메뉴 건너뛰기




Volumn 247, Issue 9-10, 2014, Pages 759-796

Amphipols for Each Season

Author keywords

Biochemistry; Biophysics; Folding; Membrane proteins; Stabilization; Surfactants

Indexed keywords

AMPHIPOL; DODECYL SULFATE SODIUM; MEMBRANE PROTEIN; POLYMER; UNCLASSIFIED DRUG; UREA; LIPID BILAYER; SOLUTION AND SOLUBILITY; SURFACTANT; WATER;

EID: 84910116811     PISSN: 00222631     EISSN: 14321424     Source Type: Journal    
DOI: 10.1007/s00232-014-9666-8     Document Type: Article
Times cited : (93)

References (155)
  • 2
    • 84911003666 scopus 로고    scopus 로고
    • Outer membrane protein F stabilised with minimal amphipol forms linear arrays and LPS-dependent 2D crystals
    • PID: 24585057
    • Arunmanee W, Harris JR, Lakey JH (2014) Outer membrane protein F stabilised with minimal amphipol forms linear arrays and LPS-dependent 2D crystals. J Membr Biol. doi:10.1007/s00232-014-9640-5
    • (2014) J Membr Biol
    • Arunmanee, W.1    Harris, J.R.2    Lakey, J.H.3
  • 3
    • 79959294939 scopus 로고    scopus 로고
    • New advances in production and functional folding of G protein-coupled receptors
    • PID: 21497924
    • Banères J-L, Popot J-L, Mouillac B (2011) New advances in production and functional folding of G protein-coupled receptors. Trends Biotechnol 29:314–322
    • (2011) Trends Biotechnol , vol.29 , pp. 314-322
    • Banères, J.-L.1    Popot, J.-L.2    Mouillac, B.3
  • 4
    • 84865762982 scopus 로고    scopus 로고
    • Poly(styrene-co-maleic acid)-based pH-sensitive liposomes mediate cytosolic delivery of drugs for enhanced cancer chemotherapy
    • PID: 22884831, COI: 1:CAS:528:DC%2BC38XhtF2ru7fP
    • Banerjee S, Sen K, Pal TK, Guha SK (2012) Poly(styrene-co-maleic acid)-based pH-sensitive liposomes mediate cytosolic delivery of drugs for enhanced cancer chemotherapy. Int J Pharm 436:786–797
    • (2012) Int J Pharm , vol.436 , pp. 786-797
    • Banerjee, S.1    Sen, K.2    Pal, T.K.3    Guha, S.K.4
  • 5
    • 67650361634 scopus 로고    scopus 로고
    • Toward multiprotein nanoarrays using nanografting and DNA-directed immobilization of proteins
    • PID: 19583282, COI: 1:CAS:528:DC%2BD1MXnsVehs70%3D
    • Bano F, Fruk L, Sanavio B, Glettenberg M, Casalis L, Niemeyer CM, Scoles G (2009) Toward multiprotein nanoarrays using nanografting and DNA-directed immobilization of proteins. Nano Lett 9:2614–2618
    • (2009) Nano Lett , vol.9 , pp. 2614-2618
    • Bano, F.1    Fruk, L.2    Sanavio, B.3    Glettenberg, M.4    Casalis, L.5    Niemeyer, C.M.6    Scoles, G.7
  • 6
    • 84861615590 scopus 로고    scopus 로고
    • Amphipol mediated surface immobilization of FhuA: a platform for label-free detection of the bacteriophage protein pb5
    • COI: 1:CAS:528:DC%2BC38Xnt1Khu7s%3D
    • Basit H, Sharma S, Van der Heyden A, Gondran C, Breyton C, Dumy P, Winnik FM, Labbé P (2012) Amphipol mediated surface immobilization of FhuA: a platform for label-free detection of the bacteriophage protein pb5. Chem Commun 48:6037–6039
    • (2012) Chem Commun , vol.48 , pp. 6037-6039
    • Basit, H.1    Sharma, S.2    Van der Heyden, A.3    Gondran, C.4    Breyton, C.5    Dumy, P.6    Winnik, F.M.7    Labbé, P.8
  • 7
    • 77957959485 scopus 로고    scopus 로고
    • Non-ionic amphipols: new tools for in vitro studies of membrane proteins. Validation and development of biochemical and biophysical applications
    • Bazzacco P (2009) Non-ionic amphipols: new tools for in vitro studies of membrane proteins. Validation and development of biochemical and biophysical applications. Ph. D. Thesis, Université Paris-7, Paris, 176 p
    • (2009) Ph. D. Thesis, Université Paris-7, Paris , pp. 176
    • Bazzacco, P.1
  • 8
    • 72449183187 scopus 로고    scopus 로고
    • Trapping and stabilization of integral membrane proteins by hydrophobically grafted glucose-based telomers
    • PID: 20000638, COI: 1:CAS:528:DC%2BD1MXhsVKhs7nK
    • Bazzacco P, Sharma KS, Durand G, Giusti F, Ebel C, Popot J-L, Pucci B (2009) Trapping and stabilization of integral membrane proteins by hydrophobically grafted glucose-based telomers. Biomacromolecules 10:3317–3326
    • (2009) Biomacromolecules , vol.10 , pp. 3317-3326
    • Bazzacco, P.1    Sharma, K.S.2    Durand, G.3    Giusti, F.4    Ebel, C.5    Popot, J.-L.6    Pucci, B.7
  • 11
    • 84876163719 scopus 로고    scopus 로고
    • DNA nanotubes for NMR structure determination of membrane proteins
    • PID: 23518667
    • Bellot G, McClintock MA, Chou JJ, Shih WM (2013) DNA nanotubes for NMR structure determination of membrane proteins. Nat Protoc 8:755–770
    • (2013) Nat Protoc , vol.8 , pp. 755-770
    • Bellot, G.1    McClintock, M.A.2    Chou, J.J.3    Shih, W.M.4
  • 12
    • 77950465278 scopus 로고    scopus 로고
    • Amphipols and fluorinated surfactants: two alternatives to detergents for studying membrane proteins in vitro
    • Mus-Veteau I, (ed), The Humana Press, Totowa:
    • Breyton C, Pucci B, Popot J-L (2010) Amphipols and fluorinated surfactants: two alternatives to detergents for studying membrane proteins in vitro. In: Mus-Veteau I (ed) Heterologous expression of membrane proteins: methods and protocols. The Humana Press, Totowa, pp 219–245
    • (2010) Heterologous expression of membrane proteins: methods and protocols , pp. 219-245
    • Breyton, C.1    Pucci, B.2    Popot, J.-L.3
  • 13
    • 84882744404 scopus 로고    scopus 로고
    • Structure and folding of outer membrane proteins
    • Tamm LK, (ed), Academic Press, Elsevier, Oxford:
    • Buchanan SK, Yamashita S, Fleming KG (2012) Structure and folding of outer membrane proteins. In: Tamm LK (ed) Membranes. Academic Press, Elsevier, Oxford, pp 139–163
    • (2012) Membranes , pp. 139-163
    • Buchanan, S.K.1    Yamashita, S.2    Fleming, K.G.3
  • 14
    • 79957505876 scopus 로고    scopus 로고
    • Crystallizing membrane proteins for structure-function studies using lipidic mesophases
    • PID: 21599641, COI: 1:CAS:528:DC%2BC3MXmslKisLg%3D
    • Caffrey M (2011) Crystallizing membrane proteins for structure-function studies using lipidic mesophases. Biochem Soc Trans 39:725–732
    • (2011) Biochem Soc Trans , vol.39 , pp. 725-732
    • Caffrey, M.1
  • 15
    • 84889594608 scopus 로고    scopus 로고
    • TRPV1 structures in distinct conformations reveal activation mechanisms
    • PID: 24305161, COI: 1:CAS:528:DC%2BC3sXhvVyisL%2FI
    • Cao E, Liao M, Cheng Y, Julius D (2013) TRPV1 structures in distinct conformations reveal activation mechanisms. Nature 504:113–118
    • (2013) Nature , vol.504 , pp. 113-118
    • Cao, E.1    Liao, M.2    Cheng, Y.3    Julius, D.4
  • 16
    • 60349095580 scopus 로고    scopus 로고
    • Inter- and intramolecular contacts in a membrane protein/surfactant complex observed by heteronuclear dipole-to-dipole cross-relaxation
    • COI: 1:CAS:528:DC%2BD1MXitlGgu7k%3D
    • Catoire LJ, Zoonens M, van Heijenoort C, Giusti F, Popot J-L, Guittet E (2009) Inter- and intramolecular contacts in a membrane protein/surfactant complex observed by heteronuclear dipole-to-dipole cross-relaxation. J Magn Res 197:91–95
    • (2009) J Magn Res , vol.197 , pp. 91-95
    • Catoire, L.J.1    Zoonens, M.2    van Heijenoort, C.3    Giusti, F.4    Popot, J.-L.5    Guittet, E.6
  • 18
    • 77951288279 scopus 로고    scopus 로고
    • Solution NMR mapping of water-accessible residues in the transmembrane β-barrel of OmpX
    • PID: 19639312, COI: 1:CAS:528:DC%2BC3cXjtlanur4%3D
    • Catoire LJ, Zoonens M, van Heijenoort C, Giusti F, Guittet E, Popot J-L (2010b) Solution NMR mapping of water-accessible residues in the transmembrane β-barrel of OmpX. Eur Biophys J 39:623–630
    • (2010) Eur Biophys J , vol.39 , pp. 623-630
    • Catoire, L.J.1    Zoonens, M.2    van Heijenoort, C.3    Giusti, F.4    Guittet, E.5    Popot, J.-L.6
  • 19
    • 80051664851 scopus 로고    scopus 로고
    • Electrostatically-driven fast association and perdeuteration allow detection of transferred cross-relaxation for G protein-coupled receptor ligands with equilibrium dissociation constants in the high-to-low nanomolar range
    • PID: 21688157, COI: 1:CAS:528:DC%2BC3MXos1yltLo%3D
    • Catoire LJ, Damian M, Baaden M, Guittet E, Banères J-L (2011) Electrostatically-driven fast association and perdeuteration allow detection of transferred cross-relaxation for G protein-coupled receptor ligands with equilibrium dissociation constants in the high-to-low nanomolar range. J Biomol NMR 50:191–195
    • (2011) J Biomol NMR , vol.50 , pp. 191-195
    • Catoire, L.J.1    Damian, M.2    Baaden, M.3    Guittet, E.4    Banères, J.-L.5
  • 20
    • 84911002845 scopus 로고    scopus 로고
    • Micelles, bicelles, amphipols, nanodiscs, liposomes or intact cells: the hitch-hiker guide to the study of membrane proteins by NMR
    • Mus-Veteau I, (ed), Springer, New York:
    • Catoire LJ, Warnet XL, Warschawski DE (2014) Micelles, bicelles, amphipols, nanodiscs, liposomes or intact cells: the hitch-hiker guide to the study of membrane proteins by NMR. In: Mus-Veteau I (ed) Membrane protein production for structural analysis. Springer, New York (in press)
    • (2014) Membrane protein production for structural analysis
    • Catoire, L.J.1    Warnet, X.L.2    Warschawski, D.E.3
  • 24
    • 80052089906 scopus 로고    scopus 로고
    • Lipidic cubic phase technologies for membrane protein structural studies
    • PID: 21775127, COI: 1:CAS:528:DC%2BC3MXhtV2qu7vN
    • Cherezov V (2011) Lipidic cubic phase technologies for membrane protein structural studies. Curr Opin Struct Biol 21:559–566
    • (2011) Curr Opin Struct Biol , vol.21 , pp. 559-566
    • Cherezov, V.1
  • 25
    • 33645054559 scopus 로고    scopus 로고
    • Room to move: crystallizing membrane proteins in swollen lipidic mesophases
    • PID: 16490208, COI: 1:CAS:528:DC%2BD28XivVGqt7k%3D
    • Cherezov V, Clogston J, Papiz MZ, Caffrey M (2006) Room to move: crystallizing membrane proteins in swollen lipidic mesophases. J Mol Biol 357:1605–1618
    • (2006) J Mol Biol , vol.357 , pp. 1605-1618
    • Cherezov, V.1    Clogston, J.2    Papiz, M.Z.3    Caffrey, M.4
  • 27
    • 34548803570 scopus 로고    scopus 로고
    • Facile preparation of complex protein architectures with sub-100-nm resolution on surfaces
    • COI: 1:CAS:528:DC%2BD2sXhtFamtLvK
    • Coyer SR, García AJ, Delamarche E (2007) Facile preparation of complex protein architectures with sub-100-nm resolution on surfaces. Angew Chem Int Ed 46:6837–6840
    • (2007) Angew Chem Int Ed , vol.46 , pp. 6837-6840
    • Coyer, S.R.1    García, A.J.2    Delamarche, E.3
  • 28
    • 80055073153 scopus 로고    scopus 로고
    • Molecular architecture and subunit organization of TRPA1 ion channel revealed by electron microscopy
    • PID: 21908607, COI: 1:CAS:528:DC%2BC3MXhtlyktbzK
    • Cvetkov TL, Huynh KW, Cohen MR, Moiseenkova-Bell VY (2011) Molecular architecture and subunit organization of TRPA1 ion channel revealed by electron microscopy. J Biol Chem 286:38168–38176
    • (2011) J Biol Chem , vol.286 , pp. 38168-38176
    • Cvetkov, T.L.1    Huynh, K.W.2    Cohen, M.R.3    Moiseenkova-Bell, V.Y.4
  • 29
    • 67650080503 scopus 로고    scopus 로고
    • Amphipol-assisted in vitro folding of G protein-coupled receptors
    • PID: 19534448, COI: 1:CAS:528:DC%2BD1MXnt1Ogu7Y%3D
    • Dahmane T, Damian M, Mary S, Popot J-L, Banères J-L (2009) Amphipol-assisted in vitro folding of G protein-coupled receptors. Biochemistry 48:6516–6521
    • (2009) Biochemistry , vol.48 , pp. 6516-6521
    • Dahmane, T.1    Damian, M.2    Mary, S.3    Popot, J.-L.4    Banères, J.-L.5
  • 30
    • 80053569591 scopus 로고    scopus 로고
    • Sulfonated amphipols: synthesis, properties and applications
    • PID: 21638274, COI: 1:CAS:528:DC%2BC3MXmvFahsrc%3D
    • Dahmane T, Giusti F, Catoire LJ, Popot J-L (2011) Sulfonated amphipols: synthesis, properties and applications. Biopolymers 95:811–823
    • (2011) Biopolymers , vol.95 , pp. 811-823
    • Dahmane, T.1    Giusti, F.2    Catoire, L.J.3    Popot, J.-L.4
  • 31
    • 84879501057 scopus 로고    scopus 로고
    • Amphipol-assisted folding of bacteriorhodopsin in the presence and absence of lipids Functional consequences
    • PID: 22926530, COI: 1:CAS:528:DC%2BC3sXjtFGgu74%3D
    • Dahmane T, Rappaport F, Popot J-L (2013) Amphipol-assisted folding of bacteriorhodopsin in the presence and absence of lipids Functional consequences. Eur Biophys J 42:85–101
    • (2013) Eur Biophys J , vol.42 , pp. 85-101
    • Dahmane, T.1    Rappaport, F.2    Popot, J.-L.3
  • 32
    • 84856715703 scopus 로고    scopus 로고
    • High constitutive activity is an intrinsic feature of ghrelin receptor protein: a study with a functional monomeric GHS-R1a receptor reconstituted in lipid discs
    • PID: 22117076, COI: 1:CAS:528:DC%2BC38XhvVSjsbo%3D
    • Damian M, Marie J, Leyris J-P, Fehrentz J-A, Verdié P, Martinez J, Banères J-L, Mary S (2012) High constitutive activity is an intrinsic feature of ghrelin receptor protein: a study with a functional monomeric GHS-R1a receptor reconstituted in lipid discs. J Biol Chem 287:3630–3641
    • (2012) J Biol Chem , vol.287 , pp. 3630-3641
    • Damian, M.1    Marie, J.2    Leyris, J.-P.3    Fehrentz, J.-A.4    Verdié, P.5    Martinez, J.6    Banères, J.-L.7    Mary, S.8
  • 33
    • 84894611460 scopus 로고    scopus 로고
    • A step closer to membrane protein multiplexed nano-arrays using biotin-doped polypyrrole
    • PID: 24476392, COI: 1:CAS:528:DC%2BC2cXhsVKrsrk%3D
    • Della Pia EA, Holm J, Lloret N, Le Bon C, Popot J-L, Zoonens M, Nygård J, Martinez KL (2014a) A step closer to membrane protein multiplexed nano-arrays using biotin-doped polypyrrole. ACS Nano 8:1844–1853
    • (2014) ACS Nano , vol.8 , pp. 1844-1853
    • Della Pia, E.A.1    Holm, J.2    Lloret, N.3    Le Bon, C.4    Popot, J.-L.5    Zoonens, M.6    Nygård, J.7    Martinez, K.L.8
  • 34
    • 84910113035 scopus 로고    scopus 로고
    • Functionalized amphipols: a versatile toolbox suitable for applications of membrane proteins in synthetic biology
    • PID: 24728227
    • Della Pia EA, Westh Hansen R, Zoonens M, Martinez KL (2014b) Functionalized amphipols: a versatile toolbox suitable for applications of membrane proteins in synthetic biology. J Membr Biol. doi:10.1007/s00232-014-9663-y
    • (2014) J Membr Biol
    • Della Pia, E.A.1    Westh Hansen, R.2    Zoonens, M.3    Martinez, K.L.4
  • 35
    • 36048943576 scopus 로고    scopus 로고
    • Complexation of integral membrane proteins by phosphorylcholine-based amphipols
    • PID: 17825785, COI: 1:CAS:528:DC%2BD2sXht12gurfE
    • Diab C, Tribet C, Gohon Y, Popot J-L, Winnik FM (2007a) Complexation of integral membrane proteins by phosphorylcholine-based amphipols. Biochim Biophys Acta 1768:2737–2747
    • (2007) Biochim Biophys Acta , vol.1768 , pp. 2737-2747
    • Diab, C.1    Tribet, C.2    Gohon, Y.3    Popot, J.-L.4    Winnik, F.M.5
  • 36
    • 33947425242 scopus 로고    scopus 로고
    • Enthalpy of interaction and binding isotherms of non-ionic surfactants onto micellar amphiphilic polymers (amphipols)
    • PID: 17284056, COI: 1:CAS:528:DC%2BD2sXhtlemsrk%3D
    • Diab C, Winnik FM, Tribet C (2007b) Enthalpy of interaction and binding isotherms of non-ionic surfactants onto micellar amphiphilic polymers (amphipols). Langmuir 23:3025–3035
    • (2007) Langmuir , vol.23 , pp. 3025-3035
    • Diab, C.1    Winnik, F.M.2    Tribet, C.3
  • 38
    • 0037379049 scopus 로고    scopus 로고
    • Amphiphilic biopolymers (amphibiopols) as new surfactants for membrane protein solubilization
    • PID: 12649425
    • Duval-Terrié C, Cosette P, Molle G, Muller G, Dé E (2003) Amphiphilic biopolymers (amphibiopols) as new surfactants for membrane protein solubilization. Protein Sci 12:681–689
    • (2003) Protein Sci , vol.12 , pp. 681-689
    • Duval-Terrié, C.1    Cosette, P.2    Molle, G.3    Muller, G.4    Dé, E.5
  • 40
    • 84874943409 scopus 로고    scopus 로고
    • Cell-free expressed bacteriorhodopsin in different soluble membrane mimetics: biophysical properties and NMR accessibility
    • PID: 23415558, COI: 1:CAS:528:DC%2BC3sXis1Onsrg%3D
    • Etzkorn M, Raschle T, Hagn F, Gelev V, Rice AJ, Walz T, Wagner G (2013) Cell-free expressed bacteriorhodopsin in different soluble membrane mimetics: biophysical properties and NMR accessibility. Structure 21:394–401
    • (2013) Structure , vol.21 , pp. 394-401
    • Etzkorn, M.1    Raschle, T.2    Hagn, F.3    Gelev, V.4    Rice, A.J.5    Walz, T.6    Wagner, G.7
  • 41
    • 84908587074 scopus 로고    scopus 로고
    • How amphipols embed membrane proteins: global solvent accessibility and interaction with a flexible protein terminus
    • Etzkorn M, Zoonens M, Catoire LJ, Popot J-L, Hiller S (2014) How amphipols embed membrane proteins: global solvent accessibility and interaction with a flexible protein terminus. J Membr Biol. doi:10.1007/s00232-014-9657-9
    • (2014) J Membr Biol
    • Etzkorn, M.1    Zoonens, M.2    Catoire, L.J.3    Popot, J.-L.4    Hiller, S.5
  • 42
    • 84911004807 scopus 로고    scopus 로고
    • Cocco MJ: Long-term stability of a vaccine formulated with the amphipol-trapped major outer membrane protein from Chlamydia trachomatis. J Membr Biol
    • Feinstein HE, Tifrea D, Popot J-L, de la Maza LM, Cocco MJ (2014) Long-term stability of a vaccine formulated with the amphipol-trapped major outer membrane protein from Chlamydia trachomatis. J Membr Biol. doi:10.1007/s00232-014-9693-5
    • (2014) de la Maza LM
    • Feinstein, H.E.1    Tifrea, D.2    Popot, J.-L.3
  • 43
    • 84903124448 scopus 로고    scopus 로고
    • Fernandez A, Le Bon C, Baumlin N, Giusti F, Crémel G, Popot J-L, Bagnard D () In vivo characterization of the biodistribution profile of amphipols. J Membr Biol
    • Fernandez A, Le Bon C, Baumlin N, Giusti F, Crémel G, Popot J-L, Bagnard D (2014) In vivo characterization of the biodistribution profile of amphipols. J Membr Biol. doi:10.1007/s00232-014-9682-8
    • (2014)
  • 45
    • 34548329761 scopus 로고    scopus 로고
    • The use of amphipathic polymers for cryo-electron microscopy of NADH: ubiquinone oxidoreductase (Complex I)
    • PID: 17760617
    • Flötenmeyer M, Weiss H, Tribet C, Popot J-L, Leonard K (2007) The use of amphipathic polymers for cryo-electron microscopy of NADH: ubiquinone oxidoreductase (Complex I). J Microsc 227:229–235
    • (2007) J Microsc , vol.227 , pp. 229-235
    • Flötenmeyer, M.1    Weiss, H.2    Tribet, C.3    Popot, J.-L.4    Leonard, K.5
  • 46
    • 84863935182 scopus 로고    scopus 로고
    • Well-defined critical association concentration and rapid adsorption at the air/water interface of a short amphiphilic polymer, amphipol A8-35: a study by Förster resonance energy transfer and dynamic surface tension measurements
    • PID: 22712750, COI: 1:CAS:528:DC%2BC38XovVyhtrw%3D
    • Giusti F, Popot J-L, Tribet C (2012) Well-defined critical association concentration and rapid adsorption at the air/water interface of a short amphiphilic polymer, amphipol A8-35: a study by Förster resonance energy transfer and dynamic surface tension measurements. Langmuir 28:10372–10380
    • (2012) Langmuir , vol.28 , pp. 10372-10380
    • Giusti, F.1    Popot, J.-L.2    Tribet, C.3
  • 49
    • 79955791418 scopus 로고    scopus 로고
    • Etude des interactions entre un analogue du fragment transmembranaire de la glycophorine A et des polymères amphiphiles: les amphipols, DEA Thesis, Université Paris VI
    • Gohon Y (1996) Etude des interactions entre un analogue du fragment transmembranaire de la glycophorine A et des polymères amphiphiles: les amphipols, DEA Thesis, Université Paris VI, Paris, 28 p
    • (1996) Paris , pp. 28
    • Gohon, Y.1
  • 50
    • 0037700081 scopus 로고    scopus 로고
    • Membrane protein-surfactant complexes
    • COI: 1:CAS:528:DC%2BD3sXksVKjtrc%3D
    • Gohon Y, Popot J-L (2003) Membrane protein-surfactant complexes. Curr Opin Colloid Interface Sci 8:15–22
    • (2003) Curr Opin Colloid Interface Sci , vol.8 , pp. 15-22
    • Gohon, Y.1    Popot, J.-L.2
  • 51
    • 5644275289 scopus 로고    scopus 로고
    • Partial specific volume and solvent interactions of amphipol A8-35
    • PID: 15494140, COI: 1:CAS:528:DC%2BD2cXos1KlsLo%3D
    • Gohon Y, Pavlov G, Timmins P, Tribet C, Popot J-L, Ebel C (2004) Partial specific volume and solvent interactions of amphipol A8-35. Anal Biochem 334:318–334
    • (2004) Anal Biochem , vol.334 , pp. 318-334
    • Gohon, Y.1    Pavlov, G.2    Timmins, P.3    Tribet, C.4    Popot, J.-L.5    Ebel, C.6
  • 52
    • 32344431772 scopus 로고    scopus 로고
    • Well-defined nanoparticles formed by hydrophobic assembly of a short and polydisperse random terpolymer, amphipol A8-35
    • PID: 16430295, COI: 1:CAS:528:DC%2BD28Xht1Sisw%3D%3D
    • Gohon Y, Giusti F, Prata C, Charvolin D, Timmins P, Ebel C, Tribet C, Popot J-L (2006) Well-defined nanoparticles formed by hydrophobic assembly of a short and polydisperse random terpolymer, amphipol A8-35. Langmuir 22:1281–1290
    • (2006) Langmuir , vol.22 , pp. 1281-1290
    • Gohon, Y.1    Giusti, F.2    Prata, C.3    Charvolin, D.4    Timmins, P.5    Ebel, C.6    Tribet, C.7    Popot, J.-L.8
  • 54
    • 78650746623 scopus 로고    scopus 로고
    • High water solubility and fold in amphipols of proteins with large hydrophobic regions: oleosins and caleosin from seed lipid bodies
    • PID: 21146495, COI: 1:CAS:528:DC%2BC3MXhvFent70%3D
    • Gohon Y, Vindigni J-D, Pallier A, Wien F, Celia H, Giuliani A, Tribet C, Chardot T, Briozzo P (2011) High water solubility and fold in amphipols of proteins with large hydrophobic regions: oleosins and caleosin from seed lipid bodies. Biochim Biophys Acta 1808:706–716
    • (2011) Biochim Biophys Acta , vol.1808 , pp. 706-716
    • Gohon, Y.1    Vindigni, J.-D.2    Pallier, A.3    Wien, F.4    Celia, H.5    Giuliani, A.6    Tribet, C.7    Chardot, T.8    Briozzo, P.9
  • 55
    • 52649156124 scopus 로고    scopus 로고
    • Microfluidic patterning of nanodisc lipid bilayers and multiplexed analysis of protein interaction
    • PID: 18813396, COI: 1:CAS:528:DC%2BD1cXhtFCrtLnM
    • Goluch ED, Shaw AW, Sligar SG, Liu C (2008) Microfluidic patterning of nanodisc lipid bilayers and multiplexed analysis of protein interaction. Lab Chip 8:1723–1728
    • (2008) Lab Chip , vol.8 , pp. 1723-1728
    • Goluch, E.D.1    Shaw, A.W.2    Sligar, S.G.3    Liu, C.4
  • 57
    • 80052639750 scopus 로고    scopus 로고
    • Wheat germ cell-free expression system as a pathway to improve protein yield and solubility for the SSGCID pipeline
    • COI: 1:CAS:528:DC%2BC3MXhtFCgtLbK
    • Guild K, Zhang Y, Stacy R, Mundt E, Benbow S, Green A, Myler PJ (2011) Wheat germ cell-free expression system as a pathway to improve protein yield and solubility for the SSGCID pipeline. Acta Crystallogr F 67:1027–1031
    • (2011) Acta Crystallogr F , vol.67 , pp. 1027-1031
    • Guild, K.1    Zhang, Y.2    Stacy, R.3    Mundt, E.4    Benbow, S.5    Green, A.6    Myler, P.J.7
  • 58
    • 84857641142 scopus 로고    scopus 로고
    • Folding and stability of membrane transport proteins in vitro
    • PID: 22100867, COI: 1:CAS:528:DC%2BC38XjtlOmtbw%3D
    • Harris NJ, Booth PJ (2012) Folding and stability of membrane transport proteins in vitro. Biochim Biophys Acta 1818:1055–1066
    • (2012) Biochim Biophys Acta , vol.1818 , pp. 1055-1066
    • Harris, N.J.1    Booth, P.J.2
  • 59
    • 84889578787 scopus 로고    scopus 로고
    • Ion channel seen by electron microscopy
    • PID: 24305155, COI: 1:CAS:528:DC%2BC3sXhvVyisrfE
    • Henderson R (2013) Ion channel seen by electron microscopy. Nature 504:93–94
    • (2013) Nature , vol.504 , pp. 93-94
    • Henderson, R.1
  • 61
    • 84910127701 scopus 로고    scopus 로고
    • Application of amphipols for structure-functional analysis of TRP channels, J Membr Biol:
    • Huynh KW, Cohen MR, Moiseenkova-Bell VY (2014) Application of amphipols for structure-functional analysis of TRP channels. J Membr Biol. doi:10.1007/s00232-014-9684-6
    • (2014) Moiseenkova-Bell VY
    • Huynh, K.W.1    Cohen, M.R.2
  • 63
    • 67650654611 scopus 로고    scopus 로고
    • Membrane protein expression: no cells required
    • PID: 19616329, COI: 1:CAS:528:DC%2BD1MXptVeqtrg%3D
    • Katzen F, Peterson TC, Kudlicki W (2009) Membrane protein expression: no cells required. Trends Biotechnol 27:455–460
    • (2009) Trends Biotechnol , vol.27 , pp. 455-460
    • Katzen, F.1    Peterson, T.C.2    Kudlicki, W.3
  • 64
    • 84890951593 scopus 로고    scopus 로고
    • Structural and functional analysis of the native peripherin-ROM1 complex isolated from photoreceptor cells
    • PID: 24196967, COI: 1:CAS:528:DC%2BC3sXhvFymu77L
    • Kevany BM, Tsybovsky Y, Campuzano IDG, Schnier PD, Engel A, Palczewski K (2013) Structural and functional analysis of the native peripherin-ROM1 complex isolated from photoreceptor cells. J Biol Chem 288:36272–36284
    • (2013) J Biol Chem , vol.288 , pp. 36272-36284
    • Kevany, B.M.1    Tsybovsky, Y.2    Campuzano, I.D.G.3    Schnier, P.D.4    Engel, A.5    Palczewski, K.6
  • 65
    • 0035793196 scopus 로고    scopus 로고
    • Direct electrochemistry of photosystem I
    • COI: 1:CAS:528:DC%2BD3MXovFSksA%3D%3D
    • Kievit O, Brudvig GW (2001) Direct electrochemistry of photosystem I. J Electroanal Chem 497:139–149
    • (2001) J Electroanal Chem , vol.497 , pp. 139-149
    • Kievit, O.1    Brudvig, G.W.2
  • 66
    • 33748307399 scopus 로고    scopus 로고
    • Cell-free expression as an emerging technique for the large scale production of integral membrane protein
    • PID: 16930130, COI: 1:CAS:528:DC%2BD28Xht1yqsrrO
    • Klammt C, Schwarz D, Löhr F, Schneider B, Dötsch V, Bernhard F (2006) Cell-free expression as an emerging technique for the large scale production of integral membrane protein. FEBS J 273:4141–4153
    • (2006) FEBS J , vol.273 , pp. 4141-4153
    • Klammt, C.1    Schwarz, D.2    Löhr, F.3    Schneider, B.4    Dötsch, V.5    Bernhard, F.6
  • 67
    • 79956197327 scopus 로고    scopus 로고
    • Polymer-based cell-free expression of ligand-binding family B G-protein coupled receptors without detergents
    • PID: 21465615, COI: 1:CAS:528:DC%2BC3MXmtFSnur0%3D
    • Klammt C, Perrin M-H, Maslennikov I, Renault L, Krupa M, Kwiatkowski W, Stahlberg H, Vale W, Choe S (2011) Polymer-based cell-free expression of ligand-binding family B G-protein coupled receptors without detergents. Protein Sci 20:1030–1041
    • (2011) Protein Sci , vol.20 , pp. 1030-1041
    • Klammt, C.1    Perrin, M.-H.2    Maslennikov, I.3    Renault, L.4    Krupa, M.5    Kwiatkowski, W.6    Stahlberg, H.7    Vale, W.8    Choe, S.9
  • 68
    • 67650541090 scopus 로고    scopus 로고
    • Membrane proteins solubilized intact in lipid containing nanoparticles bounded by styrene maleic acid copolymer
    • PID: 19449872, COI: 1:CAS:528:DC%2BD1MXmtVGgt7s%3D
    • Knowles TJ, Finka R, Smith C, Lin Y-P, Dafforn T, Overduin M (2009) Membrane proteins solubilized intact in lipid containing nanoparticles bounded by styrene maleic acid copolymer. J Am Chem Soc 131:7484–7485
    • (2009) J Am Chem Soc , vol.131 , pp. 7484-7485
    • Knowles, T.J.1    Finka, R.2    Smith, C.3    Lin, Y.-P.4    Dafforn, T.5    Overduin, M.6
  • 69
    • 84857653322 scopus 로고    scopus 로고
    • Folding of diphteria toxin T-domain in the presence of amphipols and fluorinated surfactants: toward thermodynamic measurements of membrane protein folding
    • PID: 21945883, COI: 1:CAS:528:DC%2BC38XjtlOqtLw%3D
    • Kyrychenko A, Rodnin MV, Vargas MU, Sharma SK, Durand G, Pucci B, Popot J-L, Ladokhin AS (2012) Folding of diphteria toxin T-domain in the presence of amphipols and fluorinated surfactants: toward thermodynamic measurements of membrane protein folding. Biochim Biophys Acta 1818:1006–1012
    • (2012) Biochim Biophys Acta , vol.1818 , pp. 1006-1012
    • Kyrychenko, A.1    Rodnin, M.V.2    Vargas, M.U.3    Sharma, S.K.4    Durand, G.5    Pucci, B.6    Popot, J.-L.7    Ladokhin, A.S.8
  • 70
    • 33847379819 scopus 로고    scopus 로고
    • Constructing novel materials with DNA
    • LaBean TM, Li H (2007) Constructing novel materials with DNA. Nano Today 2:26–35
    • (2007) Nano Today , vol.2 , pp. 26-35
    • LaBean, T.M.1    Li, H.2
  • 71
    • 0035450348 scopus 로고    scopus 로고
    • Slow reorganization of small phosphatidylcholine vesicles upon adsorption of amphiphilic polymers
    • PID: 11502120
    • Ladavière C, Toustou M, Gulik-Krzywicki T, Tribet C (2001) Slow reorganization of small phosphatidylcholine vesicles upon adsorption of amphiphilic polymers. J Colloid Interface Sci 241:178–187
    • (2001) J Colloid Interface Sci , vol.241 , pp. 178-187
    • Ladavière, C.1    Toustou, M.2    Gulik-Krzywicki, T.3    Tribet, C.4
  • 72
    • 0036813129 scopus 로고    scopus 로고
    • Lateral organization of lipid membranes induced by amphiphilic polymer inclusions
    • Ladavière C, Tribet C, Cribier S (2002) Lateral organization of lipid membranes induced by amphiphilic polymer inclusions. Langmuir 18:7320–7327
    • (2002) Langmuir , vol.18 , pp. 7320-7327
    • Ladavière, C.1    Tribet, C.2    Cribier, S.3
  • 73
    • 84874084320 scopus 로고    scopus 로고
    • Amphipol trapping of a functional CYP system
    • PID: 23586999, COI: 1:CAS:528:DC%2BC3sXjtVCqurw%3D
    • Laursen T, Naur P, Møller BL (2013) Amphipol trapping of a functional CYP system. Biotechnol Appl Biochem 60:119–127
    • (2013) Biotechnol Appl Biochem , vol.60 , pp. 119-127
    • Laursen, T.1    Naur, P.2    Møller, B.L.3
  • 75
    • 84911003891 scopus 로고    scopus 로고
    • Labeling and functionalizing amphipols for biological applications
    • Le Bon C, Popot J-L, Giusti F (2014b) Labeling and functionalizing amphipols for biological applications. J Membr Biol. doi:10.1007/s00232-014-9655-y
    • (2014) J Membr Biol
    • Le Bon, C.1    Popot, J.-L.2    Giusti, F.3
  • 76
    • 84869398484 scopus 로고    scopus 로고
    • Amphipathic polymers enable the study of functional membrane proteins in the gas phase
    • PID: 23072351, COI: 1:CAS:528:DC%2BC38XhsFWks7vE
    • Leney AC, McMorran LM, Radford SE, Ashcroft AE (2012) Amphipathic polymers enable the study of functional membrane proteins in the gas phase. Anal Chem 84:9841–9847
    • (2012) Anal Chem , vol.84 , pp. 9841-9847
    • Leney, A.C.1    McMorran, L.M.2    Radford, S.E.3    Ashcroft, A.E.4
  • 77
    • 84889607320 scopus 로고    scopus 로고
    • Structure of the TRPV1 ion channel determined by electron cryo-microscopy
    • PID: 24305160, COI: 1:CAS:528:DC%2BC3sXhvVyis77N
    • Liao M, Cao E, Julius D, Cheng Y (2013) Structure of the TRPV1 ion channel determined by electron cryo-microscopy. Nature 504:107–112
    • (2013) Nature , vol.504 , pp. 107-112
    • Liao, M.1    Cao, E.2    Julius, D.3    Cheng, Y.4
  • 78
    • 84897875372 scopus 로고    scopus 로고
    • Single particle electron cryo-microscopy of a mammalian ion channel
    • COI: 1:CAS:528:DC%2BC2cXhtlCjtb3F
    • Liao M, Cao E, Julius D, Cheng Y (2014) Single particle electron cryo-microscopy of a mammalian ion channel. Curr Opin Struct Biol 27:1–7
    • (2014) Curr Opin Struct Biol , vol.27 , pp. 1-7
    • Liao, M.1    Cao, E.2    Julius, D.3    Cheng, Y.4
  • 79
    • 34347336441 scopus 로고    scopus 로고
    • Impact of polymer microstructure on the self-assembly of amphiphilic polymers in aqueous solutions
    • COI: 1:CAS:528:DC%2BD2sXlt1Cku7w%3D
    • Liu RCW, Pallier A, Brestaz M, Pantoustier N, Tribet C (2007) Impact of polymer microstructure on the self-assembly of amphiphilic polymers in aqueous solutions. Macromolecules 40:4276–4286
    • (2007) Macromolecules , vol.40 , pp. 4276-4286
    • Liu, R.C.W.1    Pallier, A.2    Brestaz, M.3    Pantoustier, N.4    Tribet, C.5
  • 80
    • 84877276942 scopus 로고    scopus 로고
    • A detergent-free strategy for the reconstitution of active enzyme complexes from native biological membranes into nanoscale discs
    • PID: 23663692, COI: 1:CAS:528:DC%2BC3sXhtFKktLrF
    • Long AR, O’Brien CC, Malhotra K, Schwall CT, Albert AD, Watts A, Alder NN (2013) A detergent-free strategy for the reconstitution of active enzyme complexes from native biological membranes into nanoscale discs. BMC Biotechnol 13:41. doi:10.1186/1472-6750-13-41
    • (2013) BMC Biotechnol , vol.13 , pp. 41
    • Long, A.R.1    O’Brien, C.C.2    Malhotra, K.3    Schwall, C.T.4    Albert, A.D.5    Watts, A.6    Alder, N.N.7
  • 81
    • 33644894171 scopus 로고    scopus 로고
    • Size, charge, and interactions with giant lipid vesicles of quantum dots coated with an amphiphilic macromolecule
    • PID: 16489822, COI: 1:CAS:528:DC%2BD28XntFGmsw%3D%3D
    • Luccardini C, Tribet C, Vial F, Marchi-Artzner V, Dahan M (2006) Size, charge, and interactions with giant lipid vesicles of quantum dots coated with an amphiphilic macromolecule. Langmuir 22:2304–2310
    • (2006) Langmuir , vol.22 , pp. 2304-2310
    • Luccardini, C.1    Tribet, C.2    Vial, F.3    Marchi-Artzner, V.4    Dahan, M.5
  • 83
    • 84868271955 scopus 로고    scopus 로고
    • The thermally induced aggregation of immunoglobulin G in solution is prevented by amphipols
    • COI: 1:CAS:528:DC%2BC38Xhs1Onu7vE
    • Ma D, Martin N, Herbet A, Boquet D, Tribet C, Winnik FM (2012) The thermally induced aggregation of immunoglobulin G in solution is prevented by amphipols. Chem Lett 41:1380–1382
    • (2012) Chem Lett , vol.41 , pp. 1380-1382
    • Ma, D.1    Martin, N.2    Herbet, A.3    Boquet, D.4    Tribet, C.5    Winnik, F.M.6
  • 85
    • 84910118231 scopus 로고    scopus 로고
    • Amphiphilic macromolecules on cell membranes: from protective layers to controlled permeabilization. J Membr Biol
    • Marie E, Sagan S, Cribier S, Tribet C (2014) Amphiphilic macromolecules on cell membranes: from protective layers to controlled permeabilization. J Membr Biol. doi:10.1007/s00232-014-9679-3
    • (2014) doi:10.1007/s00232-014-9679-3
    • Marie, E.1    Sagan, S.2    Cribier, S.3    Tribet, C.4
  • 86
    • 0037174145 scopus 로고    scopus 로고
    • Allosteric transitions of Torpedo acetylcholine receptor in lipids, detergent and amphipols: molecular interactions vs. physical constraints
    • PID: 12297315, COI: 1:CAS:528:DC%2BD38Xnt1KksL8%3D
    • Martinez KL, Gohon Y, Corringer P-J, Tribet C, Mérola F, Changeux J-P, Popot J-L (2002) Allosteric transitions of Torpedo acetylcholine receptor in lipids, detergent and amphipols: molecular interactions vs. physical constraints. FEBS Lett 528:251–256
    • (2002) FEBS Lett , vol.528 , pp. 251-256
    • Martinez, K.L.1    Gohon, Y.2    Corringer, P.-J.3    Tribet, C.4    Mérola, F.5    Changeux, J.-P.6    Popot, J.-L.7
  • 88
    • 0028294304 scopus 로고
    • 2+-ATPase from sarcoplasmic reticulum of rabbit skeletal muscle
    • PID: 8168622, COI: 1:CAS:528:DyaK2cXltVaqtLY%3D
    • 2+-ATPase from sarcoplasmic reticulum of rabbit skeletal muscle. FEBS Lett 343:155–159
    • (1994) FEBS Lett , vol.343 , pp. 155-159
    • Merino, J.M.1    Møller, J.V.2    Gutiérrez-Merino, C.3
  • 89
    • 0035919720 scopus 로고    scopus 로고
    • Use of amphipathic polymers to deliver a membrane protein to lipid bilayers
    • PID: 11470268, COI: 1:CAS:528:DC%2BD3MXltlKqtLY%3D
    • Nagy JK, Kuhn Hoffmann A, Keyes MH, Gray DN, Oxenoid K, Sanders CR (2001) Use of amphipathic polymers to deliver a membrane protein to lipid bilayers. FEBS Lett 501:115–120
    • (2001) FEBS Lett , vol.501 , pp. 115-120
    • Nagy, J.K.1    Kuhn Hoffmann, A.2    Keyes, M.H.3    Gray, D.N.4    Oxenoid, K.5    Sanders, C.R.6
  • 90
    • 33847639732 scopus 로고    scopus 로고
    • Applications of phospholipid bilayer nanodiscs in the study of membranes and membrane proteins
    • PID: 17263563, COI: 1:CAS:528:DC%2BD2sXhtVOmt74%3D
    • Nath A, Atkins WM, Sligar SG (2007) Applications of phospholipid bilayer nanodiscs in the study of membranes and membrane proteins. Biochemistry 46:2059–2069
    • (2007) Biochemistry , vol.46 , pp. 2059-2069
    • Nath, A.1    Atkins, W.M.2    Sligar, S.G.3
  • 91
    • 84874617914 scopus 로고    scopus 로고
    • From cells to peptides: “One-stop” integrated proteomic processing using amphipols
    • PID: 23394071, COI: 1:CAS:528:DC%2BC3sXit1Sqt74%3D
    • Ning Z, Seebun D, Hawley B, Chang C-K, Figeys D (2013) From cells to peptides: “One-stop” integrated proteomic processing using amphipols. J Proteome Res 12:1512–1519
    • (2013) J Proteome Res , vol.12 , pp. 1512-1519
    • Ning, Z.1    Seebun, D.2    Hawley, B.3    Chang, C.-K.4    Figeys, D.5
  • 92
    • 84911004169 scopus 로고    scopus 로고
    • APols aided protein precipitation: a rapid method for protein concentrating for proteomic analysis. J Membr Biol
    • Ning Z, Hawley B, Seebun D, Figeys D (2014) APols aided protein precipitation: a rapid method for protein concentrating for proteomic analysis. J Membr Biol. doi:10.1007/s00232-014-9668-6
    • (2014) doi:10.1007/s00232-014-9668-6
    • Ning, Z.1    Hawley, B.2    Seebun, D.3    Figeys, D.4
  • 93
    • 32344431887 scopus 로고    scopus 로고
    • Amphipols: strategies for an improved PS2 environment in aqueous solution
    • Miyake J, (ed), Elsevier, Dordrecht:
    • Nowaczyk M, Oworah-Nkruma R, Zoonens M, Rögner M, Popot J-L (2004) Amphipols: strategies for an improved PS2 environment in aqueous solution. In: Miyake J (ed) Biohydrogen III. Elsevier, Dordrecht, pp 151–159
    • (2004) Biohydrogen III , pp. 151-159
    • Nowaczyk, M.1    Oworah-Nkruma, R.2    Zoonens, M.3    Rögner, M.4    Popot, J.-L.5
  • 95
    • 84911005818 scopus 로고    scopus 로고
    • Amphipols and photosynthetic light-harvesting pigment-protein complexes, J Membr Biol:
    • Opačić M, Durand G, Bosco M, Polidori A, Popot J-L, (2014b). Amphipols and photosynthetic light-harvesting pigment-protein complexes. J Membr Biol (this issue)
    • (2014) Popot J-L
    • Opačić, M.1    Durand, G.2    Bosco, M.3    Polidori, A.4
  • 96
    • 84860752106 scopus 로고    scopus 로고
    • Detergent-free formation and physicochemical characterization of nanosized lipid–polymer complexes
    • COI: 1:CAS:528:DC%2BC38XkvVKitrc%3D
    • Orwick MC, Judge PJ, Procek J, Lindholm L, Graziadei A, Engel A, Grobner G, Watts A (2012) Detergent-free formation and physicochemical characterization of nanosized lipid–polymer complexes. Angew Chem Int Ed 51:4653–4657
    • (2012) Angew Chem Int Ed , vol.51 , pp. 4653-4657
    • Orwick, M.C.1    Judge, P.J.2    Procek, J.3    Lindholm, L.4    Graziadei, A.5    Engel, A.6    Grobner, G.7    Watts, A.8
  • 97
    • 84866314929 scopus 로고    scopus 로고
    • Detergent-free incorporation of a seven-transmembrane receptor protein into nanosized bilayer Lipodisq particles for functional and biophysical studies
    • PID: 22827450, COI: 1:CAS:528:DC%2BC38XhtVyns77E
    • Orwick-Rydmark M, Lovett JE, Graziadei A, Lindholm L, Hicks MR, Watts A (2012) Detergent-free incorporation of a seven-transmembrane receptor protein into nanosized bilayer Lipodisq particles for functional and biophysical studies. Nano Lett 12:4687–4692
    • (2012) Nano Lett , vol.12 , pp. 4687-4692
    • Orwick-Rydmark, M.1    Lovett, J.E.2    Graziadei, A.3    Lindholm, L.4    Hicks, M.R.5    Watts, A.6
  • 98
    • 84876525138 scopus 로고    scopus 로고
    • Folding of outer membrane proteins
    • PID: 23131493, COI: 1:CAS:528:DC%2BC38XhslejtbfJ
    • Otzen DE, Andersen KK (2013) Folding of outer membrane proteins. Arch Biochem Biophys 531:34–43
    • (2013) Arch Biochem Biophys , vol.531 , pp. 34-43
    • Otzen, D.E.1    Andersen, K.K.2
  • 99
    • 34147158906 scopus 로고    scopus 로고
    • Fluorinated and hemifluorinated surfactants as alternatives to detergents for membrane protein cell-free synthesis
    • PID: 17176254, COI: 1:CAS:528:DC%2BD2sXksFChtLY%3D
    • Park K-H, Berrier C, Lebaupain F, Pucci B, Popot J-L, Ghazi A, Zito F (2007) Fluorinated and hemifluorinated surfactants as alternatives to detergents for membrane protein cell-free synthesis. Biochem J 403:183–187
    • (2007) Biochem J , vol.403 , pp. 183-187
    • Park, K.-H.1    Berrier, C.2    Lebaupain, F.3    Pucci, B.4    Popot, J.-L.5    Ghazi, A.6    Zito, F.7
  • 100
    • 79953707602 scopus 로고    scopus 로고
    • In the cauldron of cell-free synthesis of membrane proteins: playing with new surfactants
    • COI: 1:CAS:528:DC%2BC3MXksFGqs70%3D
    • Park K-H, Billon-Denis E, Dahmane T, Lebaupain F, Pucci B, Breyton C, Zito F (2011) In the cauldron of cell-free synthesis of membrane proteins: playing with new surfactants. New Biotechnol 28:255–261
    • (2011) New Biotechnol , vol.28 , pp. 255-261
    • Park, K.-H.1    Billon-Denis, E.2    Dahmane, T.3    Lebaupain, F.4    Pucci, B.5    Breyton, C.6    Zito, F.7
  • 101
    • 80052233358 scopus 로고    scopus 로고
    • All-atom and coarse-grained molecular dynamics simulations of a membrane protein stabilizing polymer
    • PID: 21806035, COI: 1:CAS:528:DC%2BC3MXhtVagsLjE
    • Perlmutter JD, Drasler WJ, Xie W, Gao J, Popot J-L, Sachs JN (2011) All-atom and coarse-grained molecular dynamics simulations of a membrane protein stabilizing polymer. Langmuir 27:10523–10537
    • (2011) Langmuir , vol.27 , pp. 10523-10537
    • Perlmutter, J.D.1    Drasler, W.J.2    Xie, W.3    Gao, J.4    Popot, J.-L.5    Sachs, J.N.6
  • 102
    • 84910125751 scopus 로고    scopus 로고
    • Molecular dynamics simulations of a membrane protein/amphipol complex, J Membr Biol:
    • Perlmutter JD, Popot J-L, Sachs JN (2014) Molecular dynamics simulations of a membrane protein/amphipol complex. J Membr Biol. doi:10.1007/s00232-014-9690-8
    • (2014) Sachs JN
    • Perlmutter, J.D.1    Popot, J.-L.2
  • 103
    • 7244231305 scopus 로고    scopus 로고
    • Stabilization of membranes upon interaction of amphipathic polymers with membrane proteins
    • PID: 15459343, COI: 1:CAS:528:DC%2BD2cXpsVWhtbs%3D
    • Picard M, Duval-Terrié C, Dé E, Champeil P (2004) Stabilization of membranes upon interaction of amphipathic polymers with membrane proteins. Protein Sci 13:3056–3058
    • (2004) Protein Sci , vol.13 , pp. 3056-3058
    • Picard, M.1    Duval-Terrié, C.2    Dé, E.3    Champeil, P.4
  • 107
    • 84879499434 scopus 로고    scopus 로고
    • Folding and stability of outer membrane protein A (OmpA) from Escherichia coli in an amphipathic polymer, amphipol A8-35
    • PID: 23370791, COI: 1:CAS:528:DC%2BC3sXjtFGgurc%3D
    • Pocanschi C, Popot J-L, Kleinschmidt JH (2013) Folding and stability of outer membrane protein A (OmpA) from Escherichia coli in an amphipathic polymer, amphipol A8-35. Eur Biophys J 42:103–118
    • (2013) Eur Biophys J , vol.42 , pp. 103-118
    • Pocanschi, C.1    Popot, J.-L.2    Kleinschmidt, J.H.3
  • 110
    • 77953627340 scopus 로고    scopus 로고
    • Amphipols, nanodiscs, and fluorinated surfactants: three non-conventional approaches to studying membrane proteins in aqueous solutions
    • PID: 20307193, COI: 1:CAS:528:DC%2BC3cXpslSht7k%3D
    • Popot J-L (2010) Amphipols, nanodiscs, and fluorinated surfactants: three non-conventional 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
  • 111
    • 84914094978 scopus 로고    scopus 로고
    • Popot J-L () Folding membrane proteins in vitro: a table and some comments. Arch Biochem Biophys (in press)
    • Popot J-L (2014) Folding membrane proteins in vitro: a table and some comments. Arch Biochem Biophys (in press)
    • (2014)
  • 112
    • 84911007149 scopus 로고    scopus 로고
    • Popot J-L, Engelman DM () The paradox of membrane proteins folding in the absence of a membrane (in preparation)
    • Popot J-L, Engelman DM (2014) The paradox of membrane proteins folding in the absence of a membrane (in preparation)
    • (2014)
  • 113
    • 84911007354 scopus 로고    scopus 로고
    • Popot J-L, Kleinschmidt JH () Stabilization and folding of integral membrane proteins by amphipols (in preparation)
    • Popot J-L, Kleinschmidt JH (2014) Stabilization and folding of integral membrane proteins by amphipols (in preparation)
    • (2014)
  • 116
    • 58849133696 scopus 로고    scopus 로고
    • Molecular structure of low density lipoprotein: current status and future challenges
    • PID: 18797861, COI: 1:CAS:528:DC%2BD1MXotVeltw%3D%3D
    • Prassl R, Laggner P (2009) Molecular structure of low density lipoprotein: current status and future challenges. Eur Biophys J 38:145–158
    • (2009) Eur Biophys J , vol.38 , pp. 145-158
    • Prassl, R.1    Laggner, P.2
  • 117
    • 0034425014 scopus 로고    scopus 로고
    • Non-ionic amphiphilic polymers derived from tris(hydroxymethyl)-acrylamidomethane keep membrane proteins soluble and native in the absence of detergent
    • COI: 1:STN:280:DC%2BD3MrksVehtw%3D%3D
    • Prata C, Giusti F, Gohon Y, Pucci B, Popot J-L, Tribet C (2001) Non-ionic amphiphilic polymers derived from tris(hydroxymethyl)-acrylamidomethane keep membrane proteins soluble and native in the absence of detergent. Biopolymers 56:77–84
    • (2001) Biopolymers , vol.56 , pp. 77-84
    • Prata, C.1    Giusti, F.2    Gohon, Y.3    Pucci, B.4    Popot, J.-L.5    Tribet, C.6
  • 118
    • 33947172767 scopus 로고    scopus 로고
    • Detergents for the stabilization and crystallization of membrane proteins
    • PID: 17367711
    • Privé GG (2007) Detergents for the stabilization and crystallization of membrane proteins. Methods 41:388–397
    • (2007) Methods , vol.41 , pp. 388-397
    • Privé, G.G.1
  • 119
    • 69249118964 scopus 로고    scopus 로고
    • Lipopeptide detergents for membrane protein studies
    • Privé G (2009) Lipopeptide detergents for membrane protein studies. Curr Opin Struct Biol 19:1–7
    • (2009) Curr Opin Struct Biol , vol.19 , pp. 1-7
    • Privé, G.1
  • 120
    • 49249113021 scopus 로고    scopus 로고
    • Quantum dot-amphipol nanocomplex for intracellular delivery and real-time imaging of siRNA
    • PID: 19206308, COI: 1:CAS:528:DC%2BD1cXns1Wjsbw%3D
    • Qi L, Gao X (2008) Quantum dot-amphipol nanocomplex for intracellular delivery and real-time imaging of siRNA. ACS Nano 2:1403–1410
    • (2008) ACS Nano , vol.2 , pp. 1403-1410
    • Qi, L.1    Gao, X.2
  • 121
    • 84866077867 scopus 로고    scopus 로고
    • Cell-penetrating magnetic nanoparticles for highly efficient delivery and intracellular imaging of siRNA
    • PID: 22913876, COI: 1:CAS:528:DC%2BC38Xht1ektrrE
    • Qi L, Wu L, Zheng S, Wang Y, Fu H, Cui D (2012) Cell-penetrating magnetic nanoparticles for highly efficient delivery and intracellular imaging of siRNA. Biomacromolecules 13:2723–2730
    • (2012) Biomacromolecules , vol.13 , pp. 2723-2730
    • Qi, L.1    Wu, L.2    Zheng, S.3    Wang, Y.4    Fu, H.5    Cui, D.6
  • 123
    • 79953702800 scopus 로고    scopus 로고
    • Production of membrane proteins without cells or detergents
    • COI: 1:CAS:528:DC%2BC3MXksFGqs7w%3D
    • Rajesh S, Knowles TJ, Overduin M (2011) Production of membrane proteins without cells or detergents. New Biotechnol 28:250–254
    • (2011) New Biotechnol , vol.28 , pp. 250-254
    • Rajesh, S.1    Knowles, T.J.2    Overduin, M.3
  • 124
    • 77955981439 scopus 로고    scopus 로고
    • Nonmicellar systems for solution NMR spectroscopy of membrane proteins
    • PID: 20570504, COI: 1:CAS:528:DC%2BC3cXhtVKhtLvJ
    • Raschle T, Hiller S, Etzkorn M, Wagner G (2010) Nonmicellar systems for solution NMR spectroscopy of membrane proteins. Curr Opin Struct Biol 20:471–479
    • (2010) Curr Opin Struct Biol , vol.20 , pp. 471-479
    • Raschle, T.1    Hiller, S.2    Etzkorn, M.3    Wagner, G.4
  • 125
    • 84911003438 scopus 로고    scopus 로고
    • Etudes structurales et dynamiques de la protéine membranaire KpOmpA par RMN en phase liquide et solide
    • Renault M (2008) Etudes structurales et dynamiques de la protéine membranaire KpOmpA par RMN en phase liquide et solide. Ph. D. Thesis, Université Paul Sabatier, Toulouse, 180 p
    • (2008) Ph. D. Thesis, Université Paul Sabatier, Toulouse , pp. 180
    • Renault, M.1
  • 128
    • 84876344621 scopus 로고    scopus 로고
    • Close allies in membrane protein research: cell-free synthesis and nanotechnology
    • PID: 23343215, COI: 1:CAS:528:DC%2BC3sXmtlaitLs%3D
    • Shadiac N, Nagarajan Y, Waters S, Hrmova M (2013) Close allies in membrane protein research: cell-free synthesis and nanotechnology. Mol Membr Biol 30:229–245
    • (2013) Mol Membr Biol , vol.30 , pp. 229-245
    • Shadiac, N.1    Nagarajan, Y.2    Waters, S.3    Hrmova, M.4
  • 129
    • 62649087567 scopus 로고    scopus 로고
    • Glucose-based amphiphilic telomers designed to keep membrane proteins soluble in aqueous solutions: synthesis and physicochemical characterization
    • PID: 18980351, COI: 1:CAS:528:DC%2BD1cXhtlant7vL
    • Sharma KS, Durand G, Giusti F, Olivier B, Fabiano A-S, Bazzacco P, Dahmane T, Ebel C, Popot J-L, Pucci B (2008) Glucose-based amphiphilic telomers designed to keep membrane proteins soluble in aqueous solutions: synthesis and physicochemical characterization. Langmuir 24:13581–13590
    • (2008) Langmuir , vol.24 , pp. 13581-13590
    • Sharma, K.S.1    Durand, G.2    Giusti, F.3    Olivier, B.4    Fabiano, A.-S.5    Bazzacco, P.6    Dahmane, T.7    Ebel, C.8    Popot, J.-L.9    Pucci, B.10
  • 131
    • 34250365394 scopus 로고    scopus 로고
    • The local phospholipid environment modulates the activation of blood clotting
    • PID: 17200119, COI: 1:CAS:528:DC%2BD2sXitVCisbc%3D
    • Shaw AW, Pureza VS, Sligar SG, Morrissey JH (2007) The local phospholipid environment modulates the activation of blood clotting. J Biol Chem 282:6556–6563
    • (2007) J Biol Chem , vol.282 , pp. 6556-6563
    • Shaw, A.W.1    Pureza, V.S.2    Sligar, S.G.3    Morrissey, J.H.4
  • 134
    • 84911006230 scopus 로고
    • Swift J () Travels into Several Remote Nations of the World. In Four Parts. By Lemuel Gulliver, first a surgeon, and then a captain of several ships Benjamin Motte, London
    • Swift J (1726) Travels into Several Remote Nations of the World. In Four Parts. By Lemuel Gulliver, first a surgeon, and then a captain of several ships Benjamin Motte, London
    • (1726)
  • 136
    • 79958151390 scopus 로고    scopus 로고
    • Amphipols stabilize the Chlamydia major outer membrane protein and enhance its protective ability as a vaccine
    • PID: 21550371, COI: 1:CAS:528:DC%2BC3MXntlGgtrw%3D
    • Tifrea DF, Sun G, Pal S, Zardeneta G, Cocco MJ, Popot J-L, de la Maza LM (2011) Amphipols stabilize the Chlamydia major outer membrane protein and enhance its protective ability as a vaccine. Vaccine 29:4623–4631
    • (2011) Vaccine , vol.29 , pp. 4623-4631
    • Tifrea, D.F.1    Sun, G.2    Pal, S.3    Zardeneta, G.4    Cocco, M.J.5    Popot, J.-L.6    de la Maza, L.M.7
  • 137
    • 84901280813 scopus 로고    scopus 로고
    • Increased immuno accessibility of MOMP epitopes in a vaccine formulated with amphipols may account for the very robust protection elicited against a vaginal challenge with C. muridarum
    • Tifrea D, Pal S, Cocco MJ, Popot J-L, de la Maza LM (2014) Increased immuno accessibility of MOMP epitopes in a vaccine formulated with amphipols may account for the very robust protection elicited against a vaginal challenge with C. muridarum. J Immunol 192:5201–5213
    • (2014) J Immunol , vol.192 , pp. 5201-5213
    • Tifrea, D.1    Pal, S.2    Cocco, M.J.3    Popot, J.-L.4    de la Maza, L.M.5
  • 138
    • 37149027535 scopus 로고    scopus 로고
    • Flexible macromolecules attached to lipid bilayers: impact on fluidity, curvature, permeability and stability of the membranes
    • COI: 1:CAS:528:DC%2BD2sXhsVSrs7vI
    • Tribet C, Vial F (2008) Flexible macromolecules attached to lipid bilayers: impact on fluidity, curvature, permeability and stability of the membranes. Soft Matter 4:68–81
    • (2008) Soft Matter , vol.4 , pp. 68-81
    • Tribet, C.1    Vial, F.2
  • 139
    • 0030451437 scopus 로고    scopus 로고
    • Amphipols: polymers that keep membrane proteins soluble in aqueous solutions
    • PID: 8986761, COI: 1:CAS:528:DyaK2sXmslyq
    • Tribet C, Audebert R, Popot J-L (1996) Amphipols: polymers that keep membrane proteins soluble in aqueous solutions. Proc Natl Acad Sci USA 93:15047–15050
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 15047-15050
    • Tribet, C.1    Audebert, R.2    Popot, J.-L.3
  • 140
    • 0031249290 scopus 로고    scopus 로고
    • Stabilization of hydrophobic colloidal dispersions in water with amphiphilic polymers: application to integral membrane proteins
    • COI: 1:CAS:528:DyaK2sXmtF2lu7o%3D
    • Tribet C, Audebert R, Popot J-L (1997) Stabilization of hydrophobic colloidal dispersions in water with amphiphilic polymers: application to integral membrane proteins. Langmuir 13:5570–5576
    • (1997) Langmuir , vol.13 , pp. 5570-5576
    • Tribet, C.1    Audebert, R.2    Popot, J.-L.3
  • 142
    • 70449377616 scopus 로고    scopus 로고
    • Thermodynamic characterization of the exchange of detergents and amphipols at the surfaces of integral membrane proteins
    • PID: 19594168, COI: 1:CAS:528:DC%2BD1MXosVGjsrc%3D
    • Tribet C, Diab C, Dahmane T, Zoonens M, Popot J-L, Winnik FM (2009) Thermodynamic characterization of the exchange of detergents and amphipols at the surfaces of integral membrane proteins. Langmuir 25:12623–12634
    • (2009) Langmuir , vol.25 , pp. 12623-12634
    • Tribet, C.1    Diab, C.2    Dahmane, T.3    Zoonens, M.4    Popot, J.-L.5    Winnik, F.M.6
  • 143
    • 84877580457 scopus 로고    scopus 로고
    • Molecular organization and ATP-induced conformational changes of ABCA4, the photoreceptor-specific ABC transporter
    • PID: 23562398, COI: 1:CAS:528:DC%2BC3sXlsFalurs%3D
    • Tsybovsky Y, Orban T, Molday RS, Taylor D, Palczewski K (2013) Molecular organization and ATP-induced conformational changes of ABCA4, the photoreceptor-specific ABC transporter. Structure 21:854–860
    • (2013) Structure , vol.21 , pp. 854-860
    • Tsybovsky, Y.1    Orban, T.2    Molday, R.S.3    Taylor, D.4    Palczewski, K.5
  • 145
    • 84876703803 scopus 로고    scopus 로고
    • 3D imaging and quantitative analysis of small solubilized membrane proteins and their complexes by transmission electron microscopy
    • PID: 23267047, COI: 1:CAS:528:DC%2BC3sXlvVKiur0%3D
    • Vahedi-Faridi A, Jastrzebska B, Palczewski K, Engel A (2013) 3D imaging and quantitative analysis of small solubilized membrane proteins and their complexes by transmission electron microscopy. Microscopy 62:95–107
    • (2013) Microscopy , vol.62 , pp. 95-107
    • Vahedi-Faridi, A.1    Jastrzebska, B.2    Palczewski, K.3    Engel, A.4
  • 146
    • 13244258531 scopus 로고    scopus 로고
    • Association of octyl-modified poly(acrylic acid) onto unilamellar vesicles of lipids and kinetics of vesicle disruption
    • PID: 15667160, COI: 1:CAS:528:DC%2BD2cXhtFCiurjL
    • Vial F, Rabhi S, Tribet C (2005) Association of octyl-modified poly(acrylic acid) onto unilamellar vesicles of lipids and kinetics of vesicle disruption. Langmuir 21:853–862
    • (2005) Langmuir , vol.21 , pp. 853-862
    • Vial, F.1    Rabhi, S.2    Tribet, C.3
  • 147
    • 33845519363 scopus 로고    scopus 로고
    • Long-living channels of well defined radius opened in lipid bilayers by polydisperse, hydrophobically-modified polyacrylic acids
    • COI: 1:CAS:528:DC%2BD2sXks1Kgsrg%3D
    • Vial F, Oukhaled AG, Auvray L, Tribet C (2007) Long-living channels of well defined radius opened in lipid bilayers by polydisperse, hydrophobically-modified polyacrylic acids. Soft Matter 3:75–78
    • (2007) Soft Matter , vol.3 , pp. 75-78
    • Vial, F.1    Oukhaled, A.G.2    Auvray, L.3    Tribet, C.4
  • 148
    • 67650075577 scopus 로고    scopus 로고
    • Rate of permeabilization of giant vesicles by amphiphilic polyacrylates compared to the adsorption of these polymers onto large vesicles and tethered lipid bilayers
    • PID: 19371041, COI: 1:CAS:528:DC%2BD1MXksFymtbY%3D
    • Vial F, Cousin F, Bouteiller L, Tribet C (2009) Rate of permeabilization of giant vesicles by amphiphilic polyacrylates compared to the adsorption of these polymers onto large vesicles and tethered lipid bilayers. Langmuir 25:7506–7513
    • (2009) Langmuir , vol.25 , pp. 7506-7513
    • Vial, F.1    Cousin, F.2    Bouteiller, L.3    Tribet, C.4
  • 150
    • 35148869587 scopus 로고    scopus 로고
    • Progress in miniaturization of protein arrays-a step closer to high-density nanoarrays
    • PID: 17933681, COI: 1:CAS:528:DC%2BD2sXhtFKitrfK
    • Wingren C, Borrebaeck CA (2007) Progress in miniaturization of protein arrays-a step closer to high-density nanoarrays. Drug Discov Today 12:813–818
    • (2007) Drug Discov Today , vol.12 , pp. 813-818
    • Wingren, C.1    Borrebaeck, C.A.2
  • 151
    • 0032470010 scopus 로고    scopus 로고
    • Conformation of the C-terminal secretion signal of the Serratia marcescens haem acquisition protein (HasA) in amphipols solution, a new class of surfactant
    • Wolff N, Delepierre M (1997) Conformation of the C-terminal secretion signal of the Serratia marcescens haem acquisition protein (HasA) in amphipols solution, a new class of surfactant. J Chim Phys 95:437–442
    • (1997) J Chim Phys , vol.95 , pp. 437-442
    • Wolff, N.1    Delepierre, M.2
  • 152
    • 32344432994 scopus 로고    scopus 로고
    • Caractérisation des complexes formés entre le domaine transmembranaire de la protéine OmpA et des polymères amphiphiles, les amphipols. Application à l’étude structurale des protéines membranaires par RMN à haute résolution
    • Zoonens M (2004) Caractérisation des complexes formés entre le domaine transmembranaire de la protéine OmpA et des polymères amphiphiles, les amphipols. Application à l’étude structurale des protéines membranaires par RMN à haute résolution. Ph. D. Thesis, Paris-6, Paris, 233 p
    • (2004) Ph. D. Thesis, Paris-6, Paris , pp. 233
    • Zoonens, M.1
  • 153
    • 21144446624 scopus 로고    scopus 로고
    • NMR study of a membrane protein in detergent-free aqueous solution
    • PID: 15956183, COI: 1:CAS:528:DC%2BD2MXlvF2qurg%3D
    • Zoonens M, Catoire LJ, Giusti F, Popot J-L (2005) NMR study of a membrane protein in detergent-free aqueous solution. Proc Natl Acad Sci USA 102:8893–8898
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 8893-8898
    • Zoonens, M.1    Catoire, L.J.2    Giusti, F.3    Popot, J.-L.4
  • 154
    • 35148874303 scopus 로고    scopus 로고
    • Dynamics of membrane protein/amphipol association studied by Förster resonance energy transfer. Implications for in vitro studies of amphipol-stabilized membrane proteins
    • PID: 17705558, COI: 1:CAS:528:DC%2BD2sXpt1Wisb0%3D
    • Zoonens M, Giusti F, Zito F, Popot J-L (2007) Dynamics of membrane protein/amphipol association studied by Förster resonance energy transfer. Implications for in vitro studies of amphipol-stabilized membrane proteins. Biochemistry 46:10392–10404
    • (2007) Biochemistry , vol.46 , pp. 10392-10404
    • Zoonens, M.1    Giusti, F.2    Zito, F.3    Popot, J.-L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.