메뉴 건너뛰기




Volumn 84, Issue 3, 2003, Pages 292-304

Co-expression of molecular chaperones does not improve the heterologous expression of mammalian G-protein coupled receptor expression in yeast

Author keywords

BiP; Calnexin; Folding bottleneck; GPCR; Heterologous expression; Neurokinin 1; NK 1; PDI

Indexed keywords

BIOLOGICAL MEMBRANES; CELLS; CHEMICAL BONDS; COBALT; PLASMAS; PROTEINS; YEAST;

EID: 0141533196     PISSN: 00063592     EISSN: None     Source Type: Journal    
DOI: 10.1002/bit.10771     Document Type: Article
Times cited : (60)

References (66)
  • 1
    • 0032486771 scopus 로고    scopus 로고
    • Leader peptide efficiency correlates with signal recognition particle dependence in Saccharomyces cerevisiae
    • Arnold CE, Parekh RN, Yang WL, Wittrup KD. 1998. Leader peptide efficiency correlates with signal recognition particle dependence in Saccharomyces cerevisiae. Biotechnol Bioeng 59:286-293.
    • (1998) Biotechnol Bioeng , vol.59 , pp. 286-293
    • Arnold, C.E.1    Parekh, R.N.2    Yang, W.L.3    Wittrup, K.D.4
  • 2
    • 0025974216 scopus 로고
    • High-efficiency transformation of yeast by electroportation
    • Becker D, Guarente L. 1991. High-efficiency transformation of yeast by electroportation. Meth Enzymol 194:182-187.
    • (1991) Meth Enzymol , vol.194 , pp. 182-187
    • Becker, D.1    Guarente, L.2
  • 3
    • 0002785346 scopus 로고
    • Basic concepts to analyze binding data using personal computers: The "RECEPT" program
    • Cattabeni F, Nicosia S (Eds.). New York: Plenum Press
    • Benfenati F, Guardabasso V. 1984. Basic concepts to analyze binding data using personal computers: The "RECEPT" program (p. 41-63). In Cattabeni F, Nicosia S (Eds.), Principles and methods in receptor binding. New York: Plenum Press.
    • (1984) Principles and Methods in Receptor Binding , pp. 41-63
    • Benfenati, F.1    Guardabasso, V.2
  • 4
    • 0034664985 scopus 로고    scopus 로고
    • Requirement of N-glycosylation of the prostaglandin E-2 receptor EP3 beta for correct sorting to the plasma membrane but not for correct folding
    • Boer U, Neuschafer-Rube F, Moller U, Puschel GP. 2000. Requirement of N-glycosylation of the prostaglandin E-2 receptor EP3 beta for correct sorting to the plasma membrane but not for correct folding. Biochem J 350:839-847.
    • (2000) Biochem J , vol.350 , pp. 839-847
    • Boer, U.1    Neuschafer-Rube, F.2    Moller, U.3    Puschel, G.P.4
  • 6
    • 0030069077 scopus 로고    scopus 로고
    • The peptide binding site of the substance P (NK-1) receptor localized by a photoreactive analogue of substance P: Presence of a disulfide bond
    • Boyd ND, Kage R, Dumas JJ, Krause JE, Leeman SE. 1996. The peptide binding site of the substance P (NK-1) receptor localized by a photoreactive analogue of substance P: Presence of a disulfide bond. Proc Natl Acad Sci USA 93:433-437.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 433-437
    • Boyd, N.D.1    Kage, R.2    Dumas, J.J.3    Krause, J.E.4    Leeman, S.E.5
  • 7
    • 0027759380 scopus 로고
    • A SEC63P-BiP complex from yeast is required for protein translocation in a reconstituted proteoliposome
    • Brodsky J, Scheckman R. 1993. A SEC63P-BiP complex from yeast is required for protein translocation in a reconstituted proteoliposome. J Cell Biol 123:1355-1363.
    • (1993) J Cell Biol , vol.123 , pp. 1355-1363
    • Brodsky, J.1    Scheckman, R.2
  • 8
    • 0031050445 scopus 로고    scopus 로고
    • Yeast-enhanced green fluorescent protein (yEGFP): A reporter of gene expression in Candida albicans
    • Cormack B, Bertram G, Egerton M, Gow N, Falkow S, Brown A. 1997. Yeast-enhanced green fluorescent protein (yEGFP): A reporter of gene expression in Candida albicans. Microbiology-UK 143:303-311.
    • (1997) Microbiology-UK , vol.143 , pp. 303-311
    • Cormack, B.1    Bertram, G.2    Egerton, M.3    Gow, N.4    Falkow, S.5    Brown, A.6
  • 9
    • 0034281801 scopus 로고    scopus 로고
    • Effect of PDI overexpression on recombinant protein secretion in CHO cells
    • Davis R, Schooley K, Rasmussen B, Thomas J, Reddy P. 2000. Effect of PDI overexpression on recombinant protein secretion in CHO cells. Biotechnol Prog 16:736-743.
    • (2000) Biotechnol Prog , vol.16 , pp. 736-743
    • Davis, R.1    Schooley, K.2    Rasmussen, B.3    Thomas, J.4    Reddy, P.5
  • 10
    • 0028291264 scopus 로고
    • The levels of endoplasmic-reticulum proteins and ATP effect folding and secretion of selective proteins
    • Dorner A, Kaufmam R. 1994. The levels of endoplasmic-reticulum proteins and ATP effect folding and secretion of selective proteins. Biologicals 22:103-112.
    • (1994) Biologicals , vol.22 , pp. 103-112
    • Dorner, A.1    Kaufmam, R.2
  • 11
    • 0033934481 scopus 로고    scopus 로고
    • Akr1p and the type I casein kinases act prior to the ubiquitination step of yeast endocytosis: Akr1p is required for kinase localization to the plasma membrane
    • Feng Y, Davis N. 2000. Akr1p and the type I casein kinases act prior to the ubiquitination step of yeast endocytosis: Akr1p is required for kinase localization to the plasma membrane. Mol Cell Biol 20:5350-5359.
    • (2000) Mol Cell Biol , vol.20 , pp. 5350-5359
    • Feng, Y.1    Davis, N.2
  • 12
    • 0029859847 scopus 로고    scopus 로고
    • Cyclophilin-related protein RanBP2 acts as chaperone for red/green opsin
    • Ferreira P, Nakayama T, Pak W, Travis G. 1996. Cyclophilin-related protein RanBP2 acts as chaperone for red/green opsin. Nature 383:637-640.
    • (1996) Nature , vol.383 , pp. 637-640
    • Ferreira, P.1    Nakayama, T.2    Pak, W.3    Travis, G.4
  • 13
    • 0026454825 scopus 로고
    • The extracellular domain of the neurokinin-1 receptor is required for high-affinity binding of peptides
    • Fong TM, Yu H, Huang RR, Strader CD. 1992. The extracellular domain of the neurokinin-1 receptor is required for high-affinity binding of peptides. Biochem 31:11806-11811.
    • (1992) Biochem , vol.31 , pp. 11806-11811
    • Fong, T.M.1    Yu, H.2    Huang, R.R.3    Strader, C.D.4
  • 14
    • 0000870776 scopus 로고
    • Native disulfide bond formation in protein-biosynthesis-Evidence for the role of protein disulfide isomerase
    • Freedman R. 1984. Native disulfide bond formation in protein-biosynthesis-Evidence for the role of protein disulfide isomerase. Trends Biochem Sci 9:438-441.
    • (1984) Trends Biochem Sci , vol.9 , pp. 438-441
    • Freedman, R.1
  • 15
    • 0031720851 scopus 로고    scopus 로고
    • N-terminal domain of Gpa1 (G protein alpha subunit) is sufficient for plasma membrane targeting in yeast Saccharomyces cerevisiae
    • Gillen K, Pausch M, Dohlman H. 1998. N-terminal domain of Gpa1 (G protein alpha subunit) is sufficient for plasma membrane targeting in yeast Saccharomyces cerevisiae. J Cell Sci 111:3235-3244.
    • (1998) J Cell Sci , vol.111 , pp. 3235-3244
    • Gillen, K.1    Pausch, M.2    Dohlman, H.3
  • 16
    • 0029142564 scopus 로고
    • Overexpression of integral membrane proteins for structural studies
    • Grisshammer R, Tate CG. 1995. Overexpression of integral membrane proteins for structural studies. Q Rev Biophys 28:315-422.
    • (1995) Q Rev Biophys , vol.28 , pp. 315-422
    • Grisshammer, R.1    Tate, C.G.2
  • 17
    • 0028076031 scopus 로고
    • Folding of VSV g-protein-sequential interaction with BiP and calnexin
    • Hammond C, Helenius A. 1994. Folding of VSV g-protein-sequential interaction with BiP and calnexin. Science 266:456-458.
    • (1994) Science , vol.266 , pp. 456-458
    • Hammond, C.1    Helenius, A.2
  • 18
    • 0035397488 scopus 로고    scopus 로고
    • Identification of the glycosylation sites utilized on the V-1a vasopressin receptor and assessment of their role in receptor signalling and expression
    • Hawtin SR, Davies ARL, Matthews G, Wheatley M. 2001. Identification of the glycosylation sites utilized on the V-1a vasopressin receptor and assessment of their role in receptor signalling and expression. Biochem J 357:73-81.
    • (2001) Biochem J , vol.357 , pp. 73-81
    • Hawtin, S.R.1    Davies, A.R.L.2    Matthews, G.3    Wheatley, M.4
  • 19
    • 0024426509 scopus 로고
    • Direct autoradiographic localization of adenosine-A2 receptors in the rat-brian using the A-2-selective agonist, [H-3] CGS 21680
    • Jarvis M, Williams M. 1989. Direct autoradiographic localization of adenosine-A2 receptors in the rat-brian using the A-2-selective agonist, [H-3] CGS 21680. Eur J Pharmacol 168:243-246.
    • (1989) Eur J Pharmacol , vol.168 , pp. 243-246
    • Jarvis, M.1    Williams, M.2
  • 20
    • 0029824179 scopus 로고    scopus 로고
    • 6-Phenyl-1,4-dihydropyridine derivatives as potent and selective A(3) adenosine receptor antagonists
    • Jiang J, vanRhee A, Melman N, Ji X, Jacobson K. 1996. 6-phenyl-1,4-dihydropyridine derivatives as potent and selective A(3) adenosine receptor antagonists. J Med Chem 39:4667-4675.
    • (1996) J Med Chem , vol.39 , pp. 4667-4675
    • Jiang, J.1    VanRhee, A.2    Melman, N.3    Ji, X.4    Jacobson, K.5
  • 21
    • 0028852748 scopus 로고
    • Characterization of the substance-P (Nk-1) receptor in tunicamycin-treated transfected cells using a photoaffinity analog of substance-P
    • Kage R, Hershey AD, Krause JE, Boyd ND, Leeman SE. 1995. Characterization of the substance-P (Nk-1) receptor in tunicamycin-treated transfected cells using a photoaffinity analog of substance-P. J Neurochem 64:316-321.
    • (1995) J Neurochem , vol.64 , pp. 316-321
    • Kage, R.1    Hershey, A.D.2    Krause, J.E.3    Boyd, N.D.4    Leeman, S.E.5
  • 22
    • 0028999737 scopus 로고
    • Sodium orthovanadate-resistant mutants of Saccharomyces cerevisiae show defects in golgi-mediated protein glycosylation, sporulation and detergent resistance
    • Kanikennulat C, Montalvo E, Neff N. 1995. Sodium orthovanadate-resistant mutants of Saccharomyces cerevisiae show defects in golgi-mediated protein glycosylation, sporulation and detergent resistance. Genetics 140:933-943.
    • (1995) Genetics , vol.140 , pp. 933-943
    • Kanikennulat, C.1    Montalvo, E.2    Neff, N.3
  • 23
    • 0028801931 scopus 로고
    • Calnexin and BiP act as sequential molecular chaperones during thyroglobulin folding in the endoplasmic-reticulum
    • Kim P, Arvan P. 1995. Calnexin and BiP act as sequential molecular chaperones during thyroglobulin folding in the endoplasmic-reticulum. J Cell Biol 128:29-38.
    • (1995) J Cell Biol , vol.128 , pp. 29-38
    • Kim, P.1    Arvan, P.2
  • 24
    • 0029960789 scopus 로고    scopus 로고
    • Glutamate residues in the second extracellular loop of the human A2a adenosine receptor are required for ligand recognition
    • Kim J, Jiang Q, Glashofer M, Yehle S, Wess J, Jacobson KA. 1996. Glutamate residues in the second extracellular loop of the human A2a adenosine receptor are required for ligand recognition. Mol Pharmacol 49:683-691.
    • (1996) Mol Pharmacol , vol.49 , pp. 683-691
    • Kim, J.1    Jiang, Q.2    Glashofer, M.3    Yehle, S.4    Wess, J.5    Jacobson, K.A.6
  • 25
    • 0029379610 scopus 로고
    • Production of rat protein disulfide-isomerase in Saccharomyces cerevisiae
    • Laboissiere M, Chivers P, Raines R. 1995. Production of rat protein disulfide-isomerase in Saccharomyces cerevisiae. Prot Expr Purif 6:700-706.
    • (1995) Prot Expr Purif , vol.6 , pp. 700-706
    • Laboissiere, M.1    Chivers, P.2    Raines, R.3
  • 26
    • 0033529236 scopus 로고    scopus 로고
    • Role of N-glycosylation in the expression and functional properties of human AT(1) receptor
    • Lanctot PM, Leclerc PC, Escher E, Leduc R, Guillemette G. 1999. Role of N-glycosylation in the expression and functional properties of human AT(1) receptor. Biochemistry 38:8621-8627.
    • (1999) Biochemistry , vol.38 , pp. 8621-8627
    • Lanctot, P.M.1    Leclerc, P.C.2    Escher, E.3    Leduc, R.4    Guillemette, G.5
  • 27
    • 0025195574 scopus 로고
    • Binding characteristics of I-125 Bolton-Hunter Sar9, Met(O2)11 Substance-P, a new selective radioligand for the Nk1 Receptor
    • Lew R, Geraghty DP, Drapeau G, Regoli D, Burcher E. 1990. Binding characteristics of I-125 Bolton-Hunter Sar9, Met(O2)11 Substance-P, a new selective radioligand for the Nk1 Receptor. Eur J Pharmacol 184:97-108.
    • (1990) Eur J Pharmacol , vol.184 , pp. 97-108
    • Lew, R.1    Geraghty, D.P.2    Drapeau, G.3    Regoli, D.4    Burcher, E.5
  • 28
    • 0032941754 scopus 로고    scopus 로고
    • Yeast mutants affecting possible quality control of plasma membrane proteins
    • Li Y et al. 1999. Yeast mutants affecting possible quality control of plasma membrane proteins. Mol Cell Biol 19:3588-3599.
    • (1999) Mol Cell Biol , vol.19 , pp. 3588-3599
    • Li, Y.1
  • 29
    • 0033999819 scopus 로고    scopus 로고
    • An endosome-to-plasma membrane pathway involved in trafficking of a mutant plasma membrane ATPase in yeast
    • Luo WJ, Chang A. 2000. An endosome-to-plasma membrane pathway involved in trafficking of a mutant plasma membrane ATPase in yeast. Mol Biol Cell 11:579-592.
    • (2000) Mol Biol Cell , vol.11 , pp. 579-592
    • Luo, W.J.1    Chang, A.2
  • 30
    • 0034031594 scopus 로고    scopus 로고
    • Recognizing misfolded proteins in the endoplasmic reticulum
    • Matouschek A. 2000. Recognizing misfolded proteins in the endoplasmic reticulum. Nature Struct Biol 7:265-266.
    • (2000) Nature Struct Biol , vol.7 , pp. 265-266
    • Matouschek, A.1
  • 33
    • 0028170231 scopus 로고
    • Sequential interaction of the chaperones BiP and GRP94 with immunoglobulin-chains in the endoplasmic-reticulum
    • Melnick J, Dul J, Argon Y. 1994. Sequential interaction of the chaperones BiP and GRP94 with immunoglobulin-chains in the endoplasmic-reticulum. Nature 370:373-375.
    • (1994) Nature , vol.370 , pp. 373-375
    • Melnick, J.1    Dul, J.2    Argon, Y.3
  • 34
    • 0035859796 scopus 로고    scopus 로고
    • Mutational analysis of the role of N-glycosylation in alpha-factor receptor function
    • Mentesana P, Konopka J. 2001. Mutational analysis of the role of N-glycosylation in alpha-factor receptor function. Biochem 40:9685-9694.
    • (2001) Biochem , vol.40 , pp. 9685-9694
    • Mentesana, P.1    Konopka, J.2
  • 35
    • 0034646876 scopus 로고    scopus 로고
    • Chaperone selection during glycoprotein translocation into the endoplasmic reticulum
    • Molinari M, Helenius A. 2000. Chaperone selection during glycoprotein translocation into the endoplasmic reticulum. Science 288:331-333.
    • (2000) Science , vol.288 , pp. 331-333
    • Molinari, M.1    Helenius, A.2
  • 36
    • 0034846624 scopus 로고    scopus 로고
    • Adenosine, adenosine receptors and myocardial protection: An updated overview
    • Mubagwa K, Flameng W. 2001. Adenosine, adenosine receptors and myocardial protection: An updated overview. Cardiovasc Res 52:25-39.
    • (2001) Cardiovasc Res , vol.52 , pp. 25-39
    • Mubagwa, K.1    Flameng, W.2
  • 37
    • 0031543433 scopus 로고    scopus 로고
    • G-protein-coupled receptors in Saccharomyces cerevisiae: High-throughput screening assays for drug discovery
    • Pausch M. 1997. G-protein-coupled receptors in Saccharomyces cerevisiae: High-throughput screening assays for drug discovery. Trends Biotechnol 15:487-494.
    • (1997) Trends Biotechnol , vol.15 , pp. 487-494
    • Pausch, M.1
  • 38
    • 0031104672 scopus 로고    scopus 로고
    • Expression level tuning for optimal heterologous protein secretion in Saccharomyces cerevisiae
    • Parekh RN, Wittrup KD. 1997. Expression level tuning for optimal heterologous protein secretion in Saccharomyces cerevisiae. Biotechnol Prog 13:117-122.
    • (1997) Biotechnol Prog , vol.13 , pp. 117-122
    • Parekh, R.N.1    Wittrup, K.D.2
  • 39
    • 0028881645 scopus 로고
    • Saccharomyces cerevisiae CNE1 encodes an endoplasmic-reticulum (ER) membrane-protein with sequence similarity to calnexin and calreticulin and functions as a constituent of the ER quality-control apparatus
    • Parlati F, Dominguez M, Bergeron J, Thomas D. 1995. Saccharomyces cerevisiae CNE1 encodes an endoplasmic-reticulum (ER) membrane-protein with sequence similarity to calnexin and calreticulin and functions as a constituent of the ER quality-control apparatus. J Biol Chem 270:244-253.
    • (1995) J Biol Chem , vol.270 , pp. 244-253
    • Parlati, F.1    Dominguez, M.2    Bergeron, J.3    Thomas, D.4
  • 40
    • 0034607918 scopus 로고    scopus 로고
    • Export from the endoplasmic reticulum represents the limiting step in the maturation and cell surface expression of the human delta opioid receptor
    • Petaja-Repo UE, Hogue M, Laperriere A, Walker P, Bouvier M. 2000. Export from the endoplasmic reticulum represents the limiting step in the maturation and cell surface expression of the human delta opioid receptor. J Biol Chem 275:13727-13736.
    • (2000) J Biol Chem , vol.275 , pp. 13727-13736
    • Petaja-Repo, U.E.1    Hogue, M.2    Laperriere, A.3    Walker, P.4    Bouvier, M.5
  • 41
    • 0028290280 scopus 로고
    • A carboxyl-terminally truncated mutant and nonglycosylated A(2a) adenosine receptors retain ligand binding
    • Piersen C, True C, Wells J. 1994. A carboxyl-terminally truncated mutant and nonglycosylated A(2a) adenosine receptors retain ligand binding. Mol Pharmacol 45:861-870.
    • (1994) Mol Pharmacol , vol.45 , pp. 861-870
    • Piersen, C.1    True, C.2    Wells, J.3
  • 42
    • 0029862555 scopus 로고    scopus 로고
    • Pharmacological characterization of the rat A(2a) adenosine receptor functionally coupled to the yeast pheromone response pathway
    • Price L, Strnad J, Pausch M, Hadcock J. 1996. Pharmacological characterization of the rat A(2a) adenosine receptor functionally coupled to the yeast pheromone response pathway. Mol Pharmacol 50:829-837.
    • (1996) Mol Pharmacol , vol.50 , pp. 829-837
    • Price, L.1    Strnad, J.2    Pausch, M.3    Hadcock, J.4
  • 43
    • 0028840683 scopus 로고
    • Functional coupling of a mammalian somatostatin receptor to the yeast pheromone response pathway
    • Price LA, Kajkowski EM, Hadcock JR, Ozenberger BA, Pausch MH. 1995. Functional coupling of a mammalian somatostatin receptor to the yeast pheromone response pathway. Mol Cell Biol 15:6188-6195.
    • (1995) Mol Cell Biol , vol.15 , pp. 6188-6195
    • Price, L.A.1    Kajkowski, E.M.2    Hadcock, J.R.3    Ozenberger, B.A.4    Pausch, M.H.5
  • 44
    • 0029862555 scopus 로고    scopus 로고
    • Pharmacological characterization of the rat A(2a) adenosine receptor functionally coupled to the yeast pheromone response pathway
    • Price LA, Strnad J, Pausch MH, Hadcock JR. 1996. Pharmacological characterization of the rat A(2a) adenosine receptor functionally coupled to the yeast pheromone response pathway. Mol Pharm 50:829-837.
    • (1996) Mol Pharm , vol.50 , pp. 829-837
    • Price, L.A.1    Strnad, J.2    Pausch, M.H.3    Hadcock, J.R.4
  • 46
    • 0031594899 scopus 로고    scopus 로고
    • The tachykinin NK1 receptor. Part II: Distribution and pathophysiological
    • Quartara L, Maggi CA. 1998. The tachykinin NK1 receptor. Part II: Distribution and pathophysiological. Neuropeptides 32:1-49.
    • (1998) Neuropeptides , vol.32 , pp. 1-49
    • Quartara, L.1    Maggi, C.A.2
  • 47
    • 0030990121 scopus 로고    scopus 로고
    • Physiological regulation of membrane protein sorting late in the secretory pathway of Saccharomyces cerevisiae
    • Roberg K, Rowley N, Kaiser C. 1997. Physiological regulation of membrane protein sorting late in the secretory pathway of Saccharomyces cerevisiae. J Cell Biol 137:1469-1482.
    • (1997) J Cell Biol , vol.137 , pp. 1469-1482
    • Roberg, K.1    Rowley, N.2    Kaiser, C.3
  • 48
    • 0029257263 scopus 로고
    • Constitutive overexpression of secreted heterologous proteins decreases extractable BiP and protein disulfide isomerase levels in Saccharomyces cerevisiae
    • Robinson A, Wittrup K. 1995. Constitutive overexpression of secreted heterologous proteins decreases extractable BiP and protein disulfide isomerase levels in Saccharomyces cerevisiae. Biotechnol Prog 11:171-177.
    • (1995) Biotechnol Prog , vol.11 , pp. 171-177
    • Robinson, A.1    Wittrup, K.2
  • 49
    • 0028219869 scopus 로고
    • Protein disulfide-isomerase over-expresssion increases secretion of foreign proteins in saccharomyces cerevisiae
    • Robinson A, Hines V, Wittrup K. 1994. Protein disulfide-isomerase over-expresssion increases secretion of foreign proteins in saccharomyces cerevisiae. BioTechnol 12:381-384.
    • (1994) BioTechnol , vol.12 , pp. 381-384
    • Robinson, A.1    Hines, V.2    Wittrup, K.3
  • 50
    • 0029944822 scopus 로고    scopus 로고
    • Reduction of BiP levels decreases heterologous protein secretion in Saccharomyces cerevisiae
    • Robinson AS, Bockhaus JA, Voegler AC, Wittrup KD. 1996. Reduction of BiP levels decreases heterologous protein secretion in Saccharomyces cerevisiae. J Biol Chem 271:10017-10022.
    • (1996) J Biol Chem , vol.271 , pp. 10017-10022
    • Robinson, A.S.1    Bockhaus, J.A.2    Voegler, A.C.3    Wittrup, K.D.4
  • 51
    • 0033526048 scopus 로고    scopus 로고
    • Golgi structure correlates with transitional endoplasmic reticulum organization in Pichia pastoris and Saccharomyces cerevisiae
    • Rossanese OW, Soderholm J, Bevis BJ, Sears IB, O'Connor J, Williamson EK, Glick BS. 1999. Golgi structure correlates with transitional endoplasmic reticulum organization in Pichia pastoris and Saccharomyces cerevisiae. J Cell Biol 145:69-81.
    • (1999) J Cell Biol , vol.145 , pp. 69-81
    • Rossanese, O.W.1    Soderholm, J.2    Bevis, B.J.3    Sears, I.B.4    O'Connor, J.5    Williamson, E.K.6    Glick, B.S.7
  • 52
    • 0034677991 scopus 로고    scopus 로고
    • Ubiquitination of the PEST-like endocytosis signal of the yeast a-factor receptor
    • Roth A, Davis N. 2000. Ubiquitination of the PEST-like endocytosis signal of the yeast a-factor receptor. J Biol Chem 275:8143-8153.
    • (2000) J Biol Chem , vol.275 , pp. 8143-8153
    • Roth, A.1    Davis, N.2
  • 53
    • 0031734361 scopus 로고    scopus 로고
    • Association of gonadotropin receptor precursors with the protein folding chaperone calnexin
    • Rozell T, Davis D, Chai Y, Segaloff D. 1998. Association of gonadotropin receptor precursors with the protein folding chaperone calnexin. Endocrinol 139:1588-1593.
    • (1998) Endocrinol , vol.139 , pp. 1588-1593
    • Rozell, T.1    Davis, D.2    Chai, Y.3    Segaloff, D.4
  • 54
    • 0028070288 scopus 로고
    • Constitutive expression of the humand D-2S-dopamine receptor in the unicellular yeast Saccharomyces cerevisiae
    • Sander P, Grunewald S, Maul G, Reilander H, Michel H. 1994. Constitutive expression of the humand D-2S-dopamine receptor in the unicellular yeast Saccharomyces cerevisiae. Biochem Biophys Acta-Biomembranes 1193:255-262.
    • (1994) Biochem Biophys Acta-Biomembranes , vol.1193 , pp. 255-262
    • Sander, P.1    Grunewald, S.2    Maul, G.3    Reilander, H.4    Michel, H.5
  • 55
    • 0026589260 scopus 로고
    • SEC61P and BiP directly facilitate polypeptide translocation in the ER
    • Sanders S, Whitfield K, Vogel J, Rose M, Scheckman R. 1992. SEC61P and BiP directly facilitate polypeptide translocation in the ER. Cell 69:353-365.
    • (1992) Cell , vol.69 , pp. 353-365
    • Sanders, S.1    Whitfield, K.2    Vogel, J.3    Rose, M.4    Scheckman, R.5
  • 56
    • 0035834428 scopus 로고    scopus 로고
    • Regulation of receptor fate by ubiquitination of activated beta(2)-adrenergic receptor and beta-arrestin
    • Shenoy S, McDonald P, Kohout T, Lefkowitz R. 2001. Regulation of receptor fate by ubiquitination of activated beta(2)-adrenergic receptor and beta-arrestin. Science 294:1307-1313.
    • (2001) Science , vol.294 , pp. 1307-1313
    • Shenoy, S.1    McDonald, P.2    Kohout, T.3    Lefkowitz, R.4
  • 57
    • 0031879861 scopus 로고    scopus 로고
    • Increasing the secretory capacity of Saccharomyces cerevisiae for production of single-chain antibody fragments
    • Shusta E, Raines R, Pluckthun A, Wittrup K. 1998. Increasing the secretory capacity of Saccharomyces cerevisiae for production of single-chain antibody fragments. Nature Biotechnol 16:773-777.
    • (1998) Nature Biotechnol , vol.16 , pp. 773-777
    • Shusta, E.1    Raines, R.2    Pluckthun, A.3    Wittrup, K.4
  • 59
    • 0026738643 scopus 로고
    • The yeast EUG1 gene encodes an endoplasmic-reticulum proteins that is functionally related to protein disulfide isomerase
    • Tachibana C, Stevens T. 1992. The yeast EUG1 gene encodes an endoplasmic-reticulum proteins that is functionally related to protein disulfide isomerase. Mol Cell Biol 12:4601-4611.
    • (1992) Mol Cell Biol , vol.12 , pp. 4601-4611
    • Tachibana, C.1    Stevens, T.2
  • 60
    • 0030298385 scopus 로고    scopus 로고
    • Heterologous expression of G-protein-coupled receptors
    • Tate C, Grisshammer R.1996. Heterologous expression of G-protein-coupled receptors. Trends Biotechnol 14:426-430.
    • (1996) Trends Biotechnol , vol.14 , pp. 426-430
    • Tate, C.1    Grisshammer, R.2
  • 61
    • 0033580920 scopus 로고    scopus 로고
    • Molecular chaperones stimulate the functional expression of the cocaine-sensitive serotonin transporter
    • Tate CG, Whiteley E, Betenbaugh MJ. 1999. Molecular chaperones stimulate the functional expression of the cocaine-sensitive serotonin transporter. J Biol Chem 274:17551-17558.
    • (1999) J Biol Chem , vol.274 , pp. 17551-17558
    • Tate, C.G.1    Whiteley, E.2    Betenbaugh, M.J.3
  • 62
    • 0025196660 scopus 로고
    • 1-125 Bh Sar9, Met(O2)11-Sp, a new selective ligand for the Nk-1 receptor in the central nervous system
    • Tousignant C, Guillemette G, Drapeau G, Telemaque S, Dion S, Regoli D. 1990. 1-125 Bh Sar9, Met(O2)11-Sp, a new selective ligand for the Nk-1 receptor in the central nervous system. Brain Res 524:263-270.
    • (1990) Brain Res , vol.524 , pp. 263-270
    • Tousignant, C.1    Guillemette, G.2    Drapeau, G.3    Telemaque, S.4    Dion, S.5    Regoli, D.6
  • 63
    • 0025339295 scopus 로고
    • Loss of BiP/GRP78 functions blocks translocation of secretory proteins in yeast
    • Vogel J, Misra L, Rose M. 1990. Loss of BiP/GRP78 functions blocks translocation of secretory proteins in yeast. J Cell Biol 110:1885-1895.
    • (1990) J Cell Biol , vol.110 , pp. 1885-1895
    • Vogel, J.1    Misra, L.2    Rose, M.3
  • 64
    • 0029079403 scopus 로고
    • Functional expression of low-density-lipoprotein receptor-related protein is controlled by receptor-associated protein in-vivo
    • Willnow T, Armstrong S, Hammer R, Herz J. 1995. Functional expression of low-density-lipoprotein receptor-related protein is controlled by receptor-associated protein in-vivo. Proc Natl Acad Sci USA 92:4537-4541.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 4537-4541
    • Willnow, T.1    Armstrong, S.2    Hammer, R.3    Herz, J.4
  • 65
    • 0033230290 scopus 로고    scopus 로고
    • Facilitating the formation of disulfide bonds in the Escherichia coli periplasm via coexpression of yeast protein disulfide isomerase
    • Zhan X, Schwaller M, Gilbert H, Georgiou G. 1999. Facilitating the formation of disulfide bonds in the Escherichia coli periplasm via coexpression of yeast protein disulfide isomerase. Biotechnol Prog 15:1033-1038.
    • (1999) Biotechnol Prog , vol.15 , pp. 1033-1038
    • Zhan, X.1    Schwaller, M.2    Gilbert, H.3    Georgiou, G.4
  • 66
    • 0034757165 scopus 로고    scopus 로고
    • Hsp70 molecular chaperone facilitates endoplasmic reticulum-associated protein degradation of cystic fibrosis transmembrane conductance regulator in yeast
    • Zhang Y, Nijbroek G, Sullivan M, McCracken A, Watkins S, Michaelis S, Brodsky J. 2001. Hsp70 molecular chaperone facilitates endoplasmic reticulum-associated protein degradation of cystic fibrosis transmembrane conductance regulator in yeast. Mol Biol Cell 12:1303-1314.
    • (2001) Mol Biol Cell , vol.12 , pp. 1303-1314
    • Zhang, Y.1    Nijbroek, G.2    Sullivan, M.3    McCracken, A.4    Watkins, S.5    Michaelis, S.6    Brodsky, J.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.