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Volumn 3, Issue 3, 2013, Pages

Dynamics intrinsic to cystic fibrosis transmembrane conductance regulator function and stability

Author keywords

[No Author keywords available]

Indexed keywords

CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR;

EID: 84882242517     PISSN: None     EISSN: 21571422     Source Type: Journal    
DOI: 10.1101/cshperspect.a009522     Document Type: Article
Times cited : (25)

References (85)
  • 3
    • 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
    • Alexander C., Ivetac A, Liu X, Norimatsu Y, Serrano JR, Landstrom A., Sansom M, Dawson DC. 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    Sansom, M.7    Dawson, D.C.8
  • 6
    • 27844520938 scopus 로고    scopus 로고
    • Crystallographic and single-particle analyses of native-and nucleotide-bound forms of the cystic fibrosis transmembrane conductance regulator (CFTR) protein
    • Awayn N.H., Rosenberg MF, Kamis AB, Aleksandrov LA, Riordan J.R., Ford RC. 2005. Crystallographic and single-particle analyses of native-and nucleotide-bound forms of the cystic fibrosis transmembrane conductance regulator (CFTR) protein. Biochem Soc Trans 33: 996-999.
    • (2005) Biochem Soc Trans , vol.33 , pp. 996-999
    • Awayn, N.H.1    Rosenberg, M.F.2    Kamis, A.B.3    Aleksandrov, L.A.4    Riordan, J.R.5    Ford, R.C.6
  • 8
    • 0035910510 scopus 로고    scopus 로고
    • Cystic fibrosis transmembrane conductance regulator Cl-channels with R domain deletions and translocations show phosphorylation-dependent and-independent activity
    • Baldursson O., Ostedgaard LS, Rokhlina T, Cotten JF, Welsh MJ. 2001. Cystic fibrosis transmembrane conductance regulator Cl-channels with R domain deletions and translocations show phosphorylation-dependent and-independent activity. J Biol Chem 276: 1904-1910.
    • (2001) J Biol Chem , vol.276 , pp. 1904-1910
    • Baldursson, O.1    Ostedgaard, L.S.2    Rokhlina, T.3    Cotten, J.F.4    Welsh, M.J.5
  • 9
    • 0027519153 scopus 로고
    • Regulation of the cystic fibrosis transmembrane conductance regulator Cl-channel by specific protein kinases and protein phosphatases
    • Berger H.A., Travis SM, Welsh MJ. 1993. Regulation of the cystic fibrosis transmembrane conductance regulator Cl-channel by specific protein kinases and protein phosphatases. J Biol Chem 268: 2037-2047.
    • (1993) J Biol Chem , vol.268 , pp. 2037-2047
    • Berger, H.A.1    Travis, S.M.2    Welsh, M.J.3
  • 11
    • 0027311276 scopus 로고
    • Protein kinase A (PKA) still activates CFTR chloride channel after mutagenesis of all 10 PKA consensus phosphorylation sites
    • Chang X.B., Tabcharani JA, Hou YX, Jensen TJ, Kartner N, Alon N., Hanrahan JW, Riordan JR. 1993. Protein kinase A (PKA) still activates CFTR chloride channel after mutagenesis of all 10 PKA consensus phosphorylation sites. J Biol Chem 268: 11304-11311.
    • (1993) J Biol Chem , vol.268 , pp. 11304-11311
    • Chang, X.B.1    Tabcharani, J.A.2    Hou, Y.X.3    Jensen, T.J.4    Kartner, N.5    Alon, N.6    Hanrahan, J.W.7    Riordan, J.R.8
  • 14
    • 0025987020 scopus 로고
    • Phosphorylation of the R domain by cAMP-dependent protein kinase regulates the CFTR chloride channel
    • Cheng S.H., Rich DP, Marshall J, Gregory RJ, Welsh MJ, Smith AE. 1991. Phosphorylation of the R domain by cAMP-dependent protein kinase regulates the CFTR chloride channel. Cell 66: 1027-1036.
    • (1991) Cell , vol.66 , pp. 1027-1036
    • Cheng, S.H.1    Rich, D.P.2    Marshall, J.3    Gregory, R.J.4    Welsh, M.J.5    Smith, A.E.6
  • 16
    • 84885680173 scopus 로고    scopus 로고
    • Alteration of CFTRNBD1 dynamics upon deletion of F508 underlying the basic defect
    • Chong P.A., Forman-Kay JD. 2010. Alteration of CFTRNBD1 dynamics upon deletion of F508 underlying the basic defect. Pediatr Pulmonol 45 (Suppl): 240.
    • (2010) Pediatr Pulmonol , vol.45 , Issue.SUPPL. , pp. 240
    • Chong, P.A.1    Forman-Kay, J.D.2
  • 17
    • 12344263101 scopus 로고    scopus 로고
    • Functional roles of nonconserved structural segments in CFTR's NH2-terminal nucleotide binding domain
    • Csanady L., Chan KW, Nairn AC, Gadsby DC. 2005. Functional roles of nonconserved structural segments in CFTR's NH2-terminal nucleotide binding domain. J Gen Physiol 125: 43-55.
    • (2005) J Gen Physiol , vol.125 , pp. 43-55
    • Csanady, L.1    Chan, K.W.2    Nairn, A.C.3    Gadsby, D.C.4
  • 18
    • 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. 2009. 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 107: 1241-1246.
    • (2009) Proc Natl Acad Sci , vol.107 , pp. 1241-1246
    • Csanady, L.1    Vergani, P.2    Gadsby, D.C.3
  • 21
    • 33748644877 scopus 로고    scopus 로고
    • Structure of a bacterial multidrug ABC transporter
    • Dawson R.J., 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
  • 22
    • 0026781952 scopus 로고
    • Processing of mutant cystic fibrosis transmembrane conductance regulator is temperature-sensitive
    • Denning G.M., Anderson MP, Amara JF, Marshall J, Smith A.E., Welsh MJ. 1992. Processing of mutant cystic fibrosis transmembrane conductance regulator is temperature-sensitive. Nature 358: 761-764.
    • (1992) Nature , vol.358 , pp. 761-764
    • Denning, G.M.1    Anderson, M.P.2    Amara, J.F.3    Marshall, J.4    Smith, A.E.5    Welsh, M.J.6
  • 24
    • 11444266284 scopus 로고    scopus 로고
    • TheDF508 cystic fibrosis mutation impairs domain-domain interactions and arrests post-translational folding of CFTR
    • Du K., Sharma M, Lukacs GL. 2005. TheDF508 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
  • 25
    • 0028328645 scopus 로고
    • Phosphorylation by cAMP-dependent protein kinase causes a conformational change in the R domain of the cystic fibrosis transmembrane conductance regulator
    • Dulhanty A.M., Riordan JR. 1994. Phosphorylation by cAMP-dependent protein kinase causes a conformational change in the R domain of the cystic fibrosis transmembrane conductance regulator. Biochemistry 33: 4072-4079.
    • (1994) Biochemistry , vol.33 , pp. 4072-4079
    • Dulhanty, A.M.1    Riordan, J.R.2
  • 26
    • 27144464910 scopus 로고    scopus 로고
    • Flexible nets. The roles of intrinsic disorder in protein interaction networks
    • Dunker A.K., Cortese MS, Romero P, Iakoucheva LM, Uversky VN. 2005. Flexible nets. The roles of intrinsic disorder in protein interaction networks. FEBS J 272: 5129-5148.
    • (2005) FEBS J , vol.272 , pp. 5129-5148
    • Dunker, A.K.1    Cortese, M.S.2    Romero, P.3    Iakoucheva, L.M.4    Uversky, V.N.5
  • 27
    • 84885784960 scopus 로고    scopus 로고
    • Rescuing F508del-CFTR by genetic revertants, low temperature and small molecules
    • Farinha C.M., Da Paula A, Amaral MD. 2010. Rescuing F508del-CFTR by genetic revertants, low temperature and small molecules. Pediatr Pulmonol 45 (Suppl): 230.
    • (2010) Pediatr Pulmonol , vol.45 , Issue.SUPPL. , pp. 230
    • Farinha, C.M.1    da Paula, A.2    Amaral, M.D.3
  • 28
    • 44449124764 scopus 로고    scopus 로고
    • State-dependent access of anions to the cystic fibrosis transmembrane conductance regulator chloride channel pore
    • Fatehi M., Linsdell P. 2008. State-dependent access of anions to the cystic fibrosis transmembrane conductance regulator chloride channel pore. J Biol Chem 283: 6102-6109.
    • (2008) J Biol Chem , vol.283 , pp. 6102-6109
    • Fatehi, M.1    Linsdell, P.2
  • 29
    • 55549094466 scopus 로고    scopus 로고
    • Multiple membrane-cytoplasmic domain contacts in the cystic fibrosis transmembrane conductance regulator (CFTR) mediate regulation of channel gating
    • He L., Aleksandrov AA, Serohijos AW, Hegedus T, Aleksandrov LA, Cui L, Dokholyan NV, Riordan JR. 2008. Multiple membrane-cytoplasmic domain contacts in the cystic fibrosis transmembrane conductance regulator (CFTR) mediate regulation of channel gating. J Biol Chem 283: 26383-26390.
    • (2008) J Biol Chem , vol.283 , pp. 26383-26390
    • He, L.1    Aleksandrov, A.A.2    Serohijos, A.W.3    Hegedus, T.4    Aleksandrov, L.A.5    Cui, L.6    Dokholyan, N.V.7    Riordan, J.R.8
  • 30
    • 77954983869 scopus 로고    scopus 로고
    • Restoration of domain folding and interdomain assembly by second-site suppressors of the DF508 mutation in CFTR
    • He L., Aleksandrov LA, Cui L, Jensen TJ, Nesbitt KL, Riordan JR. 2010. Restoration of domain folding and interdomain assembly by second-site suppressors of the DF508 mutation in CFTR. FASEB J 24: 3103-3112.
    • (2010) FASEB J , vol.24 , pp. 3103-3112
    • He, L.1    Aleksandrov, L.A.2    Cui, L.3    Jensen, T.J.4    Nesbitt, K.L.5    Riordan, J.R.6
  • 31
    • 42649118768 scopus 로고    scopus 로고
    • Computational studies reveal phosphorylation-dependent changes in the unstructured R domain of CFTR
    • Hegedus T., Serohijos AW, Dokholyan NV, He L, Riordan JR. 2008. Computational studies reveal phosphorylation-dependent changes in the unstructured R domain of CFTR. J Mol Biol 378: 1052-1063.
    • (2008) J Mol Biol , vol.378 , pp. 1052-1063
    • Hegedus, T.1    Serohijos, A.W.2    Dokholyan, N.V.3    He, L.4    Riordan, J.R.5
  • 33
    • 33947154878 scopus 로고    scopus 로고
    • Structure of an ABC transporter in complex with its binding protein
    • Hollenstein K., Frei DC, Locher KP. 2007. Structure of an ABC transporter in complex with its binding protein. Nature 446: 213-216.
    • (2007) Nature , vol.446 , pp. 213-216
    • Hollenstein, K.1    Frei, D.C.2    Locher, K.P.3
  • 34
    • 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
    • Hopfner K.P., Karcher A, Shin DS, Craig L, Arthur LM, Carney J.P., Tainer JA. 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.
    • (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
  • 35
    • 61449145992 scopus 로고    scopus 로고
    • Molecular modeling of the heterodimer of human CFTR's nucleotide-binding domains using a protein-protein docking approach
    • Huang S.Y., Bolser D, Liu HY, Hwang TC, Zou X. 2009. Molecular modeling of the heterodimer of human CFTR's nucleotide-binding domains using a protein-protein docking approach. J Mol Graph Model 27: 822-828.
    • (2009) J Mol Graph Model , vol.27 , pp. 822-828
    • Huang, S.Y.1    Bolser, D.2    Liu, H.Y.3    Hwang, T.C.4    Zou, X.5
  • 36
    • 84865234037 scopus 로고    scopus 로고
    • Conformational changes relevant to channel activity and folding within the first nucleotide binding domain of the cystic fibrosis transmembrane conductance regulator
    • Hudson R.P., Chong PA, Protasevich II, Vernon R, Noy E, Bihler H., Li AJ, Kalid O, Sela-Culang I, Mense M, et al. 2012. Conformational changes relevant to channel activity and folding within the first nucleotide binding domain of the cystic fibrosis transmembrane conductance regulator. J Biol Chem 287: 28480-28494.
    • (2012) J Biol Chem , vol.287 , pp. 28480-28494
    • Hudson, R.P.1    Chong, P.A.2    Protasevich, I.I.3    Vernon, R.4    Noy, E.5    Bihler, H.6    Li, A.J.7    Kalid, O.8    Sela-Culang, I.9    Mense, M.10
  • 37
    • 0014029736 scopus 로고
    • Simple allosteric model for membrane pumps
    • Jardetzky O. 1966. Simple allosteric model for membrane pumps. Nature 211: 969-970.
    • (1966) Nature , vol.211 , pp. 969-970
    • Jardetzky, O.1
  • 38
    • 34547943910 scopus 로고    scopus 로고
    • Nucleotide-dependent allostery within the ABC transporter ATP-binding cassette: A computational study of the MJ0796 dimer
    • Jones P.M., George AM. 2007. Nucleotide-dependent allostery within the ABC transporter ATP-binding cassette: A computational study of the MJ0796 dimer. J Biol Chem 282: 22793-22803.
    • (2007) J Biol Chem , vol.282 , pp. 22793-22803
    • Jones, P.M.1    George, A.M.2
  • 39
    • 66149139241 scopus 로고    scopus 로고
    • Opening of the ADP-bound active site in the ABC transporterATPase dimer: Evidence for a constant contact, alternating sites model for the catalytic cycle
    • Jones P.M., George AM. 2009. Opening of the ADP-bound active site in the ABC transporterATPase dimer: Evidence for a constant contact, alternating sites model for the catalytic cycle. Proteins 75: 387-396.
    • (2009) Proteins , vol.75 , pp. 387-396
    • Jones, P.M.1    George, A.M.2
  • 40
    • 75649088951 scopus 로고    scopus 로고
    • NMR evidence for differential phosphorylation-dependent interactions in WTand DF508 CFTR
    • Kanelis V., Hudson RP, Thibodeau PH, Thomas PJ, Forman-Kay JD. 2010. NMR evidence for differential phosphorylation-dependent interactions in WTand DF508 CFTR. EMBO J 29: 263-277.
    • (2010) EMBO J , vol.29 , pp. 263-277
    • Kanelis, V.1    Hudson, R.P.2    Thibodeau, P.H.3    Thomas, P.J.4    Forman-Kay, J.D.5
  • 41
    • 79952653259 scopus 로고    scopus 로고
    • Liganddriven vectorial folding of ribosome-bound human CFTR NBD1
    • Khushoo A., Yang Z, Johnson AE, Skach WR. 2011. Liganddriven vectorial folding of ribosome-bound human CFTR NBD1. Mol Cell 41: 682-692.
    • (2011) Mol Cell , vol.41 , pp. 682-692
    • Khushoo, A.1    Yang, Z.2    Johnson, A.E.3    Skach, W.R.4
  • 46
    • 19944432524 scopus 로고    scopus 로고
    • Impact of the DF508 mutation in first nucleotide-binding domain of human cystic fibrosis transmembrane conductance regulator on domain folding and structure
    • Lewis H.A., Zhao X, Wang C, Sauder JM, Rooney I, Noland BW, Lorimer D, Kearins MC, Conners K, Condon B, et al. 2005. Impact of the DF508 mutation in first nucleotide-binding domain of human cystic fibrosis transmembrane conductance regulator on domain folding and structure. J Biol Chem 280: 1346-1353.
    • (2005) J Biol Chem , vol.280 , pp. 1346-1353
    • Lewis, H.A.1    Zhao, X.2    Wang, C.3    Sauder, J.M.4    Rooney, I.5    Noland, B.W.6    Lorimer, D.7    Kearins, M.C.8    Conners, K.9    Condon, B.10
  • 48
    • 77955025743 scopus 로고    scopus 로고
    • The V510D suppressor mutation stabilizes DF508-CFTR at the cell surface
    • Loo T.W., Bartlett MC, Clarke DM. 2010. The V510D suppressor mutation stabilizes DF508-CFTR at the cell surface. Biochemistry 49: 6352-6357.
    • (2010) Biochemistry , vol.49 , pp. 6352-6357
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 49
    • 0028559511 scopus 로고
    • Conformational maturation of CFTR but not its mutant counterpart (DF508) occurs in the endoplasmic reticulum and requires ATP
    • Lukacs G.L., Mohamed A, Kartner N, Chang XB, Riordan JR, Grinstein S. 1994. Conformational maturation of CFTR but not its mutant counterpart (DF508) occurs in the endoplasmic reticulum and requires ATP. EMBO J 13: 6076-6086.
    • (1994) EMBO J , vol.13 , pp. 6076-6086
    • Lukacs, G.L.1    Mohamed, A.2    Kartner, N.3    Chang, X.B.4    Riordan, J.R.5    Grinstein, S.6
  • 50
    • 0001398337 scopus 로고
    • A general theory of membrane transport from studies of bacteria
    • Mitchell P. 1957. A general theory of membrane transport from studies of bacteria. Nature 180: 134-136.
    • (1957) Nature , vol.180 , pp. 134-136
    • Mitchell, P.1
  • 51
    • 76449098928 scopus 로고    scopus 로고
    • Model of the cAMP activation of chloride transport by CFTR channel and the mechanism of potentiators
    • Moran O. 2010. Model of the cAMP activation of chloride transport by CFTR channel and the mechanism of potentiators. J Theor Biol 262: 73-79.
    • (2010) J Theor Biol , vol.262 , pp. 73-79
    • Moran, O.1
  • 52
    • 50249090046 scopus 로고    scopus 로고
    • Atomic model of human cystic fibrosis transmembrane conductance regulator: Membrane-spanning domains and coupling interfaces
    • 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
  • 53
    • 70349847830 scopus 로고    scopus 로고
    • Molecular models of the open and closed states of the whole human CFTR protein
    • Mornon J.P., 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
  • 54
    • 0034625153 scopus 로고    scopus 로고
    • A functional R domain from cystic fibrosis transmembrane conductance regulator is predominantly unstructured in solution
    • Ostedgaard L.S., Baldursson O, Vermeer DW, Welsh MJ, Robertson AD. 2000. A functional R domain from cystic fibrosis transmembrane conductance regulator is predominantly unstructured in solution. Proc Natl Acad Sci 97: 5657-5662.
    • (2000) Proc Natl Acad Sci , vol.97 , pp. 5657-5662
    • Ostedgaard, L.S.1    Baldursson, O.2    Vermeer, D.W.3    Welsh, M.J.4    Robertson, A.D.5
  • 55
    • 0026681083 scopus 로고
    • Phosphorylation of the cystic fibrosis transmembrane conductance regulator
    • Picciotto M.R., Cohn JA, Bertuzzi G, Greengard P, Nairn AC. 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
  • 56
    • 33846601303 scopus 로고    scopus 로고
    • An inward-facing conformation of a putative metal-chelatetype ABC transporter
    • Pinkett H.W., Lee AT, Lum P, Locher KP, Rees DC. 2007. An inward-facing conformation of a putative metal-chelatetype ABC transporter. Science 315: 373-377.
    • (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
  • 57
    • 77957302946 scopus 로고    scopus 로고
    • Thermal unfolding studies show the disease causing F508del mutation in CFTR thermodynamically destabilizes nucleotide-binding domain 1
    • Protasevich I., Yang Z, Wang C, Atwell S, Zhao X, Emtage S, Wetmore D., Hunt JF, Brouillette CG. 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    Wetmore, D.7    Hunt, J.F.8    Brouillette, C.G.9
  • 58
    • 0031006695 scopus 로고    scopus 로고
    • Localization and suppression of a kinetic defect in cystic fibrosis transmembrane conductance regulator folding
    • Qu B.H., Strickland EH, Thomas PJ. 1997. Localization and suppression of a kinetic defect in cystic fibrosis transmembrane conductance regulator folding. J Biol Chem 272: 15739-15744.
    • (1997) J Biol Chem , vol.272 , pp. 15739-15744
    • Qu, B.H.1    Strickland, E.H.2    Thomas, P.J.3
  • 60
    • 0027171978 scopus 로고
    • Regulation of the cystic fibrosis transmembrane conductance regulator Cl-channel by negative charge in the R domain
    • Rich D.P., Berger HA, Cheng SH, Travis SM, Saxena M, Smith A.E., Welsh MJ. 1993. Regulation of the cystic fibrosis transmembrane conductance regulator Cl-channel by negative charge in the R domain. J Biol Chem 268: 20259-20267.
    • (1993) J Biol Chem , vol.268 , pp. 20259-20267
    • Rich, D.P.1    Berger, H.A.2    Cheng, S.H.3    Travis, S.M.4    Saxena, M.5    Smith, A.E.6    Welsh, M.J.7
  • 61
    • 77957320095 scopus 로고    scopus 로고
    • Identification of a non-native state of NBD1 that is affected by DF508
    • Richardson J.M., Thibodeau PH, Watson J, Thomas PJ. 2007. Identification of a non-native state of NBD1 that is affected by DF508. Pediatr Pulmonol 45 (Suppl): 203.
    • (2007) Pediatr Pulmonol , vol.45 , Issue.SUPPL. , pp. 203
    • Richardson, J.M.1    Thibodeau, P.H.2    Watson, J.3    Thomas, P.J.4
  • 63
    • 4544378176 scopus 로고    scopus 로고
    • Purification and crystallization of the cystic fibrosis transmembrane conductance regulator (CFTR)
    • Rosenberg M.F., Kamis AB, Aleksandrov LA, Ford RC, Riordan JR. 2004. Purification and crystallization of the cystic fibrosis transmembrane conductance regulator (CFTR). J Biol Chem 279: 39051-39057.
    • (2004) J Biol Chem , vol.279 , pp. 39051-39057
    • Rosenberg, M.F.1    Kamis, A.B.2    Aleksandrov, L.A.3    Ford, R.C.4    Riordan, J.R.5
  • 64
    • 42149120706 scopus 로고    scopus 로고
    • Phenylalanine-508 mediates a cytoplasmic-membrane domain contact in the CFTR 3D structure crucial to assembly and channel function
    • Serohijos A.W., Hegedus T, Aleksandrov AA, He L, Cui L, Dokholyan N.V., Riordan JR. 2008a. Phenylalanine-508 mediates a cytoplasmic-membrane domain contact in the CFTR 3D structure crucial to assembly and channel function. Proc Natl Acad Sci 105: 3256-3261.
    • (2008) Proc Natl Acad Sci , 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    Riordan, J.R.7
  • 65
    • 40149102264 scopus 로고    scopus 로고
    • Diminished self-chaperoning activity of the DF508 mutant of CFTR results in protein misfolding
    • Serohijos A.W., Hegedus T, Riordan JR, Dokholyan NV. 2008b. Diminished self-chaperoning activity of the DF508 mutant of CFTR results in protein misfolding. PLoS Comput Biol 4: e1000008.
    • (2008) PLoS Comput Biol , vol.4
    • Serohijos, A.W.1    Hegedus, T.2    Riordan, J.R.3    Dokholyan, N.V.4
  • 66
    • 0036342413 scopus 로고    scopus 로고
    • ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer
    • Smith P.C., Karpowich N, Millen L, Moody JE, Rosen J, Thomas P.J., Hunt JF. 2002. ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer. Mol Cell 10: 139-149.
    • (2002) Mol Cell , vol.10 , 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
  • 67
    • 0027153083 scopus 로고
    • Identification of revertants for the cystic fibrosis DF508 mutation using STE6-CFTR chimeras in yeast
    • Teem J.L., Berger HA, Ostedgaard LS, Rich DP, Tsui LC, Welsh MJ. 1993. Identification of revertants for the cystic fibrosis DF508 mutation using STE6-CFTR chimeras in yeast. Cell 73: 335-346.
    • (1993) Cell , vol.73 , pp. 335-346
    • Teem, J.L.1    Berger, H.A.2    Ostedgaard, L.S.3    Rich, D.P.4    Tsui, L.C.5    Welsh, M.J.6
  • 68
    • 0029864612 scopus 로고    scopus 로고
    • Mutation of R555 in CFTR-DF508 enhances function and partially corrects defective processing
    • Teem J.L., Carson MR, Welsh MJ. 1996. Mutation of R555 in CFTR-DF508 enhances function and partially corrects defective processing. Receptors Channels 4: 63-72.
    • (1996) Receptors Channels , vol.4 , pp. 63-72
    • Teem, J.L.1    Carson, M.R.2    Welsh, M.J.3
  • 71
    • 0025906334 scopus 로고
    • Cystic fibrosis transmembrane conductance regulator: Nucleotide binding to a synthetic peptide
    • Thomas P.J., Shenbagamurthi P, Ysern X, Pedersen PL. 1991. Cystic fibrosis transmembrane conductance regulator: Nucleotide binding to a synthetic peptide. Science 251: 555-557.
    • (1991) Science , vol.251 , pp. 555-557
    • Thomas, P.J.1    Shenbagamurthi, P.2    Ysern, X.3    Pedersen, P.L.4
  • 72
    • 0029838141 scopus 로고    scopus 로고
    • Identification of protein kinase A phosphorylation sites on NBD1 and R domains of CFTR using electrospray mass spectrometry with selective phosphate ion monitoring
    • Townsend R.R., Lipniunas PH, Tulk BM, Verkman AS. 1996. Identification of protein kinase A phosphorylation sites on NBD1 and R domains of CFTR using electrospray mass spectrometry with selective phosphate ion monitoring. Protein Sci 5: 1865-1873.
    • (1996) Protein Sci , vol.5 , pp. 1865-1873
    • Townsend, R.R.1    Lipniunas, P.H.2    Tulk, B.M.3    Verkman, A.S.4
  • 74
    • 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. 2007. 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) J Biol Chem , vol.282 , pp. 4533-4544
    • Wang, W.1    Bernard, K.2    Li, G.3    Kirk, K.L.4
  • 77
    • 0028006681 scopus 로고
    • Intracellular turnover of cystic fibrosis transmembrane conductance regulator. Inefficient processing and rapid degradation of wild-type and mutant proteins
    • Ward C.L., Kopito RR. 1994. Intracellular turnover of cystic fibrosis transmembrane conductance regulator. Inefficient processing and rapid degradation of wild-type and mutant proteins. J Biol Chem 269: 25710-25718.
    • (1994) J Biol Chem , vol.269 , pp. 25710-25718
    • Ward, C.L.1    Kopito, R.R.2
  • 78
    • 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. 2007. Flexibility in the ABC transporter MsbA: Alternating access with a twist. Proc Natl Acad Sci 104: 19005-19010.
    • (2007) Proc Natl Acad Sci , vol.104 , pp. 19005-19010
    • Ward, A.1    Reyes, C.L.2    Yu, J.3    Roth, C.B.4    Chang, G.5
  • 79
    • 46749137537 scopus 로고    scopus 로고
    • DF508 mutation increases conformational flexibility of CFTR protein
    • Wieczorek G., Zielenkiewicz P. 2008. DF508 mutation increases conformational flexibility of CFTR protein. J Cyst Fibros 7: 295-300.
    • (2008) J Cyst Fibros , vol.7 , pp. 295-300
    • Wieczorek, G.1    Zielenkiewicz, P.2
  • 81
    • 0028265949 scopus 로고
    • Effect of ATP concentration on CFTR Cl-channels: A kinetic analysis of channel regulation
    • Winter M.C., Sheppard DN, Carson MR, Welsh MJ. 1994. Effect 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
  • 82
    • 0037151094 scopus 로고    scopus 로고
    • A short segment of the R domain of cystic fibrosis transmembrane conductance regulator contains channel stimulatory and inhibitory activities that are separable by sequence modification
    • Xie J., Adams LM, Zhao J, Gerken TA, Davis PB, MaJ. 2002. A short segment of the R domain of cystic fibrosis transmembrane conductance regulator contains channel stimulatory and inhibitory activities that are separable by sequence modification. J Biol Chem 277: 23019-23027.
    • (2002) J Biol Chem , vol.277 , pp. 23019-23027
    • Xie, J.1    Adams, L.M.2    Zhao, J.3    Gerken, T.A.4    Davis, P.B.5    Ma, J.6
  • 83
    • 29644442896 scopus 로고    scopus 로고
    • State-dependent chemical reactivity of an engineered cysteine reveals conformational changes in the outer vestibule of the cystic fibrosis transmembrane conductance regulator
    • Zhang Z.R., Song B, McCarty NA. 2005. State-dependent chemical reactivity of an engineered cysteine reveals conformational changes in the outer vestibule of the cystic fibrosis transmembrane conductance regulator. J Biol Chem 280: 41997-42003.
    • (2005) J Biol Chem , vol.280 , pp. 41997-42003
    • Zhang, Z.R.1    Song, B.2    McCarty, N.A.3
  • 84
    • 67650716316 scopus 로고    scopus 로고
    • Architecture of the cystic fibrosis transmembrane conductance regulator protein and structural changes associated with phosphorylation and nucleotide binding
    • Zhang L., Aleksandrov LA, Zhao Z, Birtley JR, Riordan JR, Ford RC. 2009. Architecture of the cystic fibrosis transmembrane conductance regulator protein and structural changes associated with phosphorylation and nucleotide binding. J Struct Biol 167: 242-251.
    • (2009) J Struct Biol , vol.167 , pp. 242-251
    • Zhang, L.1    Aleksandrov, L.A.2    Zhao, Z.3    Birtley, J.R.4    Riordan, J.R.5    Ford, R.C.6
  • 85
    • 78649761241 scopus 로고    scopus 로고
    • Domain location within the cystic fibrosis transmembrane conductance regulator protein investigated by electron microscopy and gold labelling
    • Zhang L., Aleksandrov LA, Riordan JR, Ford RC. 2011. Domain location within the cystic fibrosis transmembrane conductance regulator protein investigated by electron microscopy and gold labelling. Biochim Biophys Acta 1808: 399-404.
    • (2011) Biochim Biophys Acta , vol.1808 , pp. 399-404
    • Zhang, L.1    Aleksandrov, L.A.2    Riordan, J.R.3    Ford, R.C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.