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Volumn 40, Issue 1, 2011, Pages 379-408

Amphipols from a to Z*

Author keywords

amphipathic polymers; membrane biochemistry; membrane biophysics; membrane proteins

Indexed keywords

AMPHIPOLS; MEMBRANE PROTEIN; POLYMER; UNCLASSIFIED DRUG;

EID: 79955806971     PISSN: 1936122X     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev-biophys-042910-155219     Document Type: Article
Times cited : (205)

References (101)
  • 6
    • 72449183187 scopus 로고    scopus 로고
    • Trapping and stabilization of integral membrane proteins by hydrophobically grafted glucose-based telomers
    • Bazzacco P, Sharma KS, Durand G, Giusti F, Ebel C, et al. 2009. Trapping and stabilization of integral membrane proteins by hydrophobically grafted glucose-based telomers. Biomacromolecules 10:3317-26
    • (2009) Biomacromolecules , vol.10 , pp. 3317-3326
    • Bazzacco, P.1    Sharma, K.S.2    Durand, G.3    Giusti, F.4    Ebel, C.5
  • 7
    • 4744351698 scopus 로고    scopus 로고
    • Cell-free synthesis of a functional ion channel in the absence of a membrane and in the presence of detergent
    • DOI 10.1021/bi049049y
    • Berrier C, Park K-H, Abes S, Bibonne A, Betton J-M, Ghazi A. 2004. Cell-free synthesis of a functional ion channel in the absence of a membrane and in the presence of detergent. Biochemistry 43:12585-91 (Pubitemid 39314720)
    • (2004) Biochemistry , vol.43 , Issue.39 , pp. 12585-12591
    • Berrier, C.1    Park, K.-H.2    Abes, S.3    Bibonne, A.4    Betton, J.-M.5    Ghazi, A.6
  • 9
    • 0032693817 scopus 로고    scopus 로고
    • Micropatterned immobilization of a G protein-coupled receptor and direct detection of G protein activation
    • DOI 10.1038/15090
    • Bieri C, Ernst OP, Heyse S, Hofmann KP, Vogel H. 1999. Micropatterned immobilization of a G protein-coupled receptor and direct detection of G protein activation. Nat. Biotechnol. 17:1105-8 (Pubitemid 29533551)
    • (1999) Nature Biotechnology , vol.17 , Issue.11 , pp. 1105-1108
    • Bieri, C.1    Ernst, O.P.2    Heyse, S.3    Hofmann, K.P.4    Vogel, H.5
  • 10
    • 73849149844 scopus 로고    scopus 로고
    • Ligand-specific regulation of the extracellular surface of a G-protein-coupled receptor
    • Bokoch MP, Zou Y, Rasmussen SG, Liu CW, Nygaard R, et al. 2010. Ligand-specific regulation of the extracellular surface of a G-protein-coupled receptor. Nature 463:108-12
    • (2010) Nature , vol.463 , pp. 108-112
    • Bokoch, M.P.1    Zou, Y.2    Rasmussen, S.G.3    Liu, C.W.4    Nygaard, R.5
  • 11
    • 69349089410 scopus 로고    scopus 로고
    • Micellar and biochemical properties of (hemi)fluorinated surfactants are controlled by the size of the polar head
    • Breyton C, Gabel F, Abla M, Pierre Y, Lebaupain F, et al. 2009. Micellar and biochemical properties of (hemi)fluorinated surfactants are controlled by the size of the polar head. Biophys. J. 97:1077-86
    • (2009) Biophys. J. , vol.97 , pp. 1077-1086
    • Breyton, C.1    Gabel, F.2    Abla, M.3    Pierre, Y.4    Lebaupain, F.5
  • 12
    • 77950465278 scopus 로고    scopus 로고
    • Amphipols and fluorinated surfactants: Two alternatives to detergents for studying membrane proteins in vitro
    • ed. I Mus-Veteau Totowa, NJ: Humana
    • Breyton C, Pucci B, Popot J-L. 2010. Amphipols and fluorinated surfactants: two alternatives to detergents for studying membrane proteins in vitro. In Heterologous Expression of Membrane Proteins: Methods and Protocols, ed. I Mus-Veteau, pp. 219-45. Totowa, NJ: Humana
    • (2010) Heterologous Expression of Membrane Proteins: Methods and Protocols , pp. 219-245
    • Breyton, C.1    Pucci, B.2    Popot, J.-L.3
  • 14
    • 0033178531 scopus 로고    scopus 로고
    • β-barrel proteins from bacterial outer membranes: Structure, function and refolding
    • DOI 10.1016/S0959-440X(99)80064-5
    • Buchanan SK. 1999. Beta-barrel proteins from bacterial outer membranes: structure, function and refolding. Curr. Opin. Struct. Biol. 9:455-61 (Pubitemid 29377888)
    • (1999) Current Opinion in Structural Biology , vol.9 , Issue.4 , pp. 455-461
    • Buchanan, S.K.1
  • 15
    • 84934436148 scopus 로고    scopus 로고
    • Cell-free expression for nano-lipoprotein particles: Building a high-throughput membrane protein solubility platform
    • Cappuccio JA, Hinz AK, Kuhn EA, Fletcher JE, Arroyo ES, et al. 2009. Cell-free expression for nano-lipoprotein particles: building a high-throughput membrane protein solubility platform. Methods Mol. Biol. 498:273-96
    • (2009) Methods Mol. Biol. , vol.498 , pp. 273-296
    • Cappuccio, J.A.1    Hinz, A.K.2    Kuhn, E.A.3    Fletcher, J.E.4    Arroyo, E.S.5
  • 18
    • 60349095580 scopus 로고    scopus 로고
    • Inter- and intramolecular contacts in a membrane protein/surfactant complex observed by heteronuclear dipole-to-dipole cross-relaxation
    • 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
  • 20
    • 0019168472 scopus 로고
    • Functional properties of the acetylcholine receptor protein
    • Changeux J-P, Giraudat J, Heidmann T, Popot J-L, Sobel A. 1980. Functional properties of the acetyl-choline receptor protein. Neurochem. Int. 2:219-31 (Pubitemid 11180945)
    • (1980) Neurochemistry International , vol.VOL. 2 , pp. 219-231
    • Changeux, J.P.1    Giraudat, J.2    Heidmann, T.3
  • 21
    • 58849151738 scopus 로고    scopus 로고
    • The use of amphipols as universal molecular adapters to immobilize membrane proteins onto solid supports
    • Charvolin D, Perez J-B, Rouvière F, Giusti F, Bazzacco P, et al. 2009. The use of amphipols as universal molecular adapters to immobilize membrane proteins onto solid supports. Proc. Natl. Acad. Sci. USA 106:405-10
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 405-410
    • Charvolin, D.1    Perez, J.-B.2    Rouvière, F.3    Giusti, F.4    Bazzacco, P.5
  • 22
    • 77949538692 scopus 로고    scopus 로고
    • Atomic structure and dynamics of pentameric ligand-gated ion channels: New insight from bacterial homologues
    • Corringer P-J, Baaden M, Bocquet N, Delarue M, Dufresne V, et al. 2010. Atomic structure and dynamics of pentameric ligand-gated ion channels: new insight from bacterial homologues. J. Physiol. 588:565-72
    • (2010) J. Physiol. , vol.588 , pp. 565-572
    • Corringer, P.-J.1    Baaden, M.2    Bocquet, N.3    Delarue, M.4    Dufresne, V.5
  • 25
    • 36048943576 scopus 로고    scopus 로고
    • Complexation of integral membrane proteins by phosphorylcholine-based amphipols
    • DOI 10.1016/j.bbamem.2007.07.007, PII S0005273607002489
    • Diab C, Tribet C, Gohon Y, Popot J-L, Winnik FM. 2007. Complexation of integral membrane proteins by phosphorylcholine-based amphipols. Biochim. Biophys. Acta 1768:2737-47 (Pubitemid 350081033)
    • (2007) Biochimica et Biophysica Acta - Biomembranes , vol.1768 , Issue.11 , pp. 2737-2747
    • Diab, C.1    Tribet, C.2    Gohon, Y.3    Popot, J.-L.4    Winnik, F.M.5
  • 26
    • 33947425242 scopus 로고    scopus 로고
    • Enthalpy of interaction and binding isotherms of non-ionic surfactants onto micellar amphiphilic polymers (amphipols)
    • DOI 10.1021/la062522j
    • Diab C, Winnik FM, Tribet C. 2007. Enthalpy of interaction and binding isotherms of nonionic surfactants onto micellar amphiphilic polymers (amphipols). Langmuir 23:3025-35 (Pubitemid 46450130)
    • (2007) Langmuir , vol.23 , Issue.6 , pp. 3025-3035
    • Diab, C.1    Winnik, F.M.2    Tribet, C.3
  • 28
    • 34548329761 scopus 로고    scopus 로고
    • The use of amphipathic polymers for cryo electron microscopy of NADH:ubiquinone oxidoreductase (complex I)
    • DOI 10.1111/j.1365-2818.2007.01805.x
    • 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. 227:229-35 (Pubitemid 47339674)
    • (2007) Journal of Microscopy , vol.227 , Issue.3 , pp. 229-235
    • Flotenmeyer, M.1    Weiss, H.2    Tribet, C.3    Popot, J.-L.4    Leonard, K.5
  • 32
    • 43649083325 scopus 로고    scopus 로고
    • Bacteri-orhodopsin/amphipol complexes: Structural and functional properties
    • Gohon Y, Dahmane T, Ruigrok R, Schuck P, Charvolin D, et al. 2008. Bacteri-orhodopsin/amphipol complexes: structural and functional properties. Biophys. J. 94:3523-37
    • (2008) Biophys. J. , vol.94 , pp. 3523-3537
    • Gohon, Y.1    Dahmane, T.2    Ruigrok, R.3    Schuck, P.4    Charvolin, D.5
  • 33
    • 32344431772 scopus 로고    scopus 로고
    • Well-defined nanoparticles formed by hydrophobic assembly of a short and polydisperse random terpolymer, amphipol A8-35
    • DOI 10.1021/la052243g
    • Gohon Y, Giusti F, Prata C, Charvolin D, Timmins P, et al. 2006. Well-defined nanoparticles formed by hydrophobic assembly of a short and polydisperse random terpolymer, amphipol A8-35. Langmuir 22:1281-90 (Pubitemid 43282189)
    • (2006) Langmuir , vol.22 , Issue.3 , 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
  • 34
    • 5644275289 scopus 로고    scopus 로고
    • Partial specific volume and solvent interactions of amphipol A8-35
    • DOI 10.1016/j.ab.2004.07.033, PII S0003269704006451
    • 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. 334:318-34 (Pubitemid 39370968)
    • (2004) Analytical Biochemistry , vol.334 , Issue.2 , pp. 318-334
    • Gohon, Y.1    Pavlov, G.2    Timmins, P.3    Tribet, C.4    Popot, J.-L.5    Ebel, C.6
  • 37
    • 0033534176 scopus 로고    scopus 로고
    • Reconstitutive refolding of diacylglycerol kinase, an integral membrane protein
    • Gorzelle BM, Nagy JK, Oxenoid K, Lonzer WL, Cafiso DS, Sanders CR. 1999. Reconstitutive refolding of diacylglycerol kinase, an integral membrane protein. Biochemistry 38:16373-82 (Pubitemid 129520561)
    • (1999) Biochemistry , vol.38 , Issue.49 , pp. 16373-16382
    • Gorzelle, B.M.1    Nagy, J.K.2    Oxenoid, K.3    Lonzer, W.L.4    Cafiso, D.S.5    Sanders, C.R.6
  • 38
    • 23444448243 scopus 로고    scopus 로고
    • Adding value to fusion proteins through covalent labelling
    • DOI 10.1016/j.copbio.2005.06.001, PII S0958166905000923, Protein Technologies and Commercial Enzymes
    • Gronemeyer T, Godin G, Johnsson K. 2005. Adding value to fusion proteins through covalent labelling. Curr. Opin. Struct. Biol. 16:453-58 (Pubitemid 41111532)
    • (2005) Current Opinion in Biotechnology , vol.16 , Issue.4 , pp. 453-458
    • Gronemeyer, T.1    Godin, G.2    Johnsson, K.3
  • 39
    • 58149242730 scopus 로고    scopus 로고
    • Structure of a potentially open state of a proton-activated pentameric ligand-gated ion channel
    • Hilf RJ, Dutzler R. 2009. Structure of a potentially open state of a proton-activated pentameric ligand-gated ion channel. Nature 457:115-18
    • (2009) Nature , vol.457 , pp. 115-118
    • Hilf, R.J.1    Dutzler, R.2
  • 40
    • 69249098842 scopus 로고    scopus 로고
    • Structural snapshots of conformational changesinaseven-helix membrane protein: Lessons from bacteriorhodopsin
    • HiraiT,SubramaniamS, Lanyi JK. 2009. Structural snapshots of conformational changesinaseven-helix membrane protein: lessons from bacteriorhodopsin. Curr. Opin. Struct. Biol. 19:433-39
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 433-439
    • Hirai, T.1    Subramaniam, S.2    Lanyi, J.K.3
  • 42
    • 0019887931 scopus 로고
    • Refolding of an integral membrane protein. Denaturation, renaturation, and reconstitution of intact bacteriorhodopsin and two proteolytic fragments
    • Huang K-S, Bayley H, Liao M-J, London E, Khorana HG. 1981. Refolding of an integral membrane protein. Denaturation, renaturation, and reconstitution of intact bacteriorhodopsin and two proteolytic fragments. J. Biol. Chem. 256:3802-9
    • (1981) J. Biol. Chem. , vol.256 , pp. 3802-9
    • Huang, K.-S.1    Bayley, H.2    Liao, M.-J.3    London, E.4    Khorana, H.G.5
  • 43
    • 77953584951 scopus 로고    scopus 로고
    • Single-spanning transmembrane domains in cell growth and cell-cell interactions: More than meets the eye?
    • Hubert P, Sawma P, Duneau J-P, Khao J, Henin J, et al. 2010. Single-spanning transmembrane domains in cell growth and cell-cell interactions: more than meets the eye? Cell Adh. Migr. 4:313-24
    • (2010) Cell Adh. Migr. , vol.4 , pp. 313-324
    • Hubert, P.1    Sawma, P.2    Duneau, J.-P.3    Khao, J.4    Henin, J.5
  • 44
    • 79955813489 scopus 로고    scopus 로고
    • Advances in cell-free protein synthesis for the functional and structural analysis of membrane proteins
    • Epub ahead of print
    • Junge F, Haberstock S, Roos C, Stefer S, Proverbio D, et al. 2010. Advances in cell-free protein synthesis for the functional and structural analysis of membrane proteins. N. Biotechnol. Epub ahead of print
    • (2010) N. Biotechnol.
    • Junge, F.1    Haberstock, S.2    Roos, C.3    Stefer, S.4    Proverbio, D.5
  • 45
    • 77956188838 scopus 로고    scopus 로고
    • Modulation of G-protein coupled receptor sample quality by modified cell-free expression protocols: A case study of the human endothelin A receptor
    • Junge F, Luh LM, Proverbio D, Schäfer B, Abele R, et al. 2010. Modulation of G-protein coupled receptor sample quality by modified cell-free expression protocols: a case study of the human endothelin A receptor. J. Struct. Biol. 172:94-106
    • (2010) J. Struct. Biol. , vol.172 , pp. 94-106
    • Junge, F.1    Luh, L.M.2    Proverbio, D.3    Schäfer, B.4    Abele, R.5
  • 47
    • 0030467888 scopus 로고    scopus 로고
    • Expression of an olfactory receptor in Escherichia coli: Purification, reconstitution, and ligand binding
    • DOI 10.1021/bi9612069
    • Kiefer H, Krieger J, Olszewski JD, von Heijne G, Prestwich GD, Breer H. 1996. Expression of an olfactory receptor in Escherichia coli: purification, reconstitution, and ligand binding. Biochemistry 35:16077-84 (Pubitemid 27044069)
    • (1996) Biochemistry , vol.35 , Issue.50 , pp. 16077-16084
    • Kiefer, H.1    Krieger, J.2    Olszewski, J.D.3    Von Heijne, G.4    Prestwich, G.D.5    Breer, H.6
  • 48
    • 0032923295 scopus 로고    scopus 로고
    • Cell-free production and stable-isotope labeling of milligram quantities of proteins
    • DOI 10.1016/S0014-5793(98)01620-2, PII S0014579398016202
    • Kigawa T, Yabuki T, Yoshida Y, Tsutsui M, Ito Y, et al. 1999. Cell-free production and stable-isotope labeling of milligram quantities of proteins. FEBS Lett. 442:15-19 (Pubitemid 29065369)
    • (1999) FEBS Letters , vol.442 , Issue.1 , pp. 15-19
    • Kigawa, T.1    Yabuki, T.2    Yoshida, Y.3    Tsutsui, M.4    Ito, Y.5    Shibata, T.6    Yokoyama, S.7
  • 49
    • 28244458078 scopus 로고    scopus 로고
    • Evaluation of detergents for the soluble expression of α-helical and β-barrel-type integral membrane proteins by a preparative scale individual cell-free expression system
    • DOI 10.1111/j.1742-4658.2005.05002.x
    • Klammt C, Schwarz D, Fendler K, Haase W, Dötsch V, Bernhard F. 2005. Evaluation of detergents for the soluble expression of alpha-helical and beta-barrel-type integral membrane proteins by a preparative scale individual cell-free expression system. FEBS J. 272:6024-38 (Pubitemid 41713694)
    • (2005) FEBS Journal , vol.272 , Issue.23 , pp. 6024-6038
    • Klammt, C.1    Schwarz, D.2    Fendler, K.3    Haase, W.4    Dotsch, V.5    Bernhard, F.6
  • 50
    • 34347391677 scopus 로고    scopus 로고
    • Functional analysis of cell-free produced human endothelin B receptor reveals transmembrane segment 1 as an essential area for ET-1 binding and homodimer formation
    • Klammt C, Srivastava A, Eifler N, Junge F, Beyermann M, et al. 2007. Functional analysis of cell-free produced human endothelin B receptor reveals transmembrane segment 1 as an essential area for ET-1 binding and homodimer formation. FEBS J. 274:3259-69
    • (2007) FEBS J. , vol.274 , pp. 3259-3269
    • Klammt, C.1    Srivastava, A.2    Eifler, N.3    Junge, F.4    Beyermann, M.5
  • 51
    • 0035450348 scopus 로고    scopus 로고
    • Slow reorganization of small phosphatidylcholine vesicles upon adsorption of amphiphilic polymers
    • DOI 10.1006/jcis.2001.7675
    • Ladavière C, Toustou M, Gulik-Krzywicki T, Tribet C. 2001. Slow reorganization of small phosphatidyl-choline vesicles upon adsorption of amphiphilic polymers. J. Colloid Interface Sci. 241:178-87 (Pubitemid 32786675)
    • (2001) Journal of Colloid and Interface Science , vol.241 , Issue.1 , pp. 178-187
    • Ladaviere, C.1    Toustou, M.2    Gulik-Krzywicki, T.3    Tribet, C.4
  • 52
    • 28844480494 scopus 로고    scopus 로고
    • Effective rotational correlation times of proteins from NMR relaxation interference
    • DOI 10.1016/j.jmr.2005.08.014, PII S1090780705002934
    • Lee D, Hilty C, Wider G, Wüthrich K. 2006. Effective rotational correlation times of proteins from NMR relaxation interference. J. Magn. Reson. 178:72-76 (Pubitemid 41774013)
    • (2006) Journal of Magnetic Resonance , vol.178 , Issue.1 , pp. 72-76
    • Lee, D.1    Hilty, C.2    Wider, G.3    Wuthrich, K.4
  • 54
    • 0037174145 scopus 로고    scopus 로고
    • Allosteric transitions of Torpedo acetylcholine receptor in lipids, detergent and amphipols: Molecular interactions vs. physical constraints
    • DOI 10.1016/S0014-5793(02)03306-9, PII S0014579302033069
    • Martinez KL, Gohon Y, Corringer P-J, Tribet C, Mérola F, et al. 2002. Allosteric transitions of Torpedo acetylcholine receptor in lipids, detergent and amphipols: molecular interactions versus physical constraints. FEBS Lett. 528:251-56 (Pubitemid 35258034)
    • (2002) FEBS Letters , vol.528 , Issue.1-3 , pp. 251-256
    • Martinez, K.L.1    Gohon, Y.2    Corringer, P.-J.3    Tribet, C.4    Merola, F.5    Changeux, J.-P.6    Popot, J.-L.7
  • 55
    • 0348196678 scopus 로고    scopus 로고
    • Ligand binding to G protein-coupled receptors in tethered cell membranes
    • Martinez KL, Meyer BH, Hovius R, Lundstrom K, Vogel H. 2003. Ligand binding to G protein-coupled receptors in tethered cell membranes. Langmuir 19:10925-29
    • (2003) Langmuir , vol.19 , pp. 10925-10929
    • Martinez, K.L.1    Meyer, B.H.2    Hovius, R.3    Lundstrom, K.4    Vogel, H.5
  • 56
    • 33750459691 scopus 로고    scopus 로고
    • Dynamic Helix Interactions in Transmembrane Signaling
    • DOI 10.1016/j.cell.2006.10.016, PII S0092867406013420
    • Matthews EE, Zoonens M, Engelman DM. 2006. Dynamic helix interactions in transmembrane signaling. Cell 127:447-50 (Pubitemid 44647431)
    • (2006) Cell , vol.127 , Issue.3 , pp. 447-450
    • Matthews, E.E.1    Zoonens, M.2    Engelman, D.M.3
  • 57
    • 0028294304 scopus 로고
    • Thermal unfolding of monomeric Ca(II),Mg(II)-ATPase from sarcoplasmic reticulum of rabbit skeletal muscle
    • DOI 10.1016/0014-5793(94)80309-9
    • 2+-ATPase from sarcoplasmic reticulum of rabbit skeletal muscle. FEBS Lett. 343:155-59 (Pubitemid 24126666)
    • (1994) FEBS Letters , vol.343 , Issue.2 , pp. 155-159
    • Merino, J.M.1
  • 60
    • 77951622512 scopus 로고    scopus 로고
    • Peptide-based interference of the trans-membrane domain of neuropilin-1 inhibits glioma growth in vivo
    • Nasarre C, Roth M, Jacob L, Roth L, Koncina E, et al. 2010. Peptide-based interference of the trans-membrane domain of neuropilin-1 inhibits glioma growth in vivo. Oncogene 29:2381-92
    • (2010) Oncogene , vol.29 , pp. 2381-2392
    • Nasarre, C.1    Roth, M.2    Jacob, L.3    Roth, L.4    Koncina, E.5
  • 62
    • 34147158906 scopus 로고    scopus 로고
    • Fluorinated and hemifluorinated surfactants as alternatives to detergents for membrane protein cell-free synthesis
    • DOI 10.1042/BJ20061473
    • Park K-H, Berrier C, Lebaupain F, Pucci B, Popot J-L, et al. 2007. Fluorinated and hemifluorinated surfactants as alternatives to detergents for membrane protein cell-free synthesis. Biochem. J. 403:183-87 (Pubitemid 46569880)
    • (2007) Biochemical Journal , vol.403 , Issue.1 , 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
  • 63
    • 79953707602 scopus 로고    scopus 로고
    • In the cauldronofcell-free synthesis ofmembrane proteins: Playing with new surfactants
    • doi:10.1016/j.nbt.2010.08.008
    • Park K-H, Billon-DenisE,DahmaneT,LebaupainF,Pucci B,etal. 2010.Inthe cauldronofcell-free synthesis ofmembrane proteins: playing with new surfactants. New Biotechnol.doi:10.1016/j.nbt.2010.08.008
    • (2010) New Biotechnol.
    • Park, K.-H.1    Billon-Denis, E.2    Dahmane, T.3    Lebaupain, F.4    Pucci, B.5
  • 65
    • 7244231305 scopus 로고    scopus 로고
    • Stabilization of membranes upon interaction of amphipathic polymers with membrane proteins
    • DOI 10.1110/ps.04962104
    • Picard M, Duval-Terrié C, Dé E, Champeil P. 2004. Stabilization of membranes upon interaction of amphipathic polymers with membrane proteins. Protein Sci. 13:3056-58 (Pubitemid 39433396)
    • (2004) Protein Science , vol.13 , Issue.11 , pp. 3056-3058
    • Picard, M.1    Duval-Terrie, C.2    De, E.3    Champeil, P.4
  • 67
    • 77953627340 scopus 로고    scopus 로고
    • Amphipols, nanodiscs, and fluorinated surfactants: Three non-conventional approaches to studying membrane proteins in aqueous solutions
    • Popot J-L. 2010. Amphipols, nanodiscs, and fluorinated surfactants: three non-conventional approaches to studying membrane proteins in aqueous solutions. Annu. Rev. Biochem. 79:737-75
    • (2010) Annu. Rev. Biochem. , vol.79 , pp. 737-775
    • Popot, J.-L.1
  • 69
    • 0023583873 scopus 로고
    • Refolding of bacteriorhodopsin in lipid bilayers. A thermodynamically controlled two-stage process
    • Popot J-L, Gerchman S-E, Engelman DM. 1987. Refolding of bacteriorhodopsin in lipid bilayers: a thermodynamically controlled two-stage process. J. Mol. Biol. 198:655-76 (Pubitemid 18034980)
    • (1987) Journal of Molecular Biology , vol.198 , Issue.4 , pp. 655-676
    • Popot, J.-L.1    Gerchman, S.-E.2    Engelman, D.M.3
  • 70
    • 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
    • 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
  • 72
    • 79953702800 scopus 로고    scopus 로고
    • Production of membrane proteins without cells or detergents
    • doi:10.1016/j.nbt.2010.07.011
    • Rajesh S, Knowles TJ, Overduin M. 2010. Production of membrane proteins without cells or detergents. New Biotechnol. doi:10.1016/j.nbt.2010.07.011
    • (2010) New Biotechnol.
    • Rajesh, S.1    Knowles, T.J.2    Overduin, M.3
  • 75
    • 0034700305 scopus 로고    scopus 로고
    • Folding, assembly, and stability of the major light-harvesting complex of higher plants, LHCII, in the presence of native lipids
    • Reinsberg D, Booth PJ, Jegerschöld C, Khoo BJ, Paulsen H. 2000. Folding, assembly, and stability of the major light-harvesting complex of higher plants, LHCII, in the presence of native lipids. Biochemistry 39:14305-13
    • (2000) Biochemistry , vol.39 , pp. 14305-14313
    • Reinsberg, D.1    Booth, P.J.2    Jegerschöld, C.3    Khoo, B.J.4    Paulsen, H.5
  • 78
    • 65749112991 scopus 로고    scopus 로고
    • Plasmon resonance methods in membrane protein biology: Applications to GPCR signaling
    • Salamon Z, Tollin G, Alves I, Hruby V. 2009. Plasmon resonance methods in membrane protein biology: applications to GPCR signaling. Methods Enzymol. 461:123-46
    • (2009) Methods Enzymol. , vol.461 , pp. 123-146
    • Salamon, Z.1    Tollin, G.2    Alves, I.3    Hruby, V.4
  • 81
    • 55749110716 scopus 로고    scopus 로고
    • Production of membrane protein using cell-free expression system
    • Schwarz D, Dötsch V, Bernhard F. 2008. Production of membrane protein using cell-free expression system. Proteomics 8:3933-46
    • (2008) Proteomics , vol.8 , pp. 3933-3946
    • Schwarz, D.1    Dötsch, V.2    Bernhard, F.3
  • 82
    • 77957931096 scopus 로고    scopus 로고
    • Permeabilisation of lipid membranes and cells by a light-responsive copolymer
    • Sebai S, Cribier S, Karimi A, Massotte D, Tribet T. 2010. Permeabilisation of lipid membranes and cells by a light-responsive copolymer. Langmuir 26:14135-41
    • (2010) Langmuir , vol.26 , pp. 14135-14141
    • Sebai, S.1    Cribier, S.2    Karimi, A.3    Massotte, D.4    Tribet, T.5
  • 83
    • 62649087567 scopus 로고    scopus 로고
    • Glucose-based amphiphilic telom-ers designed to keep membrane proteins soluble in aqueous solutions: Synthesis and physicochemical characterization
    • Sharma KS, Durand G, Giusti F, Olivier B, Fabiano A-S, et al. 2008. Glucose-based amphiphilic telom-ers designed to keep membrane proteins soluble in aqueous solutions: synthesis and physicochemical characterization. Langmuir 24:13581-90
    • (2008) Langmuir , vol.24 , pp. 13581-13590
    • Sharma, K.S.1    Durand, G.2    Giusti, F.3    Olivier, B.4    Fabiano, A.-S.5
  • 84
    • 0024297305 scopus 로고
    • A continuous cell-free translation system capable of producing polypeptides in high yield
    • Spirin AS, Baranov VI, Ryabova LA, Ovodov SY, Alakhov YB. 1988. A continuous cell-free translation system capable of producing polypeptides in high yield. Science 242:1162-64
    • (1988) Science , vol.242 , pp. 1162-1164
    • Spirin, A.S.1    Baranov, V.I.2    Ryabova, L.A.3    Ovodov, S.Y.4    Alakhov, Y.B.5
  • 85
    • 0037255597 scopus 로고    scopus 로고
    • Overview of tag protein fusions: From molecular and biochemical fundamentals to commercial systems
    • Terpe K. 2003. Overview of tag protein fusions: from molecular and biochemical fundamentals to commercial systems. Appl. Microbiol. Biotechnol. 60:523-33 (Pubitemid 36169526)
    • (2003) Applied Microbiology and Biotechnology , vol.60 , Issue.5 , pp. 523-533
    • Terpe, K.1
  • 86
    • 0034621834 scopus 로고    scopus 로고
    • Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 A? resolution
    • DOI 10.1038/35015017
    • Toyoshima C, Nakasako M, Nomura H, Ogawa H. 2000. Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 A? resolution. Nature 405:647-55 (Pubitemid 30428644)
    • (2000) Nature , vol.405 , Issue.6787 , pp. 647-655
    • Toyoshima, C.1    Nakasako, M.2    Nomura, H.3    Ogawa, H.4
  • 88
    • 0031249290 scopus 로고    scopus 로고
    • Stabilization of hydrophobic colloidal dispersions in water with amphiphilic polymers: Application to integral membrane proteins
    • Tribet C, Audebert R, Popot J-L. 1997. Stabilisation of hydrophobic colloidal dispersions in water with amphiphilic polymers: application to integral membrane proteins. Langmuir 13:5570-76 (Pubitemid 127591952)
    • (1997) Langmuir , vol.13 , Issue.21 , pp. 5570-5576
    • Tribet, C.1    Audebert, R.2    Popot, J.-L.3
  • 89
    • 70449377616 scopus 로고    scopus 로고
    • Thermodynamic characterization of the exchange of detergents and amphipols at the surfaces of integral membrane proteins
    • 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 25:12623-34
    • (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
  • 91
    • 44049103958 scopus 로고    scopus 로고
    • Residence time of receptor - Ligand complexes and its effect on biological function
    • DOI 10.1021/bi8002023
    • Tummino PJ, Copeland RA. 2008. Residence time of receptor-ligand complexes and its effect on biological function. Biochemistry 47:5481-92 (Pubitemid 351711169)
    • (2008) Biochemistry , vol.47 , Issue.20 , pp. 5481-5492
    • Tummino, P.J.1    Copeland, R.A.2
  • 92
    • 67650075577 scopus 로고    scopus 로고
    • Rate of permeabilization of giant vesicles by amphiphilic polyacrylates comparedto the adsorption of these polymers onto large vesicles and tethered lipid bilayers
    • Vial F, Cousin F, Bouteiller L, Tribet C. 2009. Rate of permeabilization of giant vesicles by amphiphilic polyacrylates comparedto the adsorption of these polymers onto large vesicles and tethered lipid bilayers. Langmuir 25:7506-13
    • (2009) Langmuir , vol.25 , pp. 7506-7513
    • Vial, F.1    Cousin, F.2    Bouteiller, L.3    Tribet, C.4
  • 93
    • 33845519363 scopus 로고    scopus 로고
    • Long-living channels of well defined radius opened in lipid bilayers by polydisperse, hydrophobically-modified polyacrylic acids
    • DOI 10.1039/b613003h
    • 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 (Pubitemid 44925793)
    • (2007) Soft Matter , vol.3 , Issue.1 , pp. 75-78
    • Vial, F.1    Oukhaled, A.G.2    Auvray, L.3    Tribet, C.4
  • 94
    • 13244258531 scopus 로고    scopus 로고
    • Association of octyl-modified poly(acrylic acid) onto unilamellar vesicles of lipids and kinetics of vesicle disruption
    • DOI 10.1021/la048039v
    • 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 21:853-62 (Pubitemid 40184781)
    • (2005) Langmuir , vol.21 , Issue.3 , pp. 853-862
    • Vial, F.1    Rabhi, S.2    Tribet, C.3
  • 95
    • 70349671196 scopus 로고    scopus 로고
    • Applications of protein biochips in biomedical and biotechnological research
    • Weinrich D, Jonkheijm P, Niemeyer CM, Waldmann H. 2009. Applications of protein biochips in biomedical and biotechnological research. Angew. Chem. Int. Ed. 48:7744-51
    • (2009) Angew. Chem. Int. Ed. , vol.48 , pp. 7744-7751
    • Weinrich, D.1    Jonkheijm, P.2    Niemeyer, C.M.3    Waldmann, H.4
  • 96
    • 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. 95:437-42
    • (1997) J. Chim. Phys. , vol.95 , pp. 437-442
    • Wolff, N.1    Delepierre, M.2
  • 97
    • 33750595486 scopus 로고    scopus 로고
    • Label-free detection methods for protein microarrays
    • DOI 10.1002/pmic.200600216
    • Yu XB, Xu DK, Cheng Q. 2006. Label-free detection methods for protein microarrays. Proteomics 6:5493-503 (Pubitemid 44683217)
    • (2006) Proteomics , vol.6 , Issue.20 , pp. 5493-5503
    • Yu, X.1    Xu, D.2    Cheng, Q.3
  • 98
    • 32344432994 scopus 로고    scopus 로고
    • Caractérisation des complexes formes entre le domaine transmembranaire de la proteine OmpA et des polymeres amphiphiles, les amphipols
    • Doctorat d'Universite. Univ. Paris-VI
    • Zoonens M. 2004. Caractérisation des complexes formes entre le domaine transmembranaire de la proteine OmpA et des polymeres amphiphiles, les amphipols. Application a l'étude structurale des proteines membranaires par RMNa haute resolution. Doctorat d'Universite. Univ. Paris-VI. 233 pp.
    • (2004) Application A l'Étude Structurale des Proteines Membranaires Par RMNa Haute Resolution , pp. 233
    • Zoonens, M.1
  • 100
    • 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
    • DOI 10.1021/bi7007596
    • Zoonens M, Giusti F, Zito F, Popot J-L. 2007. Dynamics of membrane protein/amphipol association studied by Forster resonance energy transfer. Implications for in vitro studies of amphipol-stabilized membrane proteins. Biochemistry 46:10392-404 (Pubitemid 350067632)
    • (2007) Biochemistry , vol.46 , Issue.36 , pp. 10392-10404
    • Zoonens, M.1    Giusti, F.2    Zito, F.3    Popot, J.-L.4
  • 101
    • 0015871909 scopus 로고
    • In vitro synthesis of protein in microbial systems
    • Zubay G. 1973. In vitro synthesis of protein in microbial systems. Annu. Rev. Genet. 7:267-87
    • (1973) Annu. Rev. Genet. , vol.7 , pp. 267-287
    • Zubay, G.1


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