메뉴 건너뛰기




Volumn 23, Issue 6, 2014, Pages 769-789

Membrane protein stability can be compromised by detergent interactions with the extramembranous soluble domains

Author keywords

CD; CFTR; Detergent interaction; DSC; Extramembrane domain; Membrane protein; NBD1; Soluble domain; Thermal unfolding

Indexed keywords

CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR; DETERGENT; LIPID; MEMBRANE PROTEIN; MONOMER;

EID: 84904174102     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.2460     Document Type: Article
Times cited : (77)

References (102)
  • 1
    • 4344579363 scopus 로고    scopus 로고
    • A pedestrian guide to membrane protein crystallization
    • Wiener MC (2004) A pedestrian guide to membrane protein crystallization. Methods 34:364-372
    • (2004) Methods , vol.34 , pp. 364-372
    • Wiener, M.C.1
  • 2
    • 7044272757 scopus 로고    scopus 로고
    • Membrane proteins, lipids and detergents: Not just a soap opera
    • Seddon AM, Curnow P, Booth PJ (2004) Membrane proteins, lipids and detergents: not just a soap opera. Biochim Biophys Acta 1666:105-117
    • (2004) Biochim Biophys Acta , vol.1666 , pp. 105-117
    • Seddon, A.M.1    Curnow, P.2    Booth, P.J.3
  • 3
    • 0035980050 scopus 로고    scopus 로고
    • Detergents as tools in membrane biochemistry
    • Garavito RM, Ferguson-Miller S (2001) Detergents as tools in membrane biochemistry. J Biol Chem 276: 32403-32406
    • (2001) J Biol Chem , vol.276 , pp. 32403-32406
    • Garavito, R.M.1    Ferguson-Miller, S.2
  • 4
    • 33947172767 scopus 로고    scopus 로고
    • Detergents for the stabilization and crystallization of membrane proteins
    • Prive GG (2007) Detergents for the stabilization and crystallization of membrane proteins. Methods 41:388-397
    • (2007) Methods , vol.41 , pp. 388-397
    • Prive, G.G.1
  • 5
    • 85054483878 scopus 로고    scopus 로고
    • Detergents: An overview
    • Linke D (2009) Detergents: An overview. Methods Enzymol 463:63034-63042
    • (2009) Methods Enzymol , vol.463 , pp. 63034-63042
    • Linke, D.1
  • 6
    • 77950496251 scopus 로고    scopus 로고
    • Practical considerations of membrane protein instability during purification and crystallisation
    • Tate CG (2010) Practical considerations of membrane protein instability during purification and crystallisation. Methods Mol Biol 601:187-203
    • (2010) Methods Mol Biol , vol.601 , pp. 187-203
    • Tate, C.G.1
  • 7
    • 0024604085 scopus 로고
    • Detergent structure and associated lipids determinants in the stabilization of solubilized Ca21-ATPase from sarcoplasmic reticulum
    • Lund S, Orlowski S, de Foresta B, Champeil P, le Maire M, Møller JV (1989) Detergent structure and associated lipids determinants in the stabilization of solubilized Ca21-ATPase from sarcoplasmic reticulum. J Biol Chem 264:4907-4915
    • (1989) J Biol Chem , vol.264 , pp. 4907-4915
    • Lund, S.1    Orlowski, S.2    De Foresta, B.3    Champeil, P.4    Le Maire, M.5    Møller, J.V.6
  • 8
    • 0034707086 scopus 로고    scopus 로고
    • Interaction of membrane proteins and lipids with solubilizing detergents
    • Le Maire M (2000) Interaction of membrane proteins and lipids with solubilizing detergents. Biochim Biophys Acta 1508:86-111
    • (2000) Biochim Biophys Acta , vol.1508 , pp. 86-111
    • Le Maire, M.1
  • 9
    • 0037155264 scopus 로고    scopus 로고
    • Interhelical packing in detergent micelles. Folding of a cystic fibrosis transmembrane conductance regulator construct
    • Therien AG, Deber CM (2002) Interhelical packing in detergent micelles. Folding of a cystic fibrosis transmembrane conductance regulator construct. J Biol Chem 277:6067-6072
    • (2002) J Biol Chem , vol.277 , pp. 6067-6072
    • Therien, A.G.1    Deber, C.M.2
  • 10
    • 0037109010 scopus 로고    scopus 로고
    • Lipid-protein interactions in DHPC micelles containing the integral membrane protein OmpX investigated by NMR spectroscopy
    • Fernáandez C, Hilty C, Wider G, Wüthrich K (2002) Lipid-protein interactions in DHPC micelles containing the integral membrane protein OmpX investigated by NMR spectroscopy. Proc Natl Acad Sci USA 99:13533-13537
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 13533-13537
    • Fernández, C.1    Hilty, C.2    Wider, G.3    Wüthrich, K.4
  • 11
    • 0242353821 scopus 로고    scopus 로고
    • Effect of detergents on the association of the Glycophorin A transmembrane helix
    • Fisher LE, Engelman DM, Sturgis JN (2003) Effect of detergents on the association of the Glycophorin A transmembrane helix. Biophys J 85:3097-3105
    • (2003) Biophys J , vol.85 , pp. 3097-3105
    • Fisher, L.E.1    Engelman, D.M.2    Sturgis, J.N.3
  • 12
    • 0037450517 scopus 로고    scopus 로고
    • In vitro folding of alpha-helical membrane proteins
    • Kiefer H (2003) In vitro folding of alpha-helical membrane proteins. Biochim Biophys Acta 1610:57-62
    • (2003) Biochim Biophys Acta , vol.1610 , pp. 57-62
    • Kiefer, H.1
  • 14
    • 36849088540 scopus 로고    scopus 로고
    • Solution NMR of membrane proteins in bilayer mimics: Small is beautiful, but sometimes bigger is better
    • Poget SF, Girvin ME (2007) Solution NMR of membrane proteins in bilayer mimics: small is beautiful, but sometimes bigger is better. Biochim Biophys Acta 1768:3098-3106
    • (2007) Biochim Biophys Acta , vol.1768 , pp. 3098-3106
    • Poget, S.F.1    Girvin, M.E.2
  • 16
    • 79551597049 scopus 로고    scopus 로고
    • Influence of solubilizing environments on membrane protein structures
    • Cross TA, Mukesh S, Myunggi Y, Zhou HX (2011) Influence of solubilizing environments on membrane protein structures. Trends Biochem Sci 36:117-125
    • (2011) Trends Biochem Sci , vol.36 , pp. 117-125
    • Cross, T.A.1    Mukesh, S.2    Myunggi, Y.3    Zhou, H.X.4
  • 17
    • 84875880032 scopus 로고    scopus 로고
    • Open and shut: Crystal structures of the dodecylmaltoside solubilized mechanosensitive channel of small conductance from Escherichia coli and Helicobacter pylori at 4.4 Å and 4.1 Å resolutions
    • Lai JY, Poon YS, Kaiser JT, Rees DC (2013) Open and shut: Crystal structures of the dodecylmaltoside solubilized mechanosensitive channel of small conductance from Escherichia coli and Helicobacter pylori at 4.4 Å and 4.1 Å resolutions. Protein Sci 22:502-509
    • (2013) Protein Sci , vol.22 , pp. 502-509
    • Lai, J.Y.1    Poon, Y.S.2    Kaiser, J.T.3    Rees, D.C.4
  • 18
    • 77953627340 scopus 로고    scopus 로고
    • Amphipols, nanodiscs, and fluorinated surfactants: Three nonconventional approaches to studying membrane proteins in aqueous solutions
    • Popot JL (2010) Amphipols, nanodiscs, and fluorinated surfactants: three nonconventional approaches to studying membrane proteins in aqueous solutions. Annu Rev Biochem 79:737-775
    • (2010) Annu Rev Biochem , vol.79 , pp. 737-775
    • Popot, J.L.1
  • 20
    • 33750807024 scopus 로고    scopus 로고
    • Identification of conserved lipid/detergent- binding sites in a high-resolution structure of the membrane protein cytochrome c oxidase
    • Qin L, Hiser C, Mulichak A, Garavito RM, Ferguson- Miller S (2006) Identification of conserved lipid/detergent- binding sites in a high-resolution structure of the membrane protein cytochrome c oxidase. Proc Natl Acad Sci USA 103:16117-16122
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 16117-16122
    • Qin, L.1    Hiser, C.2    Mulichak, A.3    Garavito, R.M.4    Ferguson- Miller, S.5
  • 22
    • 0014940381 scopus 로고
    • The gross conformation of protein-sodium dodecyl sulfate complexes
    • Reynolds JA, Tanford C (1970) The gross conformation of protein-sodium dodecyl sulfate complexes. J Biol Chem 245:5161-5165
    • (1970) J Biol Chem , vol.245 , pp. 5161-5165
    • Reynolds, J.A.1    Tanford, C.2
  • 23
    • 0016157537 scopus 로고
    • The interaction of a cationic detergent with bovine serum albumin and other proteins
    • Nozaki Y, Reynolds JA, Tanford C (1974) The interaction of a cationic detergent with bovine serum albumin and other proteins. J Biol Chem 249:4452-4459
    • (1974) J Biol Chem , vol.249 , pp. 4452-4459
    • Nozaki, Y.1    Reynolds, J.A.2    Tanford, C.3
  • 24
    • 0001684352 scopus 로고
    • Surfactant interactions with biomembranes and proteins
    • Jones MN (1992) Surfactant interactions with biomembranes and proteins. Chem Soc Rev 21:127-136
    • (1992) Chem Soc Rev , vol.21 , pp. 127-136
    • Jones, M.N.1
  • 25
    • 0036787578 scopus 로고    scopus 로고
    • Protein unfolding in detergents: Effect of micelle structure, ionic strength, pH, and temperature
    • Otzen DE (2002) Protein unfolding in detergents: effect of micelle structure, ionic strength, pH, and temperature. Biophys J 83:2219-2230
    • (2002) Biophys J , vol.83 , pp. 2219-2230
    • Otzen, D.E.1
  • 26
    • 79958767958 scopus 로고    scopus 로고
    • The variable detergent sensitivity of proteases that are utilized for recombinant protein affinity tag removal
    • Vergis JM, Wiener MC (2011) The variable detergent sensitivity of proteases that are utilized for recombinant protein affinity tag removal. Protein Expr Purif 78:139-142
    • (2011) Protein Expr Purif , vol.78 , pp. 139-142
    • Vergis, J.M.1    Wiener, M.C.2
  • 27
    • 79953210733 scopus 로고    scopus 로고
    • Protein-surfactant interactions: A tale of many states
    • Otzen D (2011) Protein-surfactant interactions: A tale of many states. Biochim Biophys Acta 1814:562-591
    • (2011) Biochim Biophys Acta , vol.1814 , pp. 562-591
    • Otzen, D.1
  • 28
    • 0025013132 scopus 로고
    • Water-soluble proteins do not bind octyl glucoside as judged by molecular sieve chromatographic techniques
    • Lundahl P, Mascher E, Kameyama K, Takagi T (1990) Water-soluble proteins do not bind octyl glucoside as judged by molecular sieve chromatographic techniques. J Chromatogr 518:111-121
    • (1990) J Chromatogr , vol.518 , pp. 111-121
    • Lundahl, P.1    Mascher, E.2    Kameyama, K.3    Takagi, T.4
  • 29
    • 0035022141 scopus 로고    scopus 로고
    • Detergents as probes of hydrophobic binding cavities in serum albumin and other watersoluble proteins
    • Kragh-Hansen U, Hellec F, de Foresta B, le Maire M, Møller JV (2001) Detergents as probes of hydrophobic binding cavities in serum albumin and other watersoluble proteins. Biophys J 80:2898-2911
    • (2001) Biophys J , vol.80 , pp. 2898-2911
    • Kragh-Hansen, U.1    Hellec, F.2    De Foresta, B.3    Le Maire, M.4    Møller, J.V.5
  • 30
    • 56049121413 scopus 로고    scopus 로고
    • Alpha-lactalbumin is unfolded by all classes of surfactants but by different mechanisms
    • Otzen DE, Sehgal P, Westh P (2009) Alpha-lactalbumin is unfolded by all classes of surfactants but by different mechanisms. J Colloid Interface Sci 329:273-283
    • (2009) J Colloid Interface Sci , vol.329 , pp. 273-283
    • Otzen, D.E.1    Sehgal, P.2    Westh, P.3
  • 31
    • 0034798266 scopus 로고    scopus 로고
    • Artificial chaperone mediated refolding of xylanase from an alkalophilic thermophilic Bacillus sp. Implications for in vitro protein renaturation via a folding intermediate
    • Nath D, Rao M (2001) Artificial chaperone mediated refolding of xylanase from an alkalophilic thermophilic Bacillus sp. Implications for in vitro protein renaturation via a folding intermediate. Eur J Biochem 268: 5471-5478
    • (2001) Eur J Biochem , vol.268 , pp. 5471-5478
    • Nath, D.1    Rao, M.2
  • 32
    • 25144460975 scopus 로고    scopus 로고
    • Analysis of protein- surfactant interactions-A titration calorimetric and fluorescence spectroscopic investigation of interactions between Humicola insolens cutinase and an anionic surfactant
    • Nielsen AD, Arleth L, Westh P (2005) Analysis of protein- surfactant interactions-a titration calorimetric and fluorescence spectroscopic investigation of interactions between Humicola insolens cutinase and an anionic surfactant. Biochim Biophys Acta 1752:124-132
    • (2005) Biochim Biophys Acta , vol.1752 , pp. 124-132
    • Nielsen, A.D.1    Arleth, L.2    Westh, P.3
  • 33
    • 13444278724 scopus 로고    scopus 로고
    • Activation, inhibition, and destabilization of Thermomyces lanuginosus lipase by detergents
    • Mogensen JE, Sehgal P, Otzen DE (2005) Activation, inhibition, and destabilization of Thermomyces lanuginosus lipase by detergents. Biochemistry 44:1719-1730
    • (2005) Biochemistry , vol.44 , pp. 1719-1730
    • Mogensen, J.E.1    Sehgal, P.2    Otzen, D.E.3
  • 35
    • 79956335979 scopus 로고    scopus 로고
    • In vitro folding and assembly of the escherichia coli atp-binding cassette transporter, BtuCD
    • Di Bartolo ND, Hvorup RN, Locher KP, Booth PJ (2011) In vitro folding and assembly of the Escherichia coli ATP-binding cassette transporter, BtuCD. J Biol Chem 86:18807-18815
    • (2011) J Biol Chem , vol.86 , pp. 18807-18815
    • Di Bartolo, N.D.1    Hvorup, R.N.2    Locher, K.P.3    Booth, P.J.4
  • 36
    • 79957455592 scopus 로고    scopus 로고
    • Unravelling the folding and stability of an ABC (ATP-binding cassette) transporter
    • Di Bartolo N, Booth PJ (2011) Unravelling the folding and stability of an ABC (ATP-binding cassette) transporter. Biochem Soc Trans 39:751-760
    • (2011) Biochem Soc Trans , vol.39 , pp. 751-760
    • Di Bartolo, N.1    Booth, P.J.2
  • 39
    • 0027380236 scopus 로고
    • The delta F508 mutation decreases the stability of cystic fibrosis transmembrane conductance regulator in the plasma membrane. Determination of functional half-lives on transfected cells
    • Lukacs GL, Chang XB, Bear C, Kartner N, Mohamed A, Riordan JR, Grinstein S (1993) The delta F508 mutation decreases the stability of cystic fibrosis transmembrane conductance regulator in the plasma membrane. Determination of functional half-lives on transfected cells. J Biol Chem 268:21592-21598
    • (1993) J Biol Chem , vol.268 , pp. 21592-21598
    • Lukacs, G.L.1    Chang, X.B.2    Bear, C.3    Kartner, N.4    Mohamed, A.5    Riordan, J.R.6    Grinstein, S.7
  • 40
    • 0031006695 scopus 로고    scopus 로고
    • Localization and suppression of a kinetic defect in cystic fibrosis transmembrane conductance regulator folding
    • Qu BH, 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
  • 41
    • 0033917142 scopus 로고    scopus 로고
    • Defects in processing and trafficking of the cystic fibrosis transmembrane conductance regulator
    • Skach WR (2000) Defects in processing and trafficking of the cystic fibrosis transmembrane conductance regulator. Kidney Int 57:825-831
    • (2000) Kidney Int , vol.57 , pp. 825-831
    • Skach, W.R.1
  • 42
    • 15544371839 scopus 로고    scopus 로고
    • Assembly of functional CFTR chloride channels
    • Riordan JR (2005) Assembly of functional CFTR chloride channels. Annu Rev Physiol 67:701-718
    • (2005) Annu Rev Physiol , vol.67 , pp. 701-718
    • Riordan, J.R.1
  • 43
    • 11444266284 scopus 로고    scopus 로고
    • The DeltaF508 cystic fibrosis mutation impairs domain-domain interactions and arrests post-translational folding of CFTR
    • 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
  • 44
    • 38949212212 scopus 로고    scopus 로고
    • Misfolding of the cystic fibrosis transmembrane conductance regulator and disease
    • Cheung JC, Deber CM (2008) Misfolding of the cystic fibrosis transmembrane conductance regulator and disease. Biochemistry 47:1465-1473
    • (2008) Biochemistry , vol.47 , pp. 1465-1473
    • Cheung, J.C.1    Deber, C.M.2
  • 50
    • 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
  • 52
    • 0027153083 scopus 로고
    • Identification of revertants for the cystic fibrosis delta F508 mutation using STE6- CFTR chimeras in yeast
    • Teem JL, Berger HA, Ostedgaard LS, Rich DP, Tsui LC, Welsh MJ (1993) Identification of revertants for the cystic fibrosis delta F508 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
  • 53
    • 0037184104 scopus 로고    scopus 로고
    • Mutations in the nucleotide binding domain 1 signature motif region rescue processing and functional defects of cystic fibrosis transmembrane conductance regulator delta F508
    • DeCarvalho AC, Gansheroff LJ, Teem JL (2002) Mutations in the nucleotide binding domain 1 signature motif region rescue processing and functional defects of cystic fibrosis transmembrane conductance regulator delta F508. J Biol Chem 277:35896-35905
    • (2002) J Biol Chem , vol.277 , pp. 35896-35905
    • Decarvalho, A.C.1    Gansheroff, L.J.2    Teem, J.L.3
  • 54
    • 77955025743 scopus 로고    scopus 로고
    • The V510D suppressor mutation stabilizes DeltaF508-CFTR at the cell surface
    • Loo TW, Bartlett MC, Clarke DM (2010) The V510D suppressor mutation stabilizes DeltaF508-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
  • 56
    • 77954983869 scopus 로고    scopus 로고
    • Restoration of domain folding and interdomain assembly by second-site suppressors of the DeltaF508 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 DeltaF508 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
  • 60
    • 84863012811 scopus 로고    scopus 로고
    • Mouse cystic fibrosis transmembrane conductance regulator (CFTR) chimeras identify regions that partially rescue CFTR-DF508 processing and alter its gating defect
    • Dong Q, Ostedgaard LS, Rogers C, Vermeer DW, Zhang Y, Welsh MJ (2012) Mouse cystic fibrosis transmembrane conductance regulator (CFTR) chimeras identify regions that partially rescue CFTR-DF508 processing and alter its gating defect. Proc Natl Acad Sci USA 109:917-922
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 917-922
    • Dong, Q.1    Ostedgaard, L.S.2    Rogers, C.3    Vermeer, D.W.4    Zhang, Y.5    Welsh, M.J.6
  • 61
    • 84875976437 scopus 로고    scopus 로고
    • Rampant exchange of the structure and function of extramembrane domains between membrane and water soluble proteins
    • Nam H-J, Han SK, Bowie JU, Kim S (2013) Rampant exchange of the structure and function of extramembrane domains between membrane and water soluble proteins. PLoS Comput Biol 9:e1002997
    • (2013) PLoS Comput Biol , vol.9
    • Nam, H.-J.1    Han, S.K.2    Bowie, J.U.3    Kim, S.4
  • 62
    • 75649088951 scopus 로고    scopus 로고
    • NMR evidence for differential phosphorylation-dependent interactions in WT and DeltaF508 CFTR
    • Kanelis V, Hudson RP, Thibodeau PH, Thomas PJ, Forman-Kay JD (2010) NMR evidence for differential phosphorylation-dependent interactions in WT and DeltaF508 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
  • 63
    • 80052310354 scopus 로고    scopus 로고
    • Biochemical and biophysical approaches to probe CFTR structure
    • Schmidt A, Mendoza JL, Thomas PJ (2011) Biochemical and biophysical approaches to probe CFTR structure. Methods Mol Biol 741:365-376
    • (2011) Methods Mol Biol , vol.741 , pp. 365-376
    • Schmidt, A.1    Mendoza, J.L.2    Thomas, P.J.3
  • 65
    • 84857973429 scopus 로고    scopus 로고
    • Effciency of detergents at maintaining membrane protein structures in their biologically relevant forms
    • Tulumello DV, Deber CM (2012) Effciency of detergents at maintaining membrane protein structures in their biologically relevant forms. Biochim Biophys Acta 1818:1351-1358
    • (2012) Biochim Biophys Acta , vol.1818 , pp. 1351-1358
    • Tulumello, D.V.1    Deber, C.M.2
  • 66
    • 0025281866 scopus 로고
    • Study of strong to ultratight protein interactions using differential scanning calorimetry
    • Brandts JF, Lin LN (1990) Study of strong to ultratight protein interactions using differential scanning calorimetry. Biochemistry 29:6927-6940
    • (1990) Biochemistry , vol.29 , pp. 6927-6940
    • Brandts, J.F.1    Lin, L.N.2
  • 67
    • 0008262867 scopus 로고    scopus 로고
    • Wadood A Differential scanning microcalorimetr
    • In Harding SE, Chowdhry BZ, Eds, Oxford, New York: Oxford University Press
    • Cooper A, Nutley MA, Wadood A, Differential scanning microcalorimetry. In: Harding SE, Chowdhry BZ, Eds. (2000) Protein-ligand interactions: hydrodynamics and calorimetry. Oxford, New York: Oxford University Press, pp 287-318
    • (2000) Protein-ligand Interactions: Hydrodynamics and Calorimetry , pp. 287-318
    • Cooper, A.1    Nutley, M.A.2
  • 68
    • 0038333283 scopus 로고    scopus 로고
    • Stabilization of proteins by ligand binding: Application to drug screening and determination of unfolding energetics
    • Waldron TT, Murphy KP (2003) Stabilization of proteins by ligand binding: Application to drug screening and determination of unfolding energetics. Biochemistry 42:5058-5064
    • (2003) Biochemistry , vol.42 , pp. 5058-5064
    • Waldron, T.T.1    Murphy, K.P.2
  • 69
    • 0023146181 scopus 로고
    • Thermodynamic study of yeast phosphoglycerate kinase
    • Hu CQ, Sturtevant JM (1987) Thermodynamic study of yeast phosphoglycerate kinase. Biochemistry 26:178-182
    • (1987) Biochemistry , vol.26 , pp. 178-182
    • Hu, C.Q.1    Sturtevant, J.M.2
  • 70
    • 0000826487 scopus 로고
    • Biochemical applications of differential scanning calorimetry
    • Sturtevant JM (1987) Biochemical applications of differential scanning calorimetry. Ann Rev Phys Chem 38:463-488
    • (1987) Ann Rev Phys Chem , vol.38 , pp. 463-488
    • Sturtevant, J.M.1
  • 71
    • 0024291325 scopus 로고
    • Differential scanning calorimetric study of the thermal denaturation of aspartate transcarbamoylase of Escherichia coli
    • Edge V, Allewell NM, Sturtevant JM (1988) Differential scanning calorimetric study of the thermal denaturation of aspartate transcarbamoylase of Escherichia coli. Biochemistry 27:8081-8087
    • (1988) Biochemistry , vol.27 , pp. 8081-8087
    • Edge, V.1    Allewell, N.M.2    Sturtevant, J.M.3
  • 72
    • 77953133721 scopus 로고    scopus 로고
    • Tricks of the trade used to accelerate high-resolution structure determination of membrane proteins
    • Sonoda Y, Cameron A, Newstead S, Omote H, Moriyama Y, Kasahara M, Iwata S, Drew D (2010) Tricks of the trade used to accelerate high-resolution structure determination of membrane proteins. FEBS Lett 584:2539-2547
    • (2010) FEBS Lett , vol.584 , pp. 2539-2547
    • Sonoda, Y.1    Cameron, A.2    Newstead, S.3    Omote, H.4    Moriyama, Y.5    Kasahara, M.6    Iwata, S.7    Drew, D.8
  • 73
    • 39549108859 scopus 로고    scopus 로고
    • Rationalizing alpha-helical membrane protein crystallization
    • Newstead S, Ferrandon S, Iwata S (2008) Rationalizing alpha-helical membrane protein crystallization. Protein Sci 17:466-472
    • (2008) Protein Sci , vol.17 , pp. 466-472
    • Newstead, S.1    Ferrandon, S.2    Iwata, S.3
  • 76
    • 0035199839 scopus 로고    scopus 로고
    • Octyl glucoside induced formation of the molten globule-like state of glutamate dehydrogenase
    • Ghobadi S, Safarian S, Moosavi-Movahedi AA, Ranjbar B (2001) Octyl glucoside induced formation of the molten globule-like state of glutamate dehydrogenase. J Biochem 130:671-677
    • (2001) J Biochem , vol.130 , pp. 671-677
    • Ghobadi, S.1    Safarian, S.2    Moosavi-Movahedi, A.A.3    Ranjbar, B.4
  • 77
    • 0030669141 scopus 로고    scopus 로고
    • A novel procedure for the efficient purification of the cystic fibrosis transmembrane conductance regulator (CFTR
    • Ramjeesingh M, Li C, Garami E, Huan LJ, Hewryk M, Wang Y, Galley K, Bear CE (1997) A novel procedure for the efficient purification of the cystic fibrosis transmembrane conductance regulator (CFTR). Biochem J 327:17-21
    • (1997) Biochem J , vol.327 , pp. 17-21
    • Ramjeesingh, M.1    Li, C.2    Garami, E.3    Huan, L.J.4    Hewryk, M.5    Wang, Y.6    Galley, K.7    Bear, C.E.8
  • 78
    • 0032524073 scopus 로고    scopus 로고
    • Lysophosphatidylglycerol: A novel effective detergent for solubilizing and purifying the cystic fibrosis transmembrane conductance regulator
    • Huang P, Liu Q, Scarborough GA (1998) Lysophosphatidylglycerol: A novel effective detergent for solubilizing and purifying the cystic fibrosis transmembrane conductance regulator. Anal Biochem 259:89-97
    • (1998) Anal Biochem , vol.259 , pp. 89-97
    • Huang, P.1    Liu, Q.2    Scarborough, G.A.3
  • 79
    • 0942301384 scopus 로고    scopus 로고
    • Characterization of the adenosinetriphosphatase and transport activities of purified cystic fibrosis transmembrane conductance regulator
    • Ketchum CJ, Rajendrakumar GV, Maloney PC (2004) Characterization of the adenosinetriphosphatase and transport activities of purified cystic fibrosis transmembrane conductance regulator. Biochemistry 43: 1045-1053
    • (2004) Biochemistry , vol.43 , pp. 1045-1053
    • Ketchum, C.J.1    Rajendrakumar, G.V.2    Maloney, P.C.3
  • 80
    • 44449169949 scopus 로고    scopus 로고
    • The intact CFTR protein mediates ATPase rather than adenylate kinase activity
    • Ramjeesingh M, Ugwu F, Stratford FL, Huan LJ, Li C, Bear CE (2008) The intact CFTR protein mediates ATPase rather than adenylate kinase activity. Biochem J 412:315-321
    • (2008) Biochem J , vol.412 , pp. 315-321
    • Ramjeesingh, M.1    Ugwu, F.2    Stratford, F.L.3    Huan, L.J.4    Li, C.5    Bear, C.E.6
  • 81
    • 77954758860 scopus 로고    scopus 로고
    • SDS-induced fibrillation of alpha-synuclein: An alternative fibrillation pathway
    • Giehm L, Oliveira CL, Christiansen G, Pedersen JS, Otzen DE (2010) SDS-induced fibrillation of alpha-synuclein: An alternative fibrillation pathway. J Mol Biol 401:115-133
    • (2010) J Mol Biol , vol.401 , pp. 115-133
    • Giehm, L.1    Oliveira, C.L.2    Christiansen, G.3    Pedersen, J.S.4    Otzen, D.E.5
  • 83
    • 77955678117 scopus 로고    scopus 로고
    • Lysophospholipid micelles sustain the stability and catalytic activity of diacylglycerol kinase in the absence of lipids
    • Koehler J, Sulistijo ES, Sakakura M, Kim HJ, Ellis CD, Sanders CR (2010) Lysophospholipid micelles sustain the stability and catalytic activity of diacylglycerol kinase in the absence of lipids. Biochemistry 49:7089-7099
    • (2010) Biochemistry , vol.49 , pp. 7089-7099
    • Koehler, J.1    Sulistijo, E.S.2    Sakakura, M.3    Kim, H.J.4    Ellis, C.D.5    Sanders, C.R.6
  • 86
    • 0016292941 scopus 로고
    • Urea and guanidine hydrochloride denaturation of ribonuclease, lysozyme, alpha-chymotrypsin, and beta-lactoglobulin
    • Greene RF Jr, Pace CN (1974) Urea and guanidine hydrochloride denaturation of ribonuclease, lysozyme, alpha-chymotrypsin, and beta-lactoglobulin. J Biol Chem 249:5388-5393
    • (1974) J Biol Chem , vol.249 , pp. 5388-5393
    • Greene Jr., R.F.1    Pace, C.N.2
  • 87
    • 0037007485 scopus 로고    scopus 로고
    • Fifty years of solvent denaturation
    • Schellman JA (2002) Fifty years of solvent denaturation. Biophys Chem 96:91-101
    • (2002) Biophys Chem , vol.96 , pp. 91-101
    • Schellman, J.A.1
  • 88
    • 20544461199 scopus 로고    scopus 로고
    • Thermodynamics of protein interactions with urea and guanidinium hydrochloride
    • Makhatadze GI (1999) Thermodynamics of protein interactions with urea and guanidinium hydrochloride. J Phys Chem 103:4781-4785
    • (1999) J Phys Chem , vol.103 , pp. 4781-4785
    • Makhatadze, G.I.1
  • 89
    • 0141783830 scopus 로고    scopus 로고
    • Preferential interactions of urea with lysozyme and their linkage to protein denaturation
    • Timasheff SN, Xie G (2003) Preferential interactions of urea with lysozyme and their linkage to protein denaturation. Biophys Chem 105:421-448
    • (2003) Biophys Chem , vol.105 , pp. 421-448
    • Timasheff, S.N.1    Xie, G.2
  • 90
    • 0038311869 scopus 로고    scopus 로고
    • Protein stability in mixed solvents: A balance of contact interaction and excluded volume
    • Schellman JA (2003) Protein stability in mixed solvents: A balance of contact interaction and excluded volume. Biophys J 85:108-125
    • (2003) Biophys J , vol.85 , pp. 108-125
    • Schellman, J.A.1
  • 91
    • 0018588511 scopus 로고
    • Stability of proteins: Small globular proteins
    • Privalov PL (1979) Stability of proteins: small globular proteins. Adv Prot Chem 33:167-241
    • (1979) Adv Prot Chem , vol.33 , pp. 167-241
    • Privalov, P.L.1
  • 92
    • 34548842221 scopus 로고    scopus 로고
    • Conserved lipid-binding sites in membrane proteins: A focus on cytochrome c oxidase
    • Qin L, Sharpe MA, Garavito RM, Ferguson-Miller S (2007) Conserved lipid-binding sites in membrane proteins: A focus on cytochrome c oxidase. Curr Opin Struct Biol 17:444-450
    • (2007) Curr Opin Struct Biol , vol.17 , pp. 444-450
    • Qin, L.1    Sharpe, M.A.2    Garavito, R.M.3    Ferguson-Miller, S.4
  • 93
    • 0030921564 scopus 로고    scopus 로고
    • The functional purification of P-glycoprotein is dependent on maintenance of a lipid-protein interface
    • Callaghan R, Berridge G, Ferry DR, Higgins CF (1997) The functional purification of P-glycoprotein is dependent on maintenance of a lipid-protein interface. Biochim Biophys Acta 1328:109-124
    • (1997) Biochim Biophys Acta , vol.1328 , pp. 109-124
    • Callaghan, R.1    Berridge, G.2    Ferry, D.R.3    Higgins, C.F.4
  • 94
    • 0029804316 scopus 로고    scopus 로고
    • Efficient purification and reconstitution of P-glycoprotein for functional and structural studies
    • Dong M, Penin F, Baggetto LG (1996) Efficient purification and reconstitution of P-glycoprotein for functional and structural studies. J Biol Chem 271:28875-28883
    • (1996) J Biol Chem , vol.271 , pp. 28875-28883
    • Dong, M.1    Penin, F.2    Baggetto, L.G.3
  • 95
    • 0031149391 scopus 로고    scopus 로고
    • Complete removal and exchange of sodium dodecyl sulfate bound to soluble and membrane proteins and restoration of their activities, using ceramic hydroxyapatite chromatography
    • Dong M, Baggetto LG, Falson P, Le Maire M, Penin F (1997) Complete removal and exchange of sodium dodecyl sulfate bound to soluble and membrane proteins and restoration of their activities, using ceramic hydroxyapatite chromatography. Anal Biochem 247: 333-341
    • (1997) Anal Biochem , vol.247 , pp. 333-341
    • Dong, M.1    Baggetto, L.G.2    Falson, P.3    Le Maire, M.4    Penin, F.5
  • 98
    • 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
    • Aleksandrov L, Aleksandrov AA, Chang XB, Riordan JR (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
    • (2002) J Biol Chem , vol.277 , pp. 15419-15425
    • Aleksandrov, L.1    Aleksandrov, A.A.2    Chang, X.B.3    Riordan, J.R.4
  • 99
    • 56049099012 scopus 로고    scopus 로고
    • 2+-dependent ATP occlusion at the first nucleotidebinding domain (NBD1) of CFTR does not require the second (NBD2
    • 2+-dependent ATP occlusion at the first nucleotidebinding domain (NBD1) of CFTR does not require the second (NBD2). Biochem J 416:129-136
    • (2008) Biochem J 416 , pp. 129-136
    • Aleksandrov, L.1    Aleksandrov, A.2    Riordan, J.R.3
  • 100
    • 84904214720 scopus 로고    scopus 로고
    • Biophysical measures of full-length CFTR thermostability: Comparison of wild-type and F508del CFTR
    • Cant N, Rimington T, Meng X, Pollock N, Ford B (2013) Biophysical measures of full-length CFTR thermostability: Comparison of wild-type and F508del CFTR. Pediatric Pulmonol 48:209-210
    • (2013) Pediatric Pulmonol , vol.48 , pp. 209-210
    • Cant, N.1    Rimington, T.2    Meng, X.3    Pollock, N.4    Ford, B.5
  • 102
    • 33645454462 scopus 로고    scopus 로고
    • Optimization of membrane protein overexpression and purification using GFP fusions
    • Drew D, Lerch M, Kunji E, Slotboom DJ, de Gier JW (2006) Optimization of membrane protein overexpression and purification using GFP fusions. Nat Methods 3:303-313
    • (2006) Nat Methods , vol.3 , pp. 303-313
    • Drew, D.1    Lerch, M.2    Kunji, E.3    Slotboom, D.J.4    De Gier, J.W.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.