메뉴 건너뛰기




Volumn 9, Issue 7, 2000, Pages 1407-1409

Mesoscopic surfactant organization and membrane protein crystallization

Author keywords

Aquaporin; Bile salts; Detergents; Membrane protein crystallization; Self assembled system

Indexed keywords

AQUAPORIN; MEMBRANE PROTEIN; SURFACTANT;

EID: 0033862579     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.9.7.1407     Document Type: Article
Times cited : (5)

References (31)
  • 1
    • 0000311529 scopus 로고
    • Studies on the formation of helical deoxycholate complexes
    • Blow DM, Rich A. 1960. Studies on the formation of helical deoxycholate complexes. J Am Chem Soc 82:3566-3571.
    • (1960) J Am Chem Soc , vol.82 , pp. 3566-3571
    • Blow, D.M.1    Rich, A.2
  • 2
    • 0032853219 scopus 로고    scopus 로고
    • Cellular and molecular biology of the aquaporin water channels
    • Borgnia M, Nielsen S, Engel A, Agre P. 1999. Cellular and molecular biology of the aquaporin water channels. Ann Rev Biochem 68:425-458.
    • (1999) Ann Rev Biochem , vol.68 , pp. 425-458
    • Borgnia, M.1    Nielsen, S.2    Engel, A.3    Agre, P.4
  • 3
    • 77956799374 scopus 로고
    • Physical-chemical properties of bile salts and their acids
    • Danielsson H, Sjövall J, eds. Amsterdam, Netherlands: Elsevier
    • Carey MC. 1985. Physical-chemical properties of bile salts and their acids. In: Danielsson H, Sjövall J, eds. Sterols and bile acids. Amsterdam, Netherlands: Elsevier. pp 345-403.
    • (1985) Sterols and Bile Acids , pp. 345-403
    • Carey, M.C.1
  • 4
    • 0032545321 scopus 로고    scopus 로고
    • Structure of the MscL homolog from Mycobacterium tuberculosis: A gated mechanosensitive ion channel
    • Chang G, Spencer RH, Lee AT, Barclay MT, Rees DC. 1998. Structure of the MscL homolog from Mycobacterium tuberculosis: A gated mechanosensitive ion channel. Science 282:2220-2226.
    • (1998) Science , vol.282 , pp. 2220-2226
    • Chang, G.1    Spencer, R.H.2    Lee, A.T.3    Barclay, M.T.4    Rees, D.C.5
  • 7
    • 0031777369 scopus 로고    scopus 로고
    • Prediction of functional residues in water channels and related proteins
    • Froger A, Tallur B, Thomas D, Delamarche C. 1998. Prediction of functional residues in water channels and related proteins. Protein Sci 7:1458-1468.
    • (1998) Protein Sci , vol.7 , pp. 1458-1468
    • Froger, A.1    Tallur, B.2    Thomas, D.3    Delamarche, C.4
  • 8
    • 0019036909 scopus 로고
    • Three-dimensional crystals of an integral membrane protein: An initial X-ray analysis
    • Garavito RM, Rosenbusch JP. 1980. Three-dimensional crystals of an integral membrane protein: An initial X-ray analysis. J Cell Biol 86:327-329.
    • (1980) J Cell Biol , vol.86 , pp. 327-329
    • Garavito, R.M.1    Rosenbusch, J.P.2
  • 10
    • 0033580880 scopus 로고    scopus 로고
    • Structure of the Escherichia coli fumarate reductase respiratory complex
    • Iverson TM, Luna-Chavez C, Cecchini G, Rees DC. 1999. Structure of the Escherichia coli fumarate reductase respiratory complex. Science 284:1961-1966.
    • (1999) Science , vol.284 , pp. 1961-1966
    • Iverson, T.M.1    Luna-Chavez, C.2    Cecchini, G.3    Rees, D.C.4
  • 11
    • 0029992660 scopus 로고    scopus 로고
    • Lipidic cubic phases: A novel concept for the crystallization of membrane proteins
    • Landau HM, Rosenbusch JP. 1996. Lipidic cubic phases: A novel concept for the crystallization of membrane proteins. Proc Natl Acad Sci USA 93:14532-14535.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 14532-14535
    • Landau, H.M.1    Rosenbusch, J.P.2
  • 12
    • 0030915303 scopus 로고    scopus 로고
    • Molecular design of aquaporin-1 water channel as revealed by electron crystallography
    • Li H, Lee S, Jap BK. 1997. Molecular design of aquaporin-1 water channel as revealed by electron crystallography. Nat Struct Biol 4:263-265.
    • (1997) Nat Struct Biol , vol.4 , pp. 263-265
    • Li, H.1    Lee, S.2    Jap, B.K.3
  • 13
    • 0032546920 scopus 로고    scopus 로고
    • Proton transfer pathways in bacteriorhodopsin at 2.3 angstrom resolution
    • Luecke H, Richter HT, Lanyi JK. 1998. Proton transfer pathways in bacteriorhodopsin at 2.3 angstrom resolution. Science 280:1934-1937.
    • (1998) Science , vol.280 , pp. 1934-1937
    • Luecke, H.1    Richter, H.T.2    Lanyi, J.K.3
  • 14
    • 0020475570 scopus 로고
    • Three-dimensional crystals of a membrane protein complex
    • Michel H. 1982. Three-dimensional crystals of a membrane protein complex. J Mol Biol 158:567-572.
    • (1982) J Mol Biol , vol.158 , pp. 567-572
    • Michel, H.1
  • 15
    • 0001791586 scopus 로고
    • Crystallization of membrane proteins
    • Michel H. 1983. Crystallization of membrane proteins. Trends in Biol Sci 8:56-59.
    • (1983) Trends in Biol Sci , vol.8 , pp. 56-59
    • Michel, H.1
  • 17
    • 0028991525 scopus 로고
    • v fragment-mediated crystallization of the membrane protein bacterial cytochrome c oxidase
    • v fragment-mediated crystallization of the membrane protein bacterial cytochrome c oxidase. Nat Struct Biol 2:842-845.
    • (1995) Nat Struct Biol , vol.2 , pp. 842-845
    • Ostermeier, C.1    Iwata, S.2    Ludwig, B.3    Michel, H.4
  • 18
    • 0030864048 scopus 로고    scopus 로고
    • X-ray structure of bacteriorhodopsin at 2.5 angstroms from microcrystals grown in lipidic cubic phases
    • Pebay-Peyroula E, Rummel G, Rosenbusch JP, Landau EM. 1997. X-ray structure of bacteriorhodopsin at 2.5 angstroms from microcrystals grown in lipidic cubic phases. Science 277:1676-1681.
    • (1997) Science , vol.277 , pp. 1676-1681
    • Pebay-Peyroula, E.1    Rummel, G.2    Rosenbusch, J.P.3    Landau, E.M.4
  • 19
    • 0029671464 scopus 로고    scopus 로고
    • Engineering the lac permease for purification and crystallization
    • Privé GG, Kaback HR. 1996. Engineering the lac permease for purification and crystallization. J Bioenerg Biomembr 28:29-34.
    • (1996) J Bioenerg Biomembr , vol.28 , pp. 29-34
    • Privé, G.G.1    Kaback, H.R.2
  • 20
    • 0001126257 scopus 로고
    • Formation of a helical steroid complex
    • Rich A, Blow DM. 1958. Formation of a helical steroid complex. Nature 182:423-426.
    • (1958) Nature , vol.182 , pp. 423-426
    • Rich, A.1    Blow, D.M.2
  • 21
    • 0027686674 scopus 로고
    • Structure at 2.5 Å of a designed peptide that maintains solubility of membrane proteins
    • Schafmeister CE, Miercke LJ, Stroud RM. 1993. Structure at 2.5 Å of a designed peptide that maintains solubility of membrane proteins. Science 262:734-738.
    • (1993) Science , vol.262 , pp. 734-738
    • Schafmeister, C.E.1    Miercke, L.J.2    Stroud, R.M.3
  • 23
    • 0002051651 scopus 로고
    • Size and structure of bile salt micelles
    • Goddard ED, ed. Washington, DC: American Chemical Society
    • Small DM. 1968. Size and structure of bile salt micelles. In: Goddard ED, ed. Molecular association in biological and related systems. Washington, DC: American Chemical Society. pp 31-52.
    • (1968) Molecular Association in Biological and Related Systems , pp. 31-52
    • Small, D.M.1
  • 24
    • 0032127999 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray analysis of ferric enterobactin receptor FepA, an integral membrane protein from Escherichia coli
    • Smith BS, Kobe B, Kurumbail R, Buchanan SK, Venkatramani L, Van Der Helm D, Deisenhofer J. 1998. Crystallization and preliminary X-ray analysis of ferric enterobactin receptor FepA, an integral membrane protein from Escherichia coli. Acta Crystallogr D 54:697-699.
    • (1998) Acta Crystallogr D , vol.54 , pp. 697-699
    • Smith, B.S.1    Kobe, B.2    Kurumbail, R.3    Buchanan, S.K.4    Venkatramani, L.5    Van Der Helm, D.6    Deisenhofer, J.7
  • 25
    • 0001567816 scopus 로고
    • The gelation of bile salt solutions
    • Sobotka H, Czeczowiczka N. 1958. The gelation of bile salt solutions. J Colloid Sci 13:188-191.
    • (1958) J Colloid Sci , vol.13 , pp. 188-191
    • Sobotka, H.1    Czeczowiczka, N.2
  • 26
    • 0033229834 scopus 로고    scopus 로고
    • Expression, purification, and structural characterization of the bacteriorhodopsin-aspartyl transcarbamylase fusion protein
    • Turner GJ, Miercke LJW, Mitra AK, Stroud RM, Betlach MC, Winter-Vann A. 1999. Expression, purification, and structural characterization of the bacteriorhodopsin-aspartyl transcarbamylase fusion protein. Prot Express Purif 17:324-338.
    • (1999) Prot Express Purif , vol.17 , pp. 324-338
    • Turner, G.J.1    Miercke, L.J.W.2    Mitra, A.K.3    Stroud, R.M.4    Betlach, M.C.5    Winter-Vann, A.6
  • 27
    • 0027366423 scopus 로고
    • Secondary structure analysis of purified functional CHIP28 water channels by CD and FTIR spectroscopy
    • van Hoek AN, Wiener M, Bicknese S, Miercke L, Biwersi J, Verkman AS. 1993. Secondary structure analysis of purified functional CHIP28 water channels by CD and FTIR spectroscopy. Biochemistry 32:11847-11856.
    • (1993) Biochemistry , vol.32 , pp. 11847-11856
    • Van Hoek, A.N.1    Wiener, M.2    Bicknese, S.3    Miercke, L.4    Biwersi, J.5    Verkman, A.S.6
  • 28
    • 0028914847 scopus 로고
    • Purification and structure-function analysis of native, PNGase F-treated, and endo-β-galactosidase-treated CHIP28 water channels
    • van Hoek AN, Wiener MC, Verbavatz JM, Brown D, Lipniunas PH, Townsend RR, Verkman AS. 1995. Purification and structure-function analysis of native, PNGase F-treated, and endo-β-galactosidase-treated CHIP28 water channels. Biochemistry 34:2212-2219.
    • (1995) Biochemistry , vol.34 , pp. 2212-2219
    • Van Hoek, A.N.1    Wiener, M.C.2    Verbavatz, J.M.3    Brown, D.4    Lipniunas, P.H.5    Townsend, R.R.6    Verkman, A.S.7
  • 30
    • 0032905870 scopus 로고    scopus 로고
    • Lessons on renal physiology from transgenic mice lacking aquaporin water channels
    • Verkman AS. 1999. Lessons on renal physiology from transgenic mice lacking aquaporin water channels. J Am Soc Nephrol 10:1126-1135.
    • (1999) J Am Soc Nephrol , vol.10 , pp. 1126-1135
    • Verkman, A.S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.