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Volumn 10, Issue 1, 1997, Pages 61-69

Functional expression of bovine opsin in the methylotrophic yeast Pichia pastoris

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EID: 0031172606     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1006/prep.1996.0704     Document Type: Article
Times cited : (37)

References (46)
  • 3
    • 0020524517 scopus 로고
    • Isolation, sequence analysis, and intron-exon arrangement of the gene encoding bovine rhodopsin
    • Nathans J., Hogness D. S. Isolation, sequence analysis, and intron-exon arrangement of the gene encoding bovine rhodopsin. Cell. 34:1983;807-814.
    • (1983) Cell , vol.34 , pp. 807-814
    • Nathans, J.1    Hogness, D.S.2
  • 5
    • 0019331937 scopus 로고
    • The N-terminal residue of bovine rhodopsin is acetylmethionine
    • Tsunasawa S., Narita K., Shichi H. The N-terminal residue of bovine rhodopsin is acetylmethionine. Biochim. Biophys. Acta. 624:1980;218-225.
    • (1980) Biochim. Biophys. Acta , vol.624 , pp. 218-225
    • Tsunasawa, S.1    Narita, K.2    Shichi, H.3
  • 6
    • 0018787250 scopus 로고
    • Rhodopsin carbohydrate: Structure of small oligosaccharides attached at two sites near the amino terminus
    • Fukuda M. N., Papermaster D. S., Hargrave P. A. Rhodopsin carbohydrate: Structure of small oligosaccharides attached at two sites near the amino terminus. J. Biol. Chem. 254:1979;8201-8207.
    • (1979) J. Biol. Chem. , vol.254 , pp. 8201-8207
    • Fukuda, M.N.1    Papermaster, D.S.2    Hargrave, P.A.3
  • 7
    • 0023859049 scopus 로고
    • Two adjacent cysteines in the C-terminal cytoplasmic tail of rhodopsin are palmitoylated
    • Ovchinnikov Yu. A., Abdulaev N. G., Bogachuck A. S. Two adjacent cysteines in the C-terminal cytoplasmic tail of rhodopsin are palmitoylated. FEBS Lett. 230:1988;1-5.
    • (1988) FEBS Lett. , vol.230 , pp. 1-5
    • Ovchinnikov, Yu.A.1    Abdulaev, N.G.2    Bogachuck, A.S.3
  • 8
    • 0025085912 scopus 로고
    • Assembly of functional rhodopsin requires a disulfide bond between cysteine residues 110 and 187
    • Karnik S. S., Khorana H. G. Assembly of functional rhodopsin requires a disulfide bond between cysteine residues 110 and 187. J. Biol. Chem. 265:1990;17520-17524.
    • (1990) J. Biol. Chem. , vol.265 , pp. 17520-17524
    • Karnik, S.S.1    Khorana, H.G.2
  • 9
    • 0027190359 scopus 로고
    • Projection structure of visual rhodopsin
    • Schertler G. F. X., Villa C., Henderson R. Projection structure of visual rhodopsin. Nature. 362:1993;770-772.
    • (1993) Nature , vol.362 , pp. 770-772
    • Schertler, G.F.X.1    Villa, C.2    Henderson, R.3
  • 10
    • 0026602063 scopus 로고
    • Rhodopsin, photoreceptor of the rod cell: An emerging pattern for structure and function
    • Khorana H. G. Rhodopsin, photoreceptor of the rod cell: An emerging pattern for structure and function. J. Biol. Chem. 267:1992;1-5.
    • (1992) J. Biol. Chem. , vol.267 , pp. 1-5
    • Khorana, H.G.1
  • 12
  • 13
    • 0025524679 scopus 로고
    • Crystallization of membrane proteins: Bovine rhodopsin
    • Yurkova E. I., Demin V. V., Abdulaev N. G. Crystallization of membrane proteins: Bovine rhodopsin. Biomed. Sci. 1:1990;585-590.
    • (1990) Biomed. Sci. , vol.1 , pp. 585-590
    • Yurkova, E.I.1    Demin, V.V.2    Abdulaev, N.G.3
  • 14
    • 0027109279 scopus 로고
    • Studies towards the crystallization of the rod visual pigment rhodopsin
    • DeGrip W. J., van Oostrum J., de Caluwe G. L. S. Studies towards the crystallization of the rod visual pigment rhodopsin. J. Crystal Growth. 122:1992;375-384.
    • (1992) J. Crystal Growth , vol.122 , pp. 375-384
    • Degrip, W.J.1    Van Oostrum, J.2    De Caluwe, G.L.S.3
  • 16
    • 0029993499 scopus 로고    scopus 로고
    • Examining rhodopsin folding and assembly through expression of polypeptide fragments
    • Ridge K. D., Lee S. S. J., Abdulaev N. G. Examining rhodopsin folding and assembly through expression of polypeptide fragments. J. Biol. Chem. 271:1996;7860-7867.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7860-7867
    • Ridge, K.D.1    Lee, S.S.J.2    Abdulaev, N.G.3
  • 18
    • 0024324759 scopus 로고
    • Production of bovine rhodopsin by mammalian cell lines expressing cloned cDNA: Spectrophotometry and subcellular localization
    • Nathans J., Weitz C. J., Agarwal N., Nir I., Papermaster D. S. Production of bovine rhodopsin by mammalian cell lines expressing cloned cDNA: Spectrophotometry and subcellular localization. Vision Res. 29:1989;907-914.
    • (1989) Vision Res. , vol.29 , pp. 907-914
    • Nathans, J.1    Weitz, C.J.2    Agarwal, N.3    Nir, I.4    Papermaster, D.S.5
  • 19
    • 0010392278 scopus 로고
    • Expression of a bovine rhodopsin gene in xenopus oocytes: Demonstration of light-dependent ionic currents
    • Khorana H. G., Knox B. E., Nasi E., Swanson R., Thompson D. A. Expression of a bovine rhodopsin gene in xenopus oocytes: Demonstration of light-dependent ionic currents. Proc. Natl. Acad. Sci. USA. 85:1988;7917-7921.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 7917-7921
    • Khorana, H.G.1    Knox, B.E.2    Nasi, E.3    Swanson, R.4    Thompson, D.A.5
  • 22
    • 0029073041 scopus 로고
    • Histidine tagging both allows convenient single-step purification of bovine rhodopsin and exerts ionic strength-dependent effects on its photochemistry
    • Jansen J. J. M., Bovee-Geurts P. H. M., Merkx M., DeGrip W. J. Histidine tagging both allows convenient single-step purification of bovine rhodopsin and exerts ionic strength-dependent effects on its photochemistry. J. Biol. Chem. 270:1995;11222-11229.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11222-11229
    • Jansen, J.J.M.1    Bovee-Geurts, P.H.M.2    Merkx, M.3    Degrip, W.J.4
  • 24
    • 0026008209 scopus 로고
    • Anti-rhodopsin monoclonal antibodies of defined specificity: Characterization and application
    • Adamus G., Zam Z. S., Arendt A., Palczewski K., McDowell J. H., Hargrave P. A. Anti-rhodopsin monoclonal antibodies of defined specificity: Characterization and application. Vision Res. 31:1991;17-31.
    • (1991) Vision Res. , vol.31 , pp. 17-31
    • Adamus, G.1    Zam, Z.S.2    Arendt, A.3    Palczewski, K.4    McDowell, J.H.5    Hargrave, P.A.6
  • 25
    • 0022571973 scopus 로고
    • Differential immunogold-dextran labeling of bovine and frog rod and cone cells using monoclonal antibodies against bovine rhodopsin
    • Hicks D., Molday R. S. Differential immunogold-dextran labeling of bovine and frog rod and cone cells using monoclonal antibodies against bovine rhodopsin. Exp. Eye Res. 42:1986;55-71.
    • (1986) Exp. Eye Res. , vol.42 , pp. 55-71
    • Hicks, D.1    Molday, R.S.2
  • 26
    • 0027195585 scopus 로고
    • Absolute quantification of target DNA: A simple competitive PCR for efficient analysis of multiple samples
    • Zachar V., Thomas R. A., Goustin A. S. Absolute quantification of target DNA: A simple competitive PCR for efficient analysis of multiple samples. Nucleic Acid Res. 21:1993;2017-2018.
    • (1993) Nucleic Acid Res. , vol.21 , pp. 2017-2018
    • Zachar, V.1    Thomas, R.A.2    Goustin, A.S.3
  • 27
    • 0029081036 scopus 로고
    • Method for constructing internal standards for use in competitive PCR
    • Zarlenga D. S., Canals A., Gasbarre L. Method for constructing internal standards for use in competitive PCR. Biotechniques. 19:1995;324-326.
    • (1995) Biotechniques , vol.19 , pp. 324-326
    • Zarlenga, D.S.1    Canals, A.2    Gasbarre, L.3
  • 28
    • 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. 277:1970;680-685.
    • (1970) Nature , vol.277 , pp. 680-685
    • Laemmli, U.K.1
  • 29
    • 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
  • 30
    • 0016253492 scopus 로고
    • Rhodopsin content in outer segment membranes of bovine and frog retinal rods
    • Papermaster D. S., Dreyer W. J. Rhodopsin content in outer segment membranes of bovine and frog retinal rods. Biochemistry. 13:1974;2438-2444.
    • (1974) Biochemistry , vol.13 , pp. 2438-2444
    • Papermaster, D.S.1    Dreyer, W.J.2
  • 31
    • 0028081167 scopus 로고
    • High-level secretion and very efficient isotopic labeling of tick anticoagulant peptide (TAP) expressed in the methylotrophic yeast,Pichia pastoris
    • Laroche Y., Storme V., De Meutter J., Messens J., Lauwereys M. High-level secretion and very efficient isotopic labeling of tick anticoagulant peptide (TAP) expressed in the methylotrophic yeast,Pichia pastoris. Bio/Technology. 12:1994;1119-1124.
    • (1994) Bio/Technology , vol.12 , pp. 1119-1124
    • Laroche, Y.1    Storme, V.2    De Meutter, J.3    Messens, J.4    Lauwereys, M.5
  • 32
    • 0029151926 scopus 로고
    • High level expression, partial purification, and functional reconstitution of the human AE1 anion exchanger inSaccharomyces cerevisiae
    • Sekler I., Kopito R., Casey J. R. High level expression, partial purification, and functional reconstitution of the human AE1 anion exchanger inSaccharomyces 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
  • 33
    • 0342541430 scopus 로고
    • Rhodopsin chemistry, structure and topography
    • Hargrave P. A. Rhodopsin chemistry, structure and topography. Prog. Ret. Res. 1:1982;1-51.
    • (1982) Prog. Ret. Res. , vol.1 , pp. 1-51
    • Hargrave, P.A.1
  • 34
    • 0028922277 scopus 로고
    • Structure and function in rhodopsin: Separation and characterization of the correctly folded and misfolded opsins produced on expression of an opsin gene containing only the native intradiscal cysteine codons
    • Ridge K. D., Lu Z., Liu X., Khorana H. G. Structure and function in rhodopsin: Separation and characterization of the correctly folded and misfolded opsins produced on expression of an opsin gene containing only the native intradiscal cysteine codons. Biochemistry. 34:1995;3261-3267.
    • (1995) Biochemistry , vol.34 , pp. 3261-3267
    • Ridge, K.D.1    Lu, Z.2    Liu, X.3    Khorana, H.G.4
  • 35
    • 0000073823 scopus 로고
    • The molar extinction of rhodopsin
    • Wald G., Brown P. K. The molar extinction of rhodopsin. J. Gen. Physiol. 37:1953;189-200.
    • (1953) J. Gen. Physiol. , vol.37 , pp. 189-200
    • Wald, G.1    Brown, P.K.2
  • 36
    • 0029142564 scopus 로고
    • Overexpression of integral membrane proteins for structural studies
    • Grisshammer R., Tate C. G. Overexpression of integral membrane proteins for structural studies. Q. Rev. Biophys. 28:1995;315-422.
    • (1995) Q. Rev. Biophys. , vol.28 , pp. 315-422
    • Grisshammer, R.1    Tate, C.G.2
  • 43
    • 14744299579 scopus 로고
    • Recent advances in the expression of foreign genes inPichia pastoris
    • Cregg J. M., Vedvick T. S., Raschke W. C. Recent advances in the expression of foreign genes inPichia pastoris. Bio/Technology. 11:1993;905-910.
    • (1993) Bio/Technology , vol.11 , pp. 905-910
    • Cregg, J.M.1    Vedvick, T.S.2    Raschke, W.C.3
  • 44
    • 0028354244 scopus 로고
    • Structure and function in rhodopsin: The role of asparagine-linked glycosylation
    • Kaushal S., Ridge K. D., Khorana H. G. Structure and function in rhodopsin: The role of asparagine-linked glycosylation. Proc. Natl. Acad. Sci. USA. 91:1994;4029-4033.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 4029-4033
    • Kaushal, S.1    Ridge, K.D.2    Khorana, H.G.3
  • 45
    • 0026058548 scopus 로고
    • Functional heterogeneity of mutant rhodopsins responsible for autosomal dominant retinitis pigmentosa
    • Sung C.-H., Schneider B. G., Agarwal N., Papermaster D. S., Nathans J. Functional heterogeneity of mutant rhodopsins responsible for autosomal dominant retinitis pigmentosa. Proc. Natl. Acad. Sci. USA. 88:1991;8840-8844.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 8840-8844
    • Sung, C.-H.1    Schneider, B.G.2    Agarwal, N.3    Papermaster, D.S.4    Nathans, J.5
  • 46
    • 0029859488 scopus 로고    scopus 로고
    • Structure and function in rhodopsin: Expression of functional mammalian opsin inSaccharomyces cerevisiae
    • Mollaaghababa R., Davidson F. F., Kaiser C., Khorana H. G. Structure and function in rhodopsin: Expression of functional mammalian opsin inSaccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA. 93:1996;11482-11486.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 11482-11486
    • Mollaaghababa, R.1    Davidson, F.F.2    Kaiser, C.3    Khorana, H.G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.