메뉴 건너뛰기




Volumn 1798, Issue 8, 2010, Pages 1540-1546

Crystallization of the membrane protein hVDAC1 produced in cell-free system

Author keywords

Cell free expression; Crystallization; Membrane protein; Voltage dependent anion channel

Indexed keywords

MEMBRANE PROTEIN; RECOMBINANT PROTEIN; VOLTAGE DEPENDENT ANION CHANNEL 1;

EID: 77953693955     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2010.04.010     Document Type: Article
Times cited : (39)

References (36)
  • 2
    • 33646155331 scopus 로고    scopus 로고
    • Enhancing functional production of G protein-coupled receptors in Pichia pastoris to levels required for structural studies via a single expression screen
    • Andre N., Cherouati N., Prual C., Steffan T., Zeder-Lutz G., Magnin T., Pattus F., Michel H., Wagner R., Reinhart C. Enhancing functional production of G protein-coupled receptors in Pichia pastoris to levels required for structural studies via a single expression screen. Protein Sci. 2006, 15:1115-1126.
    • (2006) Protein Sci. , vol.15 , pp. 1115-1126
    • Andre, N.1    Cherouati, N.2    Prual, C.3    Steffan, T.4    Zeder-Lutz, G.5    Magnin, T.6    Pattus, F.7    Michel, H.8    Wagner, R.9    Reinhart, C.10
  • 5
    • 66049128793 scopus 로고    scopus 로고
    • Crystallizing membrane proteins for structure determination: use of lipidic mesophases
    • Caffrey M. Crystallizing membrane proteins for structure determination: use of lipidic mesophases. Annu. Rev. Biophys. 2009, 38:29-51.
    • (2009) Annu. Rev. Biophys. , vol.38 , pp. 29-51
    • Caffrey, M.1
  • 6
    • 0029992660 scopus 로고    scopus 로고
    • Lipidic cubic phases: a novel concept for the crystallization of membrane proteins
    • Landau E.M., Rosenbusch J.P. Lipidic cubic phases: a novel concept for the crystallization of membrane proteins. Proc. Natl. Acad. Sci. U. S. A. 1996, 93:14532-14535.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 14532-14535
    • Landau, E.M.1    Rosenbusch, J.P.2
  • 8
    • 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
    • Berrier C., Park K.H., Abes S., Bibonne A., Betton J.M., Ghazi A. Cell-free synthesis of a functional ion channel in the absence of a membrane and in the presence of detergent. Biochemistry 2004, 43:12585-12591.
    • (2004) Biochemistry , vol.43 , pp. 12585-12591
    • Berrier, C.1    Park, K.H.2    Abes, S.3    Bibonne, A.4    Betton, J.M.5    Ghazi, A.6
  • 9
    • 15744391469 scopus 로고    scopus 로고
    • Expression of G protein coupled receptors in a cell-free translational system using detergents and thioredoxin-fusion vectors
    • Ishihara G., Goto M., Saeki M., Ito K., Hori T., Kigawa T., Shirouzu M., Yokoyama S. Expression of G protein coupled receptors in a cell-free translational system using detergents and thioredoxin-fusion vectors. Protein Expr. Purif. 2005, 41:27-37.
    • (2005) Protein Expr. Purif. , vol.41 , pp. 27-37
    • Ishihara, G.1    Goto, M.2    Saeki, M.3    Ito, K.4    Hori, T.5    Kigawa, T.6    Shirouzu, M.7    Yokoyama, S.8
  • 12
    • 0022646308 scopus 로고
    • Structure of the channels in the outer mitochondrial membrane: electron microscopic studies of the periodic arrays induced by phospholipase a(2) treatment of the Neurospora membrane
    • Mannella C.A., Ribeiro A., Frank J. Structure of the channels in the outer mitochondrial membrane: electron microscopic studies of the periodic arrays induced by phospholipase a(2) treatment of the Neurospora membrane. Biophys. J. 1986, 49:307-317.
    • (1986) Biophys. J. , vol.49 , pp. 307-317
    • Mannella, C.A.1    Ribeiro, A.2    Frank, J.3
  • 13
    • 0032875663 scopus 로고    scopus 로고
    • Crystallization of the human, mitochondrial voltage-dependent anion-selective channel in the presence of phospholipids
    • Dolder M., Zeth K., Tittmann P., Gross H., Welte W., Wallimann T. Crystallization of the human, mitochondrial voltage-dependent anion-selective channel in the presence of phospholipids. J. Struct. Biol. 1999, 127:64-71.
    • (1999) J. Struct. Biol. , vol.127 , pp. 64-71
    • Dolder, M.1    Zeth, K.2    Tittmann, P.3    Gross, H.4    Welte, W.5    Wallimann, T.6
  • 15
    • 34249696578 scopus 로고    scopus 로고
    • The supramolecular assemblies of voltage-dependent anion channels in the native membrane
    • Hoogenboom B.W., Suda K., Engel A., Fotiadis D. The supramolecular assemblies of voltage-dependent anion channels in the native membrane. J. Mol. Biol. 2007, 370:246-255.
    • (2007) J. Mol. Biol. , vol.370 , pp. 246-255
    • Hoogenboom, B.W.1    Suda, K.2    Engel, A.3    Fotiadis, D.4
  • 19
    • 0032577455 scopus 로고    scopus 로고
    • Bacterial expression and characterization of the mitochondrial outer membrane channel. Effects of n-terminal modifications
    • Koppel D.A., Kinnally K.W., Masters P., Forte M., Blachly-Dyson E., Mannella C.A. Bacterial expression and characterization of the mitochondrial outer membrane channel. Effects of n-terminal modifications. J. Biol. Chem. 1998, 273:13794-13800.
    • (1998) J. Biol. Chem. , vol.273 , pp. 13794-13800
    • Koppel, D.A.1    Kinnally, K.W.2    Masters, P.3    Forte, M.4    Blachly-Dyson, E.5    Mannella, C.A.6
  • 20
    • 0019441262 scopus 로고
    • Improved patch-clamp techniques for high-resolution current recording from cells and cell-free membrane patches
    • Hamill O.P., Marty A., Neher E., Sakmann B., Sigworth F.J. Improved patch-clamp techniques for high-resolution current recording from cells and cell-free membrane patches. Pflugers Arch. 1981, 391:85-100.
    • (1981) Pflugers Arch. , vol.391 , pp. 85-100
    • Hamill, O.P.1    Marty, A.2    Neher, E.3    Sakmann, B.4    Sigworth, F.J.5
  • 21
    • 77449116387 scopus 로고    scopus 로고
    • Impact of disease-causing SUR1 mutations on the KATP channel subunit interface probed with a rhodamine protection assay
    • E. Hosy, J.P. Dupuis, M. Vivaudou, Impact of disease-causing SUR1 mutations on the KATP channel subunit interface probed with a rhodamine protection assay. J. Biol. Chem. 285 (2010) 3084-3091.
    • (2010) J. Biol. Chem. , vol.285 , pp. 3084-3091
    • Hosy, E.1    Dupuis, J.P.2    Vivaudou, M.3
  • 23
    • 32944467057 scopus 로고    scopus 로고
    • Post-crystallization treatments for improving diffraction quality of protein crystals
    • Heras B., Martin J.L. Post-crystallization treatments for improving diffraction quality of protein crystals. Acta Crystallogr. D Biol. Crystallogr. 2005, 61:1173-1180.
    • (2005) Acta Crystallogr. D Biol. Crystallogr. , vol.61 , pp. 1173-1180
    • Heras, B.1    Martin, J.L.2
  • 26
    • 0025772895 scopus 로고
    • Patch clamping VDAC in liposomes containing whole mitochondrial membranes
    • Wunder U.R., Colombini M. Patch clamping VDAC in liposomes containing whole mitochondrial membranes. J. Membr. Biol. 1991, 123:83-91.
    • (1991) J. Membr. Biol. , vol.123 , pp. 83-91
    • Wunder, U.R.1    Colombini, M.2
  • 27
    • 67650520154 scopus 로고    scopus 로고
    • Differences between CusA and AcrB crystallisation highlighted by protein flexibility
    • Deniaud A., Goulielmakis A., Coves J., Pebay-Peyroula E. Differences between CusA and AcrB crystallisation highlighted by protein flexibility. PloS One 2009, 4:e6214.
    • (2009) PloS One , vol.4
    • Deniaud, A.1    Goulielmakis, A.2    Coves, J.3    Pebay-Peyroula, E.4
  • 28
    • 0345276579 scopus 로고    scopus 로고
    • Three-dimensional crystallization of the Escherichia coli glycerol-3-phosphate transporter: a member of the major facilitator superfamily
    • Lemieux M.J., Song J., Kim M.J., Huang Y., Villa A., Auer M., Li X.D., Wang D.N. Three-dimensional crystallization of the Escherichia coli glycerol-3-phosphate transporter: a member of the major facilitator superfamily. Protein Sci. 2003, 12:2748-2756.
    • (2003) Protein Sci. , vol.12 , pp. 2748-2756
    • Lemieux, M.J.1    Song, J.2    Kim, M.J.3    Huang, Y.4    Villa, A.5    Auer, M.6    Li, X.D.7    Wang, D.N.8
  • 33
    • 46949092587 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray crystallographic studies of human voltage-dependent anion channel isoform I (HVDAC1)
    • Meins T., Vonrhein C., Zeth K. Crystallization and preliminary X-ray crystallographic studies of human voltage-dependent anion channel isoform I (HVDAC1). Acta Crystallogr. 2008, 64:651-655.
    • (2008) Acta Crystallogr. , vol.64 , pp. 651-655
    • Meins, T.1    Vonrhein, C.2    Zeth, K.3
  • 34
    • 34748835813 scopus 로고    scopus 로고
    • High-level expression, refolding and probing the natural fold of the human voltage-dependent anion channel isoforms I and II
    • Engelhardt H., Meins T., Poynor M., Adams V., Nussberger S., Welte W., Zeth K. High-level expression, refolding and probing the natural fold of the human voltage-dependent anion channel isoforms I and II. J. Membr. Biol. 2007, 216:93-105.
    • (2007) J. Membr. Biol. , vol.216 , pp. 93-105
    • Engelhardt, H.1    Meins, T.2    Poynor, M.3    Adams, V.4    Nussberger, S.5    Welte, W.6    Zeth, K.7
  • 35
    • 0037450548 scopus 로고    scopus 로고
    • The expression of outer membrane proteins for crystallization
    • Bannwarth M., Schulz G.E. The expression of outer membrane proteins for crystallization. Biochim. Biophys. Acta 2003, 1610:37-45.
    • (2003) Biochim. Biophys. Acta , vol.1610 , pp. 37-45
    • Bannwarth, M.1    Schulz, G.E.2
  • 36
    • 77953724422 scopus 로고    scopus 로고
    • In-vitro protein production for structure determination with the rapid translation system (RTS)
    • Cho H.S., Pelton J.G., Wang W., Yokota H., Wemmer D. In-vitro protein production for structure determination with the rapid translation system (RTS). Biochemica (Roche) 2001, 4:27-29.
    • (2001) Biochemica (Roche) , vol.4 , pp. 27-29
    • Cho, H.S.1    Pelton, J.G.2    Wang, W.3    Yokota, H.4    Wemmer, D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.