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Volumn 247, Issue 9-10, 2014, Pages 1053-1065

Long-Term Stability of a Vaccine Formulated with the Amphipol-Trapped Major Outer Membrane Protein from Chlamydia trachomatis

Author keywords

Amphipols; Chlamydia trachomatis; MOMP; NMR; Stability; Vaccine

Indexed keywords

BACTERIAL VACCINE; MAJOR OUTER MEMBRANE PROTEIN AMPHIPOL VACCINE; UNCLASSIFIED DRUG; DRUG CARRIER; OMPA OUTER MEMBRANE PROTEINS; OUTER MEMBRANE PROTEIN; SURFACTANT;

EID: 84911004807     PISSN: 00222631     EISSN: 14321424     Source Type: Journal    
DOI: 10.1007/s00232-014-9693-5     Document Type: Article
Times cited : (11)

References (71)
  • 1
    • 0028824421 scopus 로고
    • Glycine crystallization during freezing: the effects of salt form, pH, and ionic strength
    • PID: 8584480, COI: 1:CAS:528:DyaK2MXoslerurY%3D
    • Akers MJ, Milton N, Byrn SR, Nail SL (1995) Glycine crystallization during freezing: the effects of salt form, pH, and ionic strength. Pharm Res 12:1457–1461
    • (1995) Pharm Res , vol.12 , pp. 1457-1461
    • Akers, M.J.1    Milton, N.2    Byrn, S.R.3    Nail, S.L.4
  • 2
    • 0020966235 scopus 로고
    • Amino acid requirements of strains of Chlamydia trachomatis and C. psittaci growing in McCoy cells: relationship with clinical syndrome and host origin
    • PID: 6631408, COI: 1:CAS:528:DyaL3sXltF2jtb4%3D
    • Allan I, Pearce JH (1983) Amino acid requirements of strains of Chlamydia trachomatis and C. psittaci growing in McCoy cells: relationship with clinical syndrome and host origin. J Gen Microbiol 129:2001–2007
    • (1983) J Gen Microbiol , vol.129 , pp. 2001-2007
    • Allan, I.1    Pearce, J.H.2
  • 4
    • 0021346648 scopus 로고
    • Purification and partial characterization of the opacity-associated proteins of Neisseria gonorrhoeae
    • PID: 6420502, COI: 1:CAS:528:DyaL2cXhtlGmsrg%3D
    • Blake MS, Gotschlich EC (1984) Purification and partial characterization of the opacity-associated proteins of Neisseria gonorrhoeae. J Exp Med 159:452–462
    • (1984) J Exp Med , vol.159 , pp. 452-462
    • Blake, M.S.1    Gotschlich, E.C.2
  • 5
    • 0035423934 scopus 로고    scopus 로고
    • Stabilizing membrane proteins
    • PID: 11495729, COI: 1:CAS:528:DC%2BD3MXlslGlsbw%3D
    • Bowie JU (2001) Stabilizing membrane proteins. Curr Opin Struct Biol 11:397–402
    • (2001) Curr Opin Struct Biol , vol.11 , pp. 397-402
    • Bowie, J.U.1
  • 7
    • 70350068542 scopus 로고    scopus 로고
    • Biophysical and stabilization studies of the Chlamydia trachomatis mouse pneumonitis major outer membrane protein
    • PID: 19650664, COI: 1:CAS:528:DC%2BD1MXpvV2nsLs%3D
    • Cai S, He F, Samra HS, de la Maza LM, Bottazzi ME, Joshi SB, Middaugh CR (2009) Biophysical and stabilization studies of the Chlamydia trachomatis mouse pneumonitis major outer membrane protein. Mol Pharm 6:1553–1561
    • (2009) Mol Pharm , vol.6 , pp. 1553-1561
    • Cai, S.1    He, F.2    Samra, H.S.3    de la Maza, L.M.4    Bottazzi, M.E.5    Joshi, S.B.6    Middaugh, C.R.7
  • 8
    • 0019514724 scopus 로고
    • Purification and partial characterization of the major outer membrane protein of Chlamydia trachomatis
    • PID: 7228399, COI: 1:CAS:528:DyaL3MXhsFCltLY%3D
    • Caldwell HD, Kromhout J, Schachter J (1981) Purification and partial characterization of the major outer membrane protein of Chlamydia trachomatis. Infect Immun 31:1161–1176
    • (1981) Infect Immun , vol.31 , pp. 1161-1176
    • Caldwell, H.D.1    Kromhout, J.2    Schachter, J.3
  • 9
    • 0038632059 scopus 로고    scopus 로고
    • Effect of freezing and thawing rates on denaturation of proteins in aqueous solutions
    • PID: 12673768, COI: 1:CAS:528:DC%2BD3sXjvFOkurs%3D
    • Cao E, Chen Y, Cui Z, Foster PR (2003) Effect of freezing and thawing rates on denaturation of proteins in aqueous solutions. Biotechnol Bioeng 82:684–690
    • (2003) Biotechnol Bioeng , vol.82 , pp. 684-690
    • Cao, E.1    Chen, Y.2    Cui, Z.3    Foster, P.R.4
  • 10
    • 60349095580 scopus 로고    scopus 로고
    • Inter- and intramolecular contacts in a membrane protein/surfactant complex observed by heteronuclear dipole-to-dipole cross-relaxation
    • PID: 19101186, 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 Reson 197:91–95
    • (2009) J Magn Reson , 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
  • 12
    • 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
  • 13
    • 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 JL (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
  • 15
    • 0030443567 scopus 로고    scopus 로고
    • Surface-induced denaturation of proteins during freezing and its inhibition by surfactants
    • PID: 8961147, COI: 1:CAS:528:DyaK28Xms1Cmt7Y%3D
    • Chang BS, Kendrick BS, Carpenter JF (1996) Surface-induced denaturation of proteins during freezing and its inhibition by surfactants. J Pharm Sci 85:1325–1330
    • (1996) J Pharm Sci , vol.85 , pp. 1325-1330
    • Chang, B.S.1    Kendrick, B.S.2    Carpenter, J.F.3
  • 16
    • 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 JL (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
  • 17
    • 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
  • 18
    • 84879501057 scopus 로고    scopus 로고
    • Amphipol-assisted folding of bacteriorhodopsin in the presence or 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 or 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
  • 19
    • 0029400480 scopus 로고
    • NMRPipe: a multidimensional spectral processing system based on UNIX pipes
    • PID: 8520220, COI: 1:CAS:528:DyaK2MXhtVSmurfK
    • Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6:277–293
    • (1995) J Biomol NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 21
    • 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
  • 22
    • 84908587074 scopus 로고    scopus 로고
    • How amphipols embed membrane proteins: global solvent accessibility and interaction with a flexible protein terminus. J Membr Biol
    • 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) doi:10.1007/s00232-014-9657-9
    • Etzkorn, M.1    Zoonens, M.2    Catoire, L.J.3    Popot, J.-L.4    Hiller, S.5
  • 23
    • 34250703143 scopus 로고    scopus 로고
    • Effects of solutes on empirical phase diagrams of human fibroblast growth factor 1
    • PID: 17094138, COI: 1:CAS:528:DC%2BD2sXmt1Cis78%3D
    • Fan H, Li H, Zhang M, Middaugh CR (2007) Effects of solutes on empirical phase diagrams of human fibroblast growth factor 1. J Pharm Sci 96:1490–1503
    • (2007) J Pharm Sci , vol.96 , pp. 1490-1503
    • Fan, H.1    Li, H.2    Zhang, M.3    Middaugh, C.R.4
  • 24
    • 0011819979 scopus 로고
    • Low-temperature unfolding of chymotrypsinogen
    • Franks F, Hatley RH (1985) Low-temperature unfolding of chymotrypsinogen. Cryobiology 22:608
    • (1985) Cryobiology , vol.22 , pp. 608
    • Franks, F.1    Hatley, R.H.2
  • 25
    • 0035980050 scopus 로고    scopus 로고
    • Detergents as tools in membrane biochemistry
    • PID: 11432878, COI: 1:CAS:528:DC%2BD3MXmvFCnu7g%3D
    • 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
  • 26
    • 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
  • 28
    • 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
  • 29
    • 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
  • 30
    • 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
  • 33
    • 0033857699 scopus 로고    scopus 로고
    • Amino acid transport into cultured McCoy cells infected with Chlamydia trachomatis
    • PID: 10948179, COI: 1:CAS:528:DC%2BD3cXmtVektLo%3D
    • Harper A, Pogson CI, Pearce JH (2000) Amino acid transport into cultured McCoy cells infected with Chlamydia trachomatis. Infect Immun 68:5439–5442
    • (2000) Infect Immun , vol.68 , pp. 5439-5442
    • Harper, A.1    Pogson, C.I.2    Pearce, J.H.3
  • 34
    • 0034607359 scopus 로고    scopus 로고
    • Biochemical and biophysical characterization of in vitro folded outer membrane porin PorA of Neisseria meningitidis
    • PID: 10727615, COI: 1:CAS:528:DC%2BD3cXhvV2lt70%3D
    • Jansen C, Wiese A, Reubsaet L, Dekker N, de Cock H, Seydel U, Tommassen J (2000) Biochemical and biophysical characterization of in vitro folded outer membrane porin PorA of Neisseria meningitidis. Biochim Biophys Acta 1464:284–298
    • (2000) Biochim Biophys Acta , vol.1464 , pp. 284-298
    • Jansen, C.1    Wiese, A.2    Reubsaet, L.3    Dekker, N.4    de Cock, H.5    Seydel, U.6    Tommassen, J.7
  • 35
    • 0032077463 scopus 로고    scopus 로고
    • Effect of process conditions on recovery of protein activity after freezing and freeze-drying
    • PID: 9653629, COI: 1:CAS:528:DyaK1cXksVagtLc%3D
    • Jiang S, Nail SL (1998) Effect of process conditions on recovery of protein activity after freezing and freeze-drying. Eur J Pharm Biopharm 45:249–257
    • (1998) Eur J Pharm Biopharm , vol.45 , pp. 249-257
    • Jiang, S.1    Nail, S.L.2
  • 36
    • 77954700033 scopus 로고    scopus 로고
    • Impact of freezing on pH of buffered solutions and consequences for monoclonal antibody aggregation
    • PID: 20039442, COI: 1:CAS:528:DC%2BC3cXpsVKntbc%3D
    • Kolhe P, Amend E, Singh SK (2010) Impact of freezing on pH of buffered solutions and consequences for monoclonal antibody aggregation. Biotechnol Prog 26:727–733
    • (2010) Biotechnol Prog , vol.26 , pp. 727-733
    • Kolhe, P.1    Amend, E.2    Singh, S.K.3
  • 37
    • 80052444492 scopus 로고    scopus 로고
    • Vaccine stabilization: research, commercialization, and potential impact
    • PID: 21651941, COI: 1:CAS:528:DC%2BC3MXhtFKjtr7E
    • Kristensen D, Chen D, Cummings R (2011) Vaccine stabilization: research, commercialization, and potential impact. Vaccine 29:7122–7124
    • (2011) Vaccine , vol.29 , pp. 7122-7124
    • Kristensen, D.1    Chen, D.2    Cummings, R.3
  • 38
    • 48549086114 scopus 로고    scopus 로고
    • Effects of solution conditions, processing parameters, and container materials on aggregation of a monoclonal antibody during freeze-thawing
    • PID: 17823949, COI: 1:CAS:528:DC%2BD1cXltlenu7c%3D
    • Kueltzo LA, Wang W, Randolph TW, Carpenter JF (2008) Effects of solution conditions, processing parameters, and container materials on aggregation of a monoclonal antibody during freeze-thawing. J Pharm Sci 97:1801–1812
    • (2008) J Pharm Sci , vol.97 , pp. 1801-1812
    • Kueltzo, L.A.1    Wang, W.2    Randolph, T.W.3    Carpenter, J.F.4
  • 39
    • 0030888166 scopus 로고    scopus 로고
    • Structural and functional characterization of a recombinant PorB class 2 protein from Neisseria meningitidis. Conformational stability and porin activity
    • PID: 9099721, COI: 1:CAS:528:DyaK2sXisl2qtbg%3D
    • Minetti CA, Tai JY, Blake MS, Pullen JK, Liang SM, Remeta DP (1997) Structural and functional characterization of a recombinant PorB class 2 protein from Neisseria meningitidis. Conformational stability and porin activity. J Biol Chem 272:10710–10720
    • (1997) J Biol Chem , vol.272 , pp. 10710-10720
    • Minetti, C.A.1    Tai, J.Y.2    Blake, M.S.3    Pullen, J.K.4    Liang, S.M.5    Remeta, D.P.6
  • 40
    • 0016139703 scopus 로고
    • Intracellular parasitism: life in an extreme environment
    • PID: 4413960, COI: 1:STN:280:DyaE2M%2FhtFartw%3D%3D
    • Moulder JW (1974) Intracellular parasitism: life in an extreme environment. J Infect Dis 130:300–306
    • (1974) J Infect Dis , vol.130 , pp. 300-306
    • Moulder, J.W.1
  • 41
    • 0024316909 scopus 로고
    • Salt precipitation during the freeze-concentration of phosphate buffer solutions
    • PID: 2611352, COI: 1:CAS:528:DyaK3cXhtFGhtLY%3D
    • Murase N, Franks F (1989) Salt precipitation during the freeze-concentration of phosphate buffer solutions. Biophys Chem 34:293–300
    • (1989) Biophys Chem , vol.34 , pp. 293-300
    • Murase, N.1    Franks, F.2
  • 42
    • 0001865876 scopus 로고
    • An unidentified virus which produces pneumonia and systemic infection in mice
    • PID: 17773453, COI: 1:STN:280:DC%2BC3cvovFWqtw%3D%3D
    • Nigg C (1942) An unidentified virus which produces pneumonia and systemic infection in mice. Science 95:49–50
    • (1942) Science , vol.95 , pp. 49-50
    • Nigg, C.1
  • 43
    • 84911005818 scopus 로고    scopus 로고
    • Amphipols and photosynthetic pigment-protein complexes, J Membr Biol:
    • Opačić M, Durand G, Bosco M, Polidori A, Popot J-L (2014) Amphipols and photosynthetic pigment-protein complexes. J Membr Biol (submitted)
    • (2014) Popot J-L
    • Opačić, M.1    Durand, G.2    Bosco, M.3    Polidori, A.4
  • 44
    • 0030743650 scopus 로고    scopus 로고
    • Immunization with an acellular vaccine consisting of the outer membrane complex of Chlamydia trachomatis induces protection against a genital challenge
    • PID: 9234798, COI: 1:CAS:528:DyaK2sXkvVarsrw%3D
    • Pal S, Theodor I, Peterson EM, de la Maza LM (1997) Immunization with an acellular vaccine consisting of the outer membrane complex of Chlamydia trachomatis induces protection against a genital challenge. Infect Immun 65:3361–3369
    • (1997) Infect Immun , vol.65 , pp. 3361-3369
    • Pal, S.1    Theodor, I.2    Peterson, E.M.3    de la Maza, L.M.4
  • 45
    • 0036719064 scopus 로고    scopus 로고
    • Immunization with the Chlamydia trachomatis mouse pneumonitis major outer membrane protein by use of CpG oligodeoxynucleotides as an adjuvant induces a protective immune response against an intranasal chlamydial challenge
    • PID: 12183524, COI: 1:CAS:528:DC%2BD38Xmtl2itbk%3D
    • Pal S, Davis HL, Peterson EM, de la Maza LM (2002) Immunization with the Chlamydia trachomatis mouse pneumonitis major outer membrane protein by use of CpG oligodeoxynucleotides as an adjuvant induces a protective immune response against an intranasal chlamydial challenge. Infect Immun 70:4812–4817
    • (2002) Infect Immun , vol.70 , pp. 4812-4817
    • Pal, S.1    Davis, H.L.2    Peterson, E.M.3    de la Maza, L.M.4
  • 46
    • 80053444734 scopus 로고    scopus 로고
    • Stability of seasonal influenza vaccines investigated by spectroscopy and microscopy methods
    • PID: 21803109, COI: 1:CAS:528:DC%2BC3MXht1Ght73N
    • Patois E, Capelle MA, Gurny R, Arvinte T (2011) Stability of seasonal influenza vaccines investigated by spectroscopy and microscopy methods. Vaccine 29:7404–7413
    • (2011) Vaccine , vol.29 , pp. 7404-7413
    • Patois, E.1    Capelle, M.A.2    Gurny, R.3    Arvinte, T.4
  • 47
    • 84910125751 scopus 로고    scopus 로고
    • Molecular dynamics simulations of a membrane protein/amphipol complex. J Membr Biol
    • Perlmutter J, Popot J-L, Sachs J (2014) Molecular dynamics simulations of a membrane protein/amphipol complex. J Membr Biol. doi:10.1007/s00232-014-9690-8
    • (2014) doi:10.1007/s00232-014-9690-8
    • Perlmutter, J.1    Popot, J.-L.2    Sachs, J.3
  • 50
    • 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 CL, 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.L.1    Popot, J.-L.2    Kleinschmidt, J.H.3
  • 51
    • 77953627340 scopus 로고    scopus 로고
    • Amphipols, nanodiscs, and fluorinated surfactants: three nonconventional 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 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
  • 54
    • 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
  • 55
    • 84911003438 scopus 로고    scopus 로고
    • Etudes structurales et dynamiques de la protéine membranaire KpOmpA par RMN en phase liquide et solide. Ph.D
    • Université Paul Sabatier, Toulouse:
    • 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
    • (2008) Thesis
    • Renault, M.1
  • 56
    • 0035783023 scopus 로고    scopus 로고
    • Stability of membrane proteins: relevance for the selection of appropriate methods for high-resolution structure determinations
    • PID: 11886216, COI: 1:CAS:528:DC%2BD38Xhslemt7s%3D
    • Rosenbusch JP (2001) Stability of membrane proteins: relevance for the selection of appropriate methods for high-resolution structure determinations. J Struct Biol 136:144–157
    • (2001) J Struct Biol , vol.136 , pp. 144-157
    • Rosenbusch, J.P.1
  • 57
    • 53549111888 scopus 로고    scopus 로고
    • Physical characterization of Clostridium difficile toxins and toxoids: effect of the formaldehyde crosslinking on thermal stability
    • PID: 18257030, COI: 1:CAS:528:DC%2BD1cXhtVyltL7M
    • Salnikova MS, Joshi SB, Rytting JH, Warny M, Middaugh CR (2008) Physical characterization of Clostridium difficile toxins and toxoids: effect of the formaldehyde crosslinking on thermal stability. J Pharm Sci 97:3735–3752
    • (2008) J Pharm Sci , vol.97 , pp. 3735-3752
    • Salnikova, M.S.1    Joshi, S.B.2    Rytting, J.H.3    Warny, M.4    Middaugh, C.R.5
  • 58
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • PID: 2449095
    • Schägger H, von Jagow G (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal Biochem 166:368–379
    • (1987) Anal Biochem , vol.166 , pp. 368-379
    • Schägger, H.1    von Jagow, G.2
  • 59
    • 84863205849 scopus 로고    scopus 로고
    • NIH Image to ImageJ: 25 years of image analysis
    • PID: 22930834, COI: 1:CAS:528:DC%2BC38XhtVKntb7P
    • Schneider CA, Rasband WS, Eliceiri KW (2012) NIH Image to ImageJ: 25 years of image analysis. Nat Methods 9:671–675
    • (2012) Nat Methods , vol.9 , pp. 671-675
    • Schneider, C.A.1    Rasband, W.S.2    Eliceiri, K.W.3
  • 60
    • 68949128705 scopus 로고    scopus 로고
    • Evidence of partial unfolding of proteins at the ice/freeze-concentrate interface by infrared microscopy
    • PID: 19544369, COI: 1:CAS:528:DC%2BD1MXptl2itLo%3D
    • Schwegman JJ, Carpenter JF, Nail SL (2009) Evidence of partial unfolding of proteins at the ice/freeze-concentrate interface by infrared microscopy. J Pharm Sci 98:3239–3246
    • (2009) J Pharm Sci , vol.98 , pp. 3239-3246
    • Schwegman, J.J.1    Carpenter, J.F.2    Nail, S.L.3
  • 61
    • 0030043206 scopus 로고    scopus 로고
    • Proteins in frozen solutions: evidence of ice-induced partial unfolding
    • PID: 8789114, COI: 1:CAS:528:DyaK28XlslGjsA%3D%3D
    • Strambini GB, Gabellieri E (1996) Proteins in frozen solutions: evidence of ice-induced partial unfolding. Biophys J 70:971–976
    • (1996) Biophys J , vol.70 , pp. 971-976
    • Strambini, G.B.1    Gabellieri, E.2
  • 63
    • 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
  • 64
    • 84901280813 scopus 로고    scopus 로고
    • Increased immunoaccessibility of MOMP epitopes in a vaccine formulated with amphipols may account for the very robust protection elicited against a vaginal challenge with Chlamydia muridarum
    • PID: 24778450, COI: 1:CAS:528:DC%2BC2cXotFGisb0%3D
    • Tifrea DF, Pal S, Popot J-L, Cocco MJ, de la Maza LM (2014) Increased immunoaccessibility of MOMP epitopes in a vaccine formulated with amphipols may account for the very robust protection elicited against a vaginal challenge with Chlamydia muridarum. J Immunol 192:5201–5213
    • (2014) J Immunol , vol.192 , pp. 5201-5213
    • Tifrea, D.F.1    Pal, S.2    Popot, J.-L.3    Cocco, M.J.4    de la Maza, L.M.5
  • 65
    • 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
  • 66
    • 42649093865 scopus 로고    scopus 로고
    • Influenza vaccines
    • PID: 18508556, COI: 1:CAS:528:DC%2BD1cXnsVOjtro%3D
    • Webby RJ, Sandbulte MR (2008) Influenza vaccines. Front Biosci 13:4912–4924
    • (2008) Front Biosci , vol.13 , pp. 4912-4924
    • Webby, R.J.1    Sandbulte, M.R.2
  • 67
    • 67449132077 scopus 로고    scopus 로고
    • Principles, approaches, and challenges for predicting protein aggregation rates and shelf life
    • PID: 18683878, COI: 1:CAS:528:DC%2BD1MXktlSisLc%3D
    • Weiss WFt, Young TM, Roberts CJ (2009) Principles, approaches, and challenges for predicting protein aggregation rates and shelf life. J Pharm Sci 98:1246–1277
    • (2009) J Pharm Sci , vol.98 , pp. 1246-1277
    • Weiss, W.F.1    Young, T.M.2    Roberts, C.J.3
  • 68
    • 79955620192 scopus 로고    scopus 로고
    • A new approach to explore the impact of freeze-thaw cycling on protein structure: hydrogen/deuterium exchange mass spectrometry (HX-MS)
    • PID: 21301933, COI: 1:CAS:528:DC%2BC3MXhs1Snsbs%3D
    • Zhang A, Qi W, Singh SK, Fernandez EJ (2011) A new approach to explore the impact of freeze-thaw cycling on protein structure: hydrogen/deuterium exchange mass spectrometry (HX-MS). Pharm Res 28:1179–1193
    • (2011) Pharm Res , vol.28 , pp. 1179-1193
    • Zhang, A.1    Qi, W.2    Singh, S.K.3    Fernandez, E.J.4
  • 70
    • 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
  • 71
    • 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


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