메뉴 건너뛰기




Volumn 11, Issue 3, 1997, Pages 284-288

Purification and functional reconstitution of the human CHIP28 water channel expressed in Saccharomyces cerevisiae

Author keywords

[No Author keywords available]

Indexed keywords

INFLUENZA VIRUS; SACCHAROMYCES CEREVISIAE;

EID: 0031439976     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1006/prep.1997.0798     Document Type: Article
Times cited : (20)

References (17)
  • 1
    • 0026503030 scopus 로고
    • Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein
    • Preston G. M., Carroll T. P., Guggino W. B., Agre P. Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein. Science. 256:1992;385-387.
    • (1992) Science , vol.256 , pp. 385-387
    • Preston, G.M.1    Carroll, T.P.2    Guggino, W.B.3    Agre, P.4
  • 2
    • 0021712623 scopus 로고
    • The major intrinsic protein (MIP) of the bovine lens fiber membrane: Characterization and structure based on cDNA cloning
    • Gorin M. B., Yancey S. B., Cline J., Revel J. P., Horwitz J. The major intrinsic protein (MIP) of the bovine lens fiber membrane: Characterization and structure based on cDNA cloning. Cell. 39:1984;49-59.
    • (1984) Cell , vol.39 , pp. 49-59
    • Gorin, M.B.1    Yancey, S.B.2    Cline, J.3    Revel, J.P.4    Horwitz, J.5
  • 4
    • 0028318868 scopus 로고
    • Molecular structure of the water channel through aquaporin CHIP. The hourglass model
    • Jung J. S., Preston G. M., Smith B. L., Guggino W. B., Agre P. Molecular structure of the water channel through aquaporin CHIP. The hourglass model. J. Biol. Chem. 269:1994;14648-14654.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14648-14654
    • Jung, J.S.1    Preston, G.M.2    Smith, B.L.3    Guggino, W.B.4    Agre, P.5
  • 5
    • 0026806764 scopus 로고
    • Reconstitution of functional water channels in liposomes containing purified red cell CHIP28 protein
    • Zeidel M. L., Ambudkar S. V., Smith B. L., Agre P. Reconstitution of functional water channels in liposomes containing purified red cell CHIP28 protein. Biochemistry. 31:1992;7436-7440.
    • (1992) Biochemistry , vol.31 , pp. 7436-7440
    • Zeidel, M.L.1    Ambudkar, S.V.2    Smith, B.L.3    Agre, P.4
  • 6
    • 0026031446 scopus 로고
    • Epitope tagging and protein surveillance
    • Kolodziej P. A., Young R. A. Epitope tagging and protein surveillance. Methods Enzymol. 194:1991;508-519.
    • (1991) Methods Enzymol. , vol.194 , pp. 508-519
    • Kolodziej, P.A.1    Young, R.A.2
  • 7
    • 0023368570 scopus 로고
    • Purification and characterization of constitutive secretory vesicles from yeast
    • Walworth N. C., Novick P. J. Purification and characterization of constitutive secretory vesicles from yeast. J. Cell. Biol. 105:1987;163-174.
    • (1987) J. Cell. Biol. , vol.105 , pp. 163-174
    • Walworth, N.C.1    Novick, P.J.2
  • 8
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:1976;248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 9
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 10
    • 0023664635 scopus 로고
    • Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes
    • Matsudaira P. Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes. J. Biol. Chem. 262:1987;10035-10038.
    • (1987) J. Biol. Chem. , vol.262 , pp. 10035-10038
    • Matsudaira, P.1
  • 11
    • 0021105845 scopus 로고
    • Incorporation of bacteriorhodopsin into large unilamellar liposomes by reverse phase evaporation
    • Rigaud J. L., Bluzat A., Buschlen S. Incorporation of bacteriorhodopsin into large unilamellar liposomes by reverse phase evaporation. Biochem. Biophys. Res. Commun. 111:1983;373-392.
    • (1983) Biochem. Biophys. Res. Commun. , vol.111 , pp. 373-392
    • Rigaud, J.L.1    Bluzat, A.2    Buschlen, S.3
  • 12
    • 0029056768 scopus 로고
    • Evidence for a glycerol pathway through aquaporin 1 (CHIP28) channels
    • Abrami L., Tacnet F., Ripoche P. Evidence for a glycerol pathway through aquaporin 1 (CHIP28) channels. Pflügers Arch. 430:1995;447-458.
    • (1995) Pflügers Arch. , vol.430 , pp. 447-458
    • Abrami, L.1    Tacnet, F.2    Ripoche, P.3
  • 13
    • 0022461542 scopus 로고
    • Osmotic water permeabilities of brush border and basolateral membrane vesicles from rat renal cortex and small intestine
    • Van Heeswijk M. P. E., Van Os C. H. Osmotic water permeabilities of brush border and basolateral membrane vesicles from rat renal cortex and small intestine. J. Membr. Biol. 92:1986;183-193.
    • (1986) J. Membr. Biol. , vol.92 , pp. 183-193
    • Van Heeswijk, M.P.E.1    Van Os, C.H.2
  • 14
    • 0027366423 scopus 로고
    • Secondary structure analysis of purified functional CHIP28 water channels by CD and FTIR spectroscopy
    • Van Hoek A. N., Wiener M., Bicknese S., Miercke L., Biwersi J., Verkman A. S. Secondary structure analysis of purified functional CHIP28 water channels by CD and FTIR spectroscopy. Biochemistry. 32:1993;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
  • 15
    • 0027472168 scopus 로고
    • The mercury-sensitive residue at cysteine-189 in the CHIP28 water channel
    • Preston G. M., Jung J. S., Guggino W. B., Agre P. The mercury-sensitive residue at cysteine-189 in the CHIP28 water channel. J. Biol. Chem. 268:1993;17-20.
    • (1993) J. Biol. Chem. , vol.268 , pp. 17-20
    • Preston, G.M.1    Jung, J.S.2    Guggino, W.B.3    Agre, P.4
  • 16
    • 0027503110 scopus 로고
    • A point mutation at cysteine 189 blocks the water permeability of rat kidney water channel CHIP28k
    • Zhang R., Van Hoek A. N., Biwersi J., Verkman A. S. A point mutation at cysteine 189 blocks the water permeability of rat kidney water channel CHIP28k. Biochemistry. 32:1993;2938-2941.
    • (1993) Biochemistry , vol.32 , pp. 2938-2941
    • Zhang, R.1    Van Hoek, A.N.2    Biwersi, J.3    Verkman, A.S.4
  • 17
    • 0029151926 scopus 로고
    • High level expression, partial purification, and functional reconstitution of the human AE1 anion exchanger in Saccharomyces cerevisiae
    • Sekler I., Kopito R., Casey J. R. High level expression, partial purification, and functional reconstitution of the human AE1 anion exchanger in Saccharomyces cerevisiae. J. Biol. Chem. 270:1995;21028-21034.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21028-21034
    • Sekler, I.1    Kopito, R.2    Casey, J.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.