctors to the rescue. Chem Biol 18: 145-147, 2011.
    • (2011) Chem Biol , vol.18 , pp. 145-147
    • Sheppard, D.N.1
  • 68
    • 33846521753 scopus 로고    scopus 로고
    • The Walker B motif of the second nucleotide-binding domain (NBD2) of CFTR plays a key role in ATPase activity by the NBD1-NBD2 heterodimer
    • Stratford FL, Ramjeesingh M, Cheung JC, Huan LJ, Bear CE. The Walker B motif of the second nucleotide-binding domain (NBD2) of CFTR plays a key role in ATPase activity by the NBD1-NBD2 heterodimer. Biochem J 401: 581-586, 2007.
    • (2007) Biochem J , vol.401 , pp. 581-586
    • Stratford, F.L.1    Ramjeesingh, M.2    Cheung, J.C.3    Huan, L.J.4    Bear, C.E.5
  • 69
    • 79958076650 scopus 로고    scopus 로고
    • Mutant cycles at CFTR's non-canonical ATP-binding site support little interface separation during gating
    • Szollosi A, Muallem DR, Csanady L, Vergani P. Mutant cycles at CFTR's non-canonical ATP-binding site support little interface separation during gating. J Gen Physiol 137: 549-562, 2011.
    • (2011) J Gen Physiol , vol.137 , pp. 549-562
    • Szollosi, A.1    Muallem, D.R.2    Csanady, L.3    Vergani, P.4
  • 70
    • 77951706563 scopus 로고    scopus 로고
    • Stable ATP binding mediated by a partial NBD dimer of the CFTR chloride channel
    • Tsai MF, Li M, Hwang TC. Stable ATP binding mediated by a partial NBD dimer of the CFTR chloride channel. J Gen Physiol 135: 399-414, 2010.
    • (2010) J Gen Physiol , vol.135 , pp. 399-414
    • Tsai, M.F.1    Li, M.2    Hwang, T.C.3
  • 71
    • 64549132504 scopus 로고    scopus 로고
    • State-dependent modulation of CFTR gating by pyrophosphate
    • Tsai MF, Shimizu H, Sohma Y, Li M, Hwang TC. State-dependent modulation of CFTR gating by pyrophosphate. J Gen Physiol 133: 405-419, 2009.
    • (2009) J Gen Physiol , vol.133 , pp. 405-419
    • Tsai, M.F.1    Shimizu, H.2    Sohma, Y.3    Li, M.4    Hwang, T.C.5
  • 72
    • 0033574068 scopus 로고    scopus 로고
    • Cooperative binding of ATP and MgADP in the sulfonylurea receptor is modulated by glibenclamide
    • Ueda K, Komine J, Matsuo M, Seino S, Amachi T. Cooperative binding of ATP and MgADP in the sulfonylurea receptor is modulated by glibenclamide. Proc Natl Acad Sci USA 96: 1268-1272, 1999.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 1268-1272
    • Ueda, K.1    Komine, J.2    Matsuo, M.3    Seino, S.4    Amachi, T.5
  • 75
    • 14544300522 scopus 로고    scopus 로고
    • CFTR channel opening by ATP-driven tight dimerization of its nucleotide-binding domains
    • Vergani P, Lockless SW, Nairn AC, Gadsby DC. CFTR channel opening by ATP-driven tight dimerization of its nucleotide-binding domains. Nature 433: 876-880, 2005.
    • (2005) Nature , vol.433 , pp. 876-880
    • Vergani, P.1    Lockless, S.W.2    Nairn, A.C.3    Gadsby, D.C.4
  • 76
    • 0037246832 scopus 로고    scopus 로고
    • On the mechanism of MgATP-dependent gating of CFTR Cl channels
    • Vergani P, Nairn AC, Gadsby DC. On the mechanism of MgATP-dependent gating of CFTR Cl channels. J Gen Physiol 121: 17-36, 2003.
    • (2003) J Gen Physiol , vol.121 , pp. 17-36
    • Vergani, P.1    Nairn, A.C.2    Gadsby, D.C.3
  • 77
    • 33745120825 scopus 로고    scopus 로고
    • CFTR chloride channel drug discovery: Inhibitors as antidiarrheals and activators for therapy of cystic fibrosis
    • Verkman AS, Lukacs GL, Galietta LJ. CFTR chloride channel drug discovery: inhibitors as antidiarrheals and activators for therapy of cystic fibrosis. Curr Pharmaceut Design 12: 2235-2247, 2006.
    • (2006) Curr Pharmaceut Design , vol.12 , pp. 2235-2247
    • Verkman, A.S.1    Lukacs, G.L.2    Galietta, L.J.3
  • 78
    • 33947543364 scopus 로고    scopus 로고
    • Curcumin opens cystic fibrosis transmembrane conductance regulator channels by a novel mechanism that requires neither ATP binding nor dimerization of the nucleotide-binding domains
    • Wang W, Bernard K, Li G, Kirk KL. Curcumin opens cystic fibrosis transmembrane conductance regulator channels by a novel mechanism that requires neither ATP binding nor dimerization of the nucleotide-binding domains. J Biol Chem 282: 4533-4544, 2007.
    • (2007) J Biol Chem , vol.282 , pp. 4533-4544
    • Wang, W.1    Bernard, K.2    Li, G.3    Kirk, K.L.4
  • 79
    • 79961146667 scopus 로고    scopus 로고
    • Alignment of transmembrane regions in the cystic fibrosis transmembrane conductance regulator chloride channel pore
    • Wang W, El Hiani Y, Linsdell P. Alignment of transmembrane regions in the cystic fibrosis transmembrane conductance regulator chloride channel pore. J Gen Physiol 138: 165-178, 2011.
    • (2011) J Gen Physiol , vol.138 , pp. 165-178
    • Wang, W.1    El Hiani, Y.2    Linsdell, P.3
  • 80
    • 82755162382 scopus 로고    scopus 로고
    • Thermally unstable gating of the most common cystic fibrosis mutant channel (DeltaF508): "rescue" by suppressor mutations in nucleotide binding domain 1 and by constitutive mutations in the cytosolic loops
    • Wang W, Okeyo GO, Tao B, Hong JS, Kirk KL. Thermally unstable gating of the most common cystic fibrosis mutant channel (DeltaF508): "rescue" by suppressor mutations in nucleotide binding domain 1 and by constitutive mutations in the cytosolic loops. J Biol Chem 286: 41937-41948, 2011.
    • (2011) J Biol Chem , vol.286 , pp. 41937-41948
    • Wang, W.1    Okeyo, G.O.2    Tao, B.3    Hong, J.S.4    Kirk, K.L.5
  • 82
    • 37649004412 scopus 로고    scopus 로고
    • Flexibility in the ABC transporter MsbA: Alternating access with a twist
    • Ward A, Reyes CL, Yu J, Roth CB, Chang G. Flexibility in the ABC transporter MsbA: alternating access with a twist. Proc Natl Acad Sci USA 104: 19005-19010, 2007.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 19005-19010
    • Ward, A.1    Reyes, C.L.2    Yu, J.3    Roth, C.B.4    Chang, G.5
  • 84
    • 0032954806 scopus 로고    scopus 로고
    • Gating of cystic fibrosis transmembrane conductance regulator chloride channels by adenosine triphosphate hydrolysis. Quantitative analysis of a cyclic gating scheme
    • Zeltwanger S, Wang F, Wang GT, Gillis KD, Hwang TC. Gating of cystic fibrosis transmembrane conductance regulator chloride channels by adenosine triphosphate hydrolysis. Quantitative analysis of a cyclic gating scheme. J Gen Physiol 113: 541-554, 1999.
    • (1999) J Gen Physiol , vol.113 , pp. 541-554
    • Zeltwanger, S.1    Wang, F.2    Wang, G.T.3    Gillis, K.D.4    Hwang, T.C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.