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Volumn 136, Issue 4, 2010, Pages 407-423

Involvement of F1296 and N1303 of CFTR in induced-fit conformational change in response to ATP binding at NBD2

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; TRANSMEMBRANE CONDUCTANCE REGULATOR;

EID: 77957853858     PISSN: 00221295     EISSN: 15407748     Source Type: Journal    
DOI: 10.1085/jgp.201010434     Document Type: Article
Times cited : (20)

References (42)
  • 1
    • 0037013262 scopus 로고    scopus 로고
    • The first nucleotide binding domain of cystic fibrosis transmembrane conductance regulator is a site of stable nucleotide interaction, whereas the second is a site of rapid turnover
    • DOI 10.1074/jbc.M111713200
    • Aleksandrov, L., A.A. Aleksandrov, X.B. Chang, and J.R. Riordan. 2002. The first nucleotide binding domain of cystic fibrosis transmembrane conductance regulator is a site of stable nucleotide interaction, whereas the second is a site of rapid turnover. J. Biol. Chem. 277:15419-15425. doi:10.1074/jbc. M111713200 (Pubitemid 34967805)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.18 , pp. 15419-15425
    • Aleksandrov, L.1    Aleksandrov, A.A.2    Chang, X.-B.3    Riordan, J.R.4
  • 2
    • 0141513675 scopus 로고    scopus 로고
    • 2-terminal nucleotide binding domain and its role in channel gating
    • DOI 10.1085/jgp.200308798
    • 2-terminal nucleotide binding domain and its role in channel gating. J. Gen. Physiol. 122:333-348. doi:10.1085/jgp.200308798 (Pubitemid 37163281)
    • (2003) Journal of General Physiology , vol.122 , Issue.3 , pp. 333-348
    • Basso, C.1    Vergani, P.2    Nairn, A.C.3    Gadsby, D.C.4
  • 3
    • 0037127222 scopus 로고    scopus 로고
    • Mutations that change the position of the putative gammaphosphate linker in the nucleotide binding domains of CFTR alter channel gating
    • Berger, A.L., M. Ikuma, J.F. Hunt, P.J. Thomas, and M.J. Welsh. 2002. Mutations that change the position of the putative gammaphosphate linker in the nucleotide binding domains of CFTR alter channel gating. J. Biol. Chem. 277:2125-2131.
    • (2002) J. Biol. Chem. , vol.277 , pp. 2125-2131
    • Berger, A.L.1    Ikuma, M.2    Hunt, J.F.3    Thomas, P.J.4    Welsh, M.J.5
  • 4
    • 17044401724 scopus 로고    scopus 로고
    • CFTR gating II: Effects of nucleotide binding on the stability of open states
    • doi:10.1085/jgp.200409228
    • Bompadre, S.G., J.H. Cho, X. Wang, X. Zou, Y. Sohma, M. Li, and T.C. Hwang. 2005. CFTR gating II: effects of nucleotide binding on the stability of open states. J. Gen. Physiol. 125:377-394. doi:10.1085/jgp.200409228
    • (2005) J. Gen. Physiol. , vol.125 , pp. 377-394
    • Bompadre, S.G.1    Cho, J.H.2    Wang, X.3    Zou, X.4    Sohma, Y.5    Li, M.6    Hwang, T.C.7
  • 7
    • 0141527345 scopus 로고    scopus 로고
    • A tweezers-like motion of the ATP-binding cassette dimer in an ABC transport cycle
    • DOI 10.1016/j.molcel.2003.08.004
    • Chen, J., G. Lu, J. Lin, A.L. Davidson, and F.A. Quiocho. 2003. A tweezers-like motion of the ATP-binding cassette dimer in an ABC transport cycle. Mol. Cell. 12:651-661. doi:10.1016/j.molcel.2003.08.004 (Pubitemid 37222486)
    • (2003) Molecular Cell , vol.12 , Issue.3 , pp. 651-661
    • Chen, J.1    Lu, G.2    Lin, J.3    Davidson, A.L.4    Quiocho, F.A.5
  • 8
    • 0001774017 scopus 로고
    • Fitting and statistical analysis of single-channel records
    • B. Sakmann and E. Neher, editors. Plenum Press, New York
    • Colquhoun, D., and FJ. Sigworth. 1995. Fitting and statistical analysis of single-channel records. In Single channel recording. B. Sakmann and E. Neher, editors. Plenum Press, New York. 483-587.
    • (1995) Single Channel Recording , pp. 483-587
    • Colquhoun, D.1    Sigworth, F.J.2
  • 9
    • 67749084300 scopus 로고    scopus 로고
    • Application of rate-equilibrium free energy relationship analysis to nonequilibrium ion channel gating mechanisms
    • doi:10.1085/jgp.200910268
    • Csanády, L. 2009. Application of rate-equilibrium free energy relationship analysis to nonequilibrium ion channel gating mechanisms. J. Gen. Physiol. 134:129-136. doi:10.1085/jgp.200910268
    • (2009) J. Gen. Physiol. , vol.134 , pp. 129-136
    • Csanády, L.1
  • 10
    • 0033817333 scopus 로고    scopus 로고
    • Severed channels probe regulation of gating of cystic fibrosis transmembrane conductance regulator by its cytoplasmic domains
    • doi:10.1085/jgp.116.3.477
    • Csanády, L., K.W. Chan, D. Seto-Young, D.C. Kopsco, A.C. Nairn, and D.C. Gadsby. 2000. Severed channels probe regulation of gating of cystic fibrosis transmembrane conductance regulator by its cytoplasmic domains. J. Gen. Physiol. 116:477-500. doi:10.1085/jgp.116.3.477
    • (2000) J. Gen. Physiol. , vol.116 , pp. 477-500
    • Csanády, L.1    Chan, K.W.2    Seto-Young, D.3    Kopsco, D.C.4    Nairn, A.C.5    Gadsby, D.C.6
  • 11
    • 33750499982 scopus 로고    scopus 로고
    • Thermodynamics of CFTR channel gating: A spreading conformational change initiates an irreversible gating cycle
    • DOI 10.1085/jgp.200609558
    • Csanády, L., A.C. Nairn, and D.C. Gadsby. 2006. Thermodynamics of CFTR channel gating: a spreading conformational change initiates an irreversible gating cycle. J. Gen. Physiol. 128:523-533. doi:10.1085/jgp.200609558 (Pubitemid 44664630)
    • (2006) Journal of General Physiology , vol.128 , Issue.5 , pp. 523-533
    • Csanady, L.1    Nairn, A.C.2    Gadsby, D.C.3
  • 12
    • 75749153312 scopus 로고    scopus 로고
    • - ion pore revealed by distributions of open channel burst durations
    • doi:10.1073/pnas.0911061107
    • - ion pore revealed by distributions of open channel burst durations. Proc. Natl. Acad. Sci. USA. 107:1241-1246. doi:10.1073/pnas.0911061107
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 1241-1246
    • Csanády, L.1    Vergani, P.2    Gadsby, D.C.3
  • 13
    • 33645307384 scopus 로고    scopus 로고
    • The ABC protein turned chloride channel whose failure causes cystic fibrosis
    • doi:10.1038/nature04712
    • Gadsby, D.C., P. Vergani, and L. Csanády. 2006. The ABC protein turned chloride channel whose failure causes cystic fibrosis. Nature. 440:477-483. doi:10.1038/nature04712
    • (2006) Nature , vol.440 , pp. 477-483
    • Gadsby, D.C.1    Vergani, P.2    Csanády, L.3
  • 14
    • 0035801375 scopus 로고    scopus 로고
    • Structure of the ABC ATPase domain of human TAP1, the transporter associated with antigen processing
    • DOI 10.1093/emboj/20.17.4964
    • Gaudet, R., and D.C. Wiley. 2001. Structure of the ABC ATPase domain of human TAP1, the transporter associated with antigen processing. EMBO J. 20:4964-4972. doi:10.1093/emboj/20.17.4964 (Pubitemid 32848648)
    • (2001) EMBO Journal , vol.20 , Issue.17 , pp. 4964-4972
    • Gaudet, R.1    Wiley, D.C.2
  • 15
    • 0033933777 scopus 로고    scopus 로고
    • Inhibition of cystic fibrosis transmembrane conductance regulator by novel interaction with the metabolic sensor AMP-activated protein kinase
    • doi:10.1172/JCI9622
    • Hallows, K.R., V. Raghuram, B.E. Kemp, L.A. Witters, and J.K. Foskett. 2000. Inhibition of cystic fibrosis transmembrane conductance regulator by novel interaction with the metabolic sensor AMP-activated protein kinase. J. Clin. Invest. 105:1711-1721. doi:10.1172/JCI9622
    • (2000) J. Clin. Invest. , vol.105 , pp. 1711-1721
    • Hallows, K.R.1    Raghuram, V.2    Kemp, B.E.3    Witters, L.A.4    Foskett, J.K.5
  • 16
    • 34548853133 scopus 로고    scopus 로고
    • Structure and mechanism of ABC transporter proteins
    • DOI 10.1016/j.sbi.2007.07.003, PII S0959440X07001029
    • Hollenstein, K., R.J. Dawson, and K.P. Locher. 2007. Structure and mechanism of ABC transporter proteins. Curr. Opin. Struct. Biol. 17:412-418. doi:10.1016/j.sbi.2007.07.003 (Pubitemid 47451766)
    • (2007) Current Opinion in Structural Biology , vol.17 , Issue.4 , pp. 412-418
    • Hollenstein, K.1    Dawson, R.J.2    Locher, K.P.3
  • 17
    • 0034705293 scopus 로고    scopus 로고
    • Structural biology of Rad50 ATPase: ATP-driven conformational control in DNA double-strand break repair and the ABC-ATPase superfamily
    • doi:10.1016/S0092-8674(00)80890-9
    • Hopfner, K.P., A. Karcher, D.S. Shin, L. Craig, L.M. Arthur, J.P. Carney, andJ.A. Tainer. 2000. Structural biology of Rad50 ATPase: ATP-driven conformational control in DNA double-strand break repair and the ABC-ATPase superfamily. Cell. 101:789-800. doi:10.1016/S0092-8674(00)80890-9
    • (2000) Cell , vol.101 , pp. 789-800
    • Hopfner, K.P.1    Karcher, A.2    Shin, D.S.3    Craig, L.4    Arthur, L.M.5    Carney, J.P.6    Tainer, J.A.7
  • 18
    • 0032542358 scopus 로고    scopus 로고
    • Crystal structure of the ATP-binding subunit of an ABC transporter
    • DOI 10.1038/25393
    • Hung, L.W., I.X. Wang, K. Nikaido, P.Q. Liu, G.F. Ames, and S.H. Kim. 1998. Crystal structure of the ATP-binding subunit of an ABC transporter. Nature. 396:703-707. doi:10.1038/25393 (Pubitemid 29003952)
    • (1998) Nature , vol.396 , Issue.6712 , pp. 703-707
    • Hung, L.-W.1    Wang, I.X.2    Nikaido, K.3    Liu, P.-Q.4    Ames, G.F.-L.5    Kim, S.-H.6
  • 19
    • 0034941969 scopus 로고    scopus 로고
    • Crystal structures of the MJ1267 ATP binding cassette reveal an induced-fit effect at the ATPase active site of an ABC transporter
    • DOI 10.1016/S0969-2126(01)00617-7, PII S0969212601006177
    • Karpowich, N., O. Martsinkevich, L. Millen, Y.R. Yuan, P.L. Dai, K. MacVey, P.J. Thomas, and J.F. Hunt. 2001. Crystal structures of the MJ1267 ATP binding cassette reveal an induced-fit effect at the ATPase active site of an ABC transporter. Structure. 9:571-586. doi:10.1016/S0969-2126(01)00617-7 (Pubitemid 32695582)
    • (2001) Structure , vol.9 , Issue.7 , pp. 571-586
    • Karpowich, N.1    Martsinkevich, O.2    Millen, L.3    Yuan, Y.-R.4    Dai, P.L.5    MacVey, K.6    Thomas, P.J.7    Hunt, J.F.8
  • 21
    • 0033520934 scopus 로고    scopus 로고
    • Large scale purification of detergent-soluble Pglycoprotein from Pichia pastoris cells and characterization of nucleotide binding properties of wild-type, Walker A, and Walker B mutant proteins
    • doi:10.1074/jbc.274.49.34711
    • Lerner-Marmarosh, N., K. Gimi, I.L. Urbatsch, P. Gros, and A.E. Senior. 1999. Large scale purification of detergent-soluble Pglycoprotein from Pichia pastoris cells and characterization of nucleotide binding properties of wild-type, Walker A, and Walker B mutant proteins. J. Biol. Chem. 274:34711-34718. doi:10.1074/jbc.274.49.34711
    • (1999) J. Biol. Chem. , vol.274 , pp. 34711-34718
    • Lerner-Marmarosh, N.1    Gimi, K.2    Urbatsch, I.L.3    Gros, P.4    Senior, A.E.5
  • 22
    • 0033536602 scopus 로고    scopus 로고
    • Evolutionarily conserved pathways of energetic connectivity in protein families
    • DOI 10.1126/science.286.5438.295
    • Lockless, S.W., and R. Ranganathan. 1999. Evolutionarily conserved pathways of energetic connectivity in protein families. Science. 286:295-299. doi:10.1126/science.286.5438.295 (Pubitemid 29484693)
    • (1999) Science , vol.286 , Issue.5438 , pp. 295-299
    • Lockless, S.W.1    Ranganathan, R.2
  • 23
    • 50249090046 scopus 로고    scopus 로고
    • Atomic model of human cystic fibrosis transmembrane conductance regulator: Membrane-spanning domains and coupling interfaces
    • doi:10.1007/s00018-008-8249-1
    • Mornon, J.P., P. Lehn, and I. Callebaut. 2008. Atomic model of human cystic fibrosis transmembrane conductance regulator: membrane-spanning domains and coupling interfaces. Cell. Mol. Life Sci. 65:2594-2612. doi:10.1007/s00018- 008-8249-1
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 2594-2612
    • Mornon, J.P.1    Lehn, P.2    Callebaut, I.3
  • 24
    • 21744431708 scopus 로고    scopus 로고
    • Functional interactions between nucleotide binding domains and leukotriene C4 binding sites of multidrug resistance protein 1 (ABCC1)
    • doi:10.1124/ mol.104.007708
    • Payen, L., M. Gao, C. Westlake, A. Theis, S.P.C. Cole, and R.G. Deeley. 2005. Functional interactions between nucleotide binding domains and leukotriene C4 binding sites of multidrug resistance protein 1 (ABCC1). Mol. Pharmacol. 67:1944-1953. doi:10.1124/ mol.104.007708
    • (2005) Mol. Pharmacol. , vol.67 , pp. 1944-1953
    • Payen, L.1    Gao, M.2    Westlake, C.3    Theis, A.4    Cole, S.P.C.5    Deeley, R.G.6
  • 25
    • 0026681083 scopus 로고
    • Phosphorylation of the cystic fibrosis transmembrane conductance regulator
    • Picciotto, M.R., J.A. Cohn, G. Bertuzzi, P. Greengard, and A.C. Nairn. 1992. Phosphorylation of the cystic fibrosis transmembrane conductance regulator. J. Biol. Chem. 267:12742-12752.
    • (1992) J. Biol. Chem. , vol.267 , pp. 12742-12752
    • Picciotto, M.R.1    Cohn, J.A.2    Bertuzzi, G.3    Greengard, P.4    Nairn, A.C.5
  • 26
    • 33845563818 scopus 로고    scopus 로고
    • Thermodynamics of the ATPase cycle of GlcV, the nucleotide-binding domain of the glucose ABC transporter of Sulfolobus solfataricus
    • DOI 10.1021/bi061230e
    • Pretz, M.G., S.V. Albers, G. Schuurman-Wolters, R. Tampé, A.J. Driessen, and C. van der Does. 2006. Thermodynamics of the ATPase cycle of GlcV, the nucleotide-binding domain of the glucose ABC transporter of sulfolobus solfataricus. Biochemistry. 45:15056-15067. doi:10.1021/bi061230e (Pubitemid 44937018)
    • (2006) Biochemistry , vol.45 , Issue.50 , pp. 15056-15067
    • Pretz, M.G.1    Albers, S.-V.2    Schuurman-Wolters, G.3    Tampe, R.4    Driessen, A.J.M.5    Van Der Does, C.6
  • 27
    • 33749076230 scopus 로고    scopus 로고
    • Distinct structural and functional properties of the ATPase sites in an asymmetric ABC transporter
    • doi:10.1016/ j.molcel.2006.07.034
    • Procko, E., I. Ferrin-O'Connell, S.L. Ng, and R. Gaudet. 2006. Distinct structural and functional properties of the ATPase sites in an asymmetric ABC transporter. Mol. Cell. 24:51-62. doi:10.1016/j.molcel.2006.07.034
    • (2006) Mol. Cell. , vol.24 , pp. 51-62
    • Procko, E.1    Ferrin-O'Connell, I.2    Ng, S.L.3    Gaudet, R.4
  • 28
    • 0033514315 scopus 로고    scopus 로고
    • Walker mutations reveal loose relationship between catalytic and channel-gating activities of purified CFTR (cystic fibrosis transmembrane conductance regulator)
    • DOI 10.1021/bi982243y
    • Ramjeesingh, M., C. Li, E. Garami, L.J. Huan, K. Galley, Y. Wang, and C.E. Bear. 1999. Walker mutations reveal loose relationship between catalytic and channel-gating activities of purified CFTR (cystic fibrosis transmembrane conductance regulator). Biochemistry. 38:1463-1468. doi:10.1021/bi982243y (Pubitemid 29070440)
    • (1999) Biochemistry , vol.38 , Issue.5 , pp. 1463-1468
    • Ramjeesingh, M.1    Li, C.2    Garami, E.3    Huan, L.-J.4    Galley, K.5    Wang, Y.6    Bear, C.E.7
  • 31
    • 0036342413 scopus 로고    scopus 로고
    • ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer
    • DOI 10.1016/S1097-2765(02)00576-2
    • Smith, P.C., N. Karpowich, L. Millen, J.E. Moody, J. Rosen, P.J. Thomas, and J.F. Hunt. 2002. ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer. Mol. Cell. 10:139-149. doi:10.1016/S1097-2765(02)00576-2 (Pubitemid 34876568)
    • (2002) Molecular Cell , vol.10 , Issue.1 , pp. 139-149
    • Smith, P.C.1    Karpowich, N.2    Millen, L.3    Moody, J.E.4    Rosen, J.5    Thomas, P.J.6    Hunt, J.F.7
  • 32
    • 0025885376 scopus 로고
    • - channel in CHO cells stably expressing the cystic fibrosis gene
    • doi:10.1038/ 352628a0
    • - channel in CHO cells stably expressing the cystic fibrosis gene. Nature. 352:628-631. doi:10.1038/ 352628a0
    • (1991) Nature , vol.352 , pp. 628-631
    • Tabcharani, J.A.1    Chang, X.B.2    Riordan, J.R.3    Hanrahan, J.W.4
  • 33
    • 64549132504 scopus 로고    scopus 로고
    • State-dependent modulation of CFTR gating by pyrophosphate
    • doi:10.1085/jgp.200810186
    • Tsai, M.F., H. Shimizu, Y. Sohma, M. Li, and T.C. Hwang. 2009. State-dependent modulation of CFTR gating by pyrophosphate. J. Gen. Physiol. 133:405-419. doi:10.1085/jgp.200810186
    • (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
  • 34
    • 0034601811 scopus 로고    scopus 로고
    • Investigation of the role of glutamine-471 and glutamine-1114 in the two catalytic sites of P-glycoprotein
    • doi:10.1021/bi001220s
    • Urbatsch, I.L., K. Gimi, S. Wilke-Mounts, and A.E. Senior. 2000. Investigation of the role of glutamine-471 and glutamine-1114 in the two catalytic sites of P-glycoprotein. Biochemistry. 39:11921-11927. doi:10.1021/bi001220s
    • (2000) Biochemistry , vol.39 , pp. 11921-11927
    • Urbatsch, I.L.1    Gimi, K.2    Wilke-Mounts, S.3    Senior, A.E.4
  • 35
    • 0028276430 scopus 로고
    • ATP alters current fluctuations of cystic fibrosis transmembrane conductance regulator: Evidence for a three-state activation mechanism
    • DOI 10.1085/jgp.104.1.123
    • Venglarik, C.J., B.D. Schultz, R.A. Frizzell, and R.J. Bridges. 1994. ATP alters current fluctuations of cystic fibrosis transmembrane conductance regulator: evidence for a three-state activation mechanism. J. Gen. Physiol. 104:123-146. doi:10.1085/jgp.104.1.123 (Pubitemid 24226327)
    • (1994) Journal of General Physiology , vol.104 , Issue.1 , pp. 123-146
    • Venglarik, C.J.1    Schultz, B.D.2    Frizzell, R.A.3    Bridges, R.J.4
  • 37
    • 14544300522 scopus 로고    scopus 로고
    • CFTR channel opening by ATP-driven tight dimerization of its nucleotide-binding domains
    • doi:10.1038/ nature03313
    • Vergani, P., S.W. Lockless, A.C. Nairn, and D.C. Gadsby. 2005. CFTR channel opening by ATP-driven tight dimerization of its nucleotide-binding domains. Nature. 433:876-880. doi:10.1038/ nature03313
    • (2005) Nature , vol.433 , pp. 876-880
    • Vergani, P.1    Lockless, S.W.2    Nairn, A.C.3    Gadsby, D.C.4
  • 38
    • 0001607723 scopus 로고
    • Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker, J.E., M. Saraste, M.J. Runswick, and N.J. Gay. 1982. Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J. 1:945-951.
    • (1982) EMBO J , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 39
    • 0033000414 scopus 로고    scopus 로고
    • Dual effects of ADP and adenylylimidodiphosphate on CFTR channel kinetics show binding to two different nucleotide binding sites
    • DOI 10.1085/jgp.114.1.55
    • Weinreich, F., J.R. Riordan, and G. Nagel. 1999. Dual effects of ADP and adenylylimidodiphosphate on CFTR channel kinetics show binding to two different nucleotide binding sites. J. Gen. Physiol. 114:55-70. doi:10.1085/jgp.114.1.55 (Pubitemid 29323755)
    • (1999) Journal of General Physiology , vol.114 , Issue.1 , pp. 55-70
    • Weinreich, F.1    Riordan, J.R.2    Nagel, G.3
  • 40
    • 0028265949 scopus 로고
    • - channels: A kinetic analysis of channel regulation
    • doi:10.1016/S0006-3495(94)80930-0
    • - channels: a kinetic analysis of channel regulation. Biophys. J. 66:1398-1403. doi:10.1016/S0006-3495(94)80930-0
    • (1994) Biophys. J. , vol.66 , pp. 1398-1403
    • Winter, M.C.1    Sheppard, D.N.2    Carson, M.R.3    Welsh, M.J.4
  • 41
    • 0035943735 scopus 로고    scopus 로고
    • The crystal structure of the MJ0796 ATP-binding cassette. Implications for the structural consequences of ATP hydrolysis in the active site of an ABC transporter
    • doi:10.1074/jbc.M100758200
    • Yuan, Y.R., S. Blecker, O. Martsinkevich, L. Millen, P.J. Thomas, and J.F. Hunt. 2001. The crystal structure of the MJ0796 ATP-binding cassette. Implications for the structural consequences of ATP hydrolysis in the active site of an ABC transporter. J. Biol. Chem. 276:32313-32321. doi:10.1074/jbc. M100758200
    • (2001) J. Biol. Chem. , vol.276 , pp. 32313-32321
    • Yuan, Y.R.1    Blecker, S.2    Martsinkevich, O.3    Millen, L.4    Thomas, P.J.5    Hunt, J.F.6
  • 42
    • 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
    • DOI 10.1085/jgp.113.4.541
    • Zeltwanger, S., F. Wang, G.T. Wang, K.D. Gillis, and T.C. Hwang. 1999. 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. doi:10.1085/jgp.113.4.541 (Pubitemid 29169621)
    • (1999) Journal of General Physiology , vol.113 , Issue.4 , pp. 541-554
    • Zeltwanger, S.1    Wang, F.2    Wang, G.-T.3    Gillis, K.D.4    Hwang, T.-C.5


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