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Volumn 1, Issue , 2008, Pages 73-104

Studying Protein Folding in Vivo

Author keywords

Diluted system; Population; Proteins; Resistance; Termination

Indexed keywords


EID: 84889864231     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9783527619498.ch36     Document Type: Chapter
Times cited : (2)

References (106)
  • 1
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Anfinsen, C. B. (1973). Principles that govern the folding of protein chains. Science 181, 223-230.
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 2
    • 0018679846 scopus 로고
    • Formation of an intrachain disulfide bond on nascent immunoglobulin light chains
    • Bergman, L. W. & Kuehl, W. M. (1979). Formation of an intrachain disulfide bond on nascent immunoglobulin light chains. J Biol Chem 254, 8869-8876.
    • (1979) J Biol Chem , vol.254 , pp. 8869-8876
    • Bergman, L.W.1    Kuehl, W.M.2
  • 3
    • 0029049090 scopus 로고
    • Cotranslational folding and calnexin binding during glycoprotein synthesis
    • Chen, W., Helenius, J., Braakman, I. & Helenius, A. (1995). Cotranslational folding and calnexin binding during glycoprotein synthesis. Proc Natl Acad Sci USA 92, 6229-6233.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 6229-6233
    • Chen, W.1    Helenius, J.2    Braakman, I.3    Helenius, A.4
  • 4
    • 0020184671 scopus 로고
    • How crowded is the cytoplasm?
    • Fulton, A. B. (1982). How crowded is the cytoplasm? Cell 30, 345-347.
    • (1982) Cell , vol.30 , pp. 345-347
    • Fulton, A.B.1
  • 5
    • 0020668187 scopus 로고
    • The effect of volume occupancy upon the thermodynamic activity of proteins: some biochemical consequences
    • Minton, A. P. (1983). The effect of volume occupancy upon the thermodynamic activity of proteins: some biochemical consequences. Mol Cell Biochem 55, 119-140.
    • (1983) Mol Cell Biochem , vol.55 , pp. 119-140
    • Minton, A.P.1
  • 6
    • 0035478585 scopus 로고    scopus 로고
    • Macromolecular crowding: obvious but underappreciated
    • Ellis, R. J. (2001). Macromolecular crowding: obvious but underappreciated. Trends Biochem Sci 26, 597-604.
    • (2001) Trends Biochem Sci , vol.26 , pp. 597-604
    • Ellis, R.J.1
  • 7
    • 0029094253 scopus 로고
    • Quality control in the secretory pathway
    • Hammond, C. & Helenius, A. (1995). Quality control in the secretory pathway. Curr Opin Cell Biol 7, 523-529.
    • (1995) Curr Opin Cell Biol , vol.7 , pp. 523-529
    • Hammond, C.1    Helenius, A.2
  • 8
    • 0037040541 scopus 로고    scopus 로고
    • Molecular chaperones in the cytosol: from nascent chain to folded protein
    • Hartl, F. U. & Hayer-Hartl, M. (2002). Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 295, 1852-1858.
    • (2002) Science , vol.295 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 9
    • 0037336295 scopus 로고    scopus 로고
    • Quality control in the endoplasmic reticulum
    • Ellgaard, L. & Helenius, A. (2003). Quality control in the endoplasmic reticulum. Nat Rev Mol Cell Biol 4, 181-191.
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 181-191
    • Ellgaard, L.1    Helenius, A.2
  • 10
    • 0026584271 scopus 로고
    • Protein folding in the cell
    • Gething, M. J. & Sambrook, J. (1992). Protein folding in the cell. Nature 355, 33-45.
    • (1992) Nature , vol.355 , pp. 33-45
    • Gething, M.J.1    Sambrook, J.2
  • 11
    • 0025816663 scopus 로고
    • Folding of influenza hemagglutinin in the endoplasmic reticulum
    • Braakman, I., Hoover-Litty, H., Wagner, K. R. & Helenius, A. (1991). Folding of influenza hemagglutinin in the endoplasmic reticulum. J Cell Biol 114, 401-411.
    • (1991) J Cell Biol , vol.114 , pp. 401-411
    • Braakman, I.1    Hoover-Litty, H.2    Wagner, K.R.3    Helenius, A.4
  • 12
    • 0029024163 scopus 로고
    • The translocation, folding, assembly and redoxdependent degradation of secretory and membrane proteins in semipermeabilized mammalian cells
    • Wilson, R., Allen, A. J., Oliver, J., Brookman, J. L., High, S. & Bulleid, N. J. (1995). The translocation, folding, assembly and redoxdependent degradation of secretory and membrane proteins in semipermeabilized mammalian cells. Biochem J 307, 679-687.
    • (1995) Biochem J , vol.307 , pp. 679-687
    • Wilson, R.1    Allen, A.J.2    Oliver, J.3    Brookman, J.L.4    High, S.5    Bulleid, N.J.6
  • 13
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 14
    • 70449276523 scopus 로고
    • The hydrolysis of rabbit y-globulin and antibodies with crystalline papain
    • Porter, R. R. (1959). The hydrolysis of rabbit y-globulin and antibodies with crystalline papain. Biochem J 73, 119-126.
    • (1959) Biochem J , vol.73 , pp. 119-126
    • Porter, R.R.1
  • 15
    • 0014060675 scopus 로고
    • Determination of sulfhydryl groups with 2,20-or 4,40-dithiodipyridine
    • Grassetti, D. R. & Murray, J. F., Jr. (1967). Determination of sulfhydryl groups with 2,20-or 4,40-dithiodipyridine. Arch Biochem Biophys 119, 41-49.
    • (1967) Arch Biochem Biophys , vol.119 , pp. 41-49
    • Grassetti, D.R.1    Murray Jr., J.F.2
  • 16
    • 0035502932 scopus 로고    scopus 로고
    • Shedding light on disulfide bond formation: engineering a redox switch in green fluorescent protein
    • Ostergaard, H., Henriksen, A., Hansen, F. G. & Winther, J. R. (2001). Shedding light on disulfide bond formation: engineering a redox switch in green fluorescent protein. EMBO J 20, 5853-5862.
    • (2001) EMBO J , vol.20 , pp. 5853-5862
    • Ostergaard, H.1    Henriksen, A.2    Hansen, F.G.3    Winther, J.R.4
  • 17
    • 0014671931 scopus 로고
    • Lest I forget thee, glutathione
    • Kosower, E. M. & Kosower, N. S. (1969). Lest I forget thee, glutathione. Nature 224, 117-120.
    • (1969) Nature , vol.224 , pp. 117-120
    • Kosower, E.M.1    Kosower, N.S.2
  • 18
    • 0029006990 scopus 로고
    • Diamide: an oxidant probe for thiols
    • Kosower, N. S. & Kosower, E. M. (1995). Diamide: an oxidant probe for thiols. Methods Enzymol 251, 123-133.
    • (1995) Methods Enzymol , vol.251 , pp. 123-133
    • Kosower, N.S.1    Kosower, E.M.2
  • 20
    • 0026604334 scopus 로고
    • Manipulating disulfide bond formation and protein folding in the endoplasmic reticulum
    • Braakman, I., Helenius, J. & Helenius, A. (1992). Manipulating disulfide bond formation and protein folding in the endoplasmic reticulum. EMBO J 11, 1717-1722.
    • (1992) EMBO J , vol.11 , pp. 1717-1722
    • Braakman, I.1    Helenius, J.2    Helenius, A.3
  • 21
    • 0027174340 scopus 로고
    • Membrane glycoprotein folding, oligomerization and intracellular transport: effects of dithiothreitol in living cells
    • Tatu, U., Braakman, I. & Helenius, A. (1993). Membrane glycoprotein folding, oligomerization and intracellular transport: effects of dithiothreitol in living cells. EMBO J 12, 2151-2157.
    • (1993) EMBO J , vol.12 , pp. 2151-2157
    • Tatu, U.1    Braakman, I.2    Helenius, A.3
  • 22
    • 0027455464 scopus 로고
    • Posttranslational folding of vesicular stomatitis virus G protein in the ER: involvement of noncovalent and covalent complexes
    • de Silva, A., Braakman, I. & Helenius, A. (1993). Posttranslational folding of vesicular stomatitis virus G protein in the ER: involvement of noncovalent and covalent complexes. J Cell Biol 120, 647-655.
    • (1993) J Cell Biol , vol.120 , pp. 647-655
    • De Silva, A.1    Braakman, I.2    Helenius, A.3
  • 23
    • 0026654505 scopus 로고
    • Calcium is required for folding of newly made subunits of the asialoglycoprotein receptor within the endoplasmic reticulum
    • Lodish, H. F., Kong, N. & Wikstrom, L. (1992). Calcium is required for folding of newly made subunits of the asialoglycoprotein receptor within the endoplasmic reticulum. J Biol Chem 267, 12753-12760.
    • (1992) J Biol Chem , vol.267 , pp. 12753-12760
    • Lodish, H.F.1    Kong, N.2    Wikstrom, L.3
  • 24
    • 0025382818 scopus 로고
    • The molecular chaperone concept
    • Ellis, R. J. (1990). The molecular chaperone concept. Semin Cell Biol 1, 1-9.
    • (1990) Semin Cell Biol , vol.1 , pp. 1-9
    • Ellis, R.J.1
  • 25
    • 0028958602 scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl, F. U. & Martin, J. (1995). Molecular chaperones in cellular protein folding. Curr Opin Struct Biol 5, 92-102.
    • (1995) Curr Opin Struct Biol , vol.5 , pp. 92-102
    • Hartl, F.U.1    Martin, J.2
  • 26
    • 0034581324 scopus 로고    scopus 로고
    • Folding and association of oligomeric and multimeric proteins
    • Jaenicke, R. & Lilie, H. (2000). Folding and association of oligomeric and multimeric proteins. Adv Protein Chem 53, 329-401.
    • (2000) Adv Protein Chem , vol.53 , pp. 329-401
    • Jaenicke, R.1    Lilie, H.2
  • 27
    • 0021076098 scopus 로고
    • Immunoglobulin heavy chain binding protein
    • Haas, I. G. & Wabl, M. (1983). Immunoglobulin heavy chain binding protein. Nature 306, 387-389.
    • (1983) Nature , vol.306 , pp. 387-389
    • Haas, I.G.1    Wabl, M.2
  • 28
    • 0026059137 scopus 로고
    • Peptidebinding specificity of the molecular chaperone BiP
    • Flynn, G. C., Pohl, J., Flocco, M. T. & Rothman, J. E. (1991). Peptidebinding specificity of the molecular chaperone BiP. Nature 353, 726-730.
    • (1991) Nature , vol.353 , pp. 726-730
    • Flynn, G.C.1    Pohl, J.2    Flocco, M.T.3    Rothman, J.E.4
  • 29
    • 0027484417 scopus 로고
    • Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiP
    • Blond-Elguindi, S., Cwirla, S. E., Dower, W. J., Lipshutz, R. J., Sprang, S. R., Sambrook, J. F. & Gething, M. J. (1993). Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiP. Cell 75, 717-728.
    • (1993) Cell , vol.75 , pp. 717-728
    • Blond-Elguindi, S.1    Cwirla, S.E.2    Dower, W.J.3    Lipshutz, R.J.4    Sprang, S.R.5    Sambrook, J.F.6    Gething, M.J.7
  • 30
    • 0028103695 scopus 로고
    • Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control
    • Hammond, C., Braakman, I. & Helenius, A. (1994). Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control. Proc Natl Acad Sci USA 91, 913-917.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 913-917
    • Hammond, C.1    Braakman, I.2    Helenius, A.3
  • 31
    • 0024325535 scopus 로고
    • Interaction of heavy chain binding protein (BiP/GRP78) with adenine nucleotides
    • Kassenbrock, C. K. & Kelly, R. B. (1989). Interaction of heavy chain binding protein (BiP/GRP78) with adenine nucleotides. EMBO J 8, 1461-1467.
    • (1989) EMBO J , vol.8 , pp. 1461-1467
    • Kassenbrock, C.K.1    Kelly, R.B.2
  • 32
    • 0028832266 scopus 로고
    • Characterization of the nucleotide binding properties and ATPase activity of recombinant hamster BiP purified from bacteria
    • Wei, J. & Hendershot, L. M. (1995). Characterization of the nucleotide binding properties and ATPase activity of recombinant hamster BiP purified from bacteria. J Biol Chem 270, 26670-26676.
    • (1995) J Biol Chem , vol.270 , pp. 26670-26676
    • Wei, J.1    Hendershot, L.M.2
  • 33
    • 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
  • 34
    • 0038037820 scopus 로고    scopus 로고
    • Role of calnexin in the glycan-independent quality control of proteolipid protein
    • Swanton, E., High, S. & Woodman, P. (2003). Role of calnexin in the glycan-independent quality control of proteolipid protein. EMBO J 22, 2948-2958.
    • (2003) EMBO J , vol.22 , pp. 2948-2958
    • Swanton, E.1    High, S.2    Woodman, P.3
  • 35
    • 0033197741 scopus 로고    scopus 로고
    • Calnexin discriminates between protein conformational states and functions as a molecular chaperone in vitro
    • Ihara, Y., Cohen-Doyle, M. F., Saito, Y. & Williams, D. B. (1999). Calnexin discriminates between protein conformational states and functions as a molecular chaperone in vitro. Mol Cell 4, 331-341.
    • (1999) Mol Cell , vol.4 , pp. 331-341
    • Ihara, Y.1    Cohen-Doyle, M.F.2    Saito, Y.3    Williams, D.B.4
  • 36
    • 0023720121 scopus 로고
    • Defective co-translational formation of disulphide bonds in protein disulphide-isomerasedeficient microsomes
    • Bulleid, N. J. & Freedman, R. B. (1988). Defective co-translational formation of disulphide bonds in protein disulphide-isomerasedeficient microsomes. Nature 335, 649-651.
    • (1988) Nature , vol.335 , pp. 649-651
    • Bulleid, N.J.1    Freedman, R.B.2
  • 37
    • 0033523910 scopus 로고    scopus 로고
    • Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells
    • Molinari, M. & Helenius, A. (1999). Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells. Nature 402, 90-93.
    • (1999) Nature , vol.402 , pp. 90-93
    • Molinari, M.1    Helenius, A.2
  • 38
    • 0031035644 scopus 로고    scopus 로고
    • Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins
    • Oliver, J. D., van der Wal, F. J., Bulleid, N. J. & High, S. (1997). Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins. Science 275, 86-88.
    • (1997) Science , vol.275 , pp. 86-88
    • Oliver, J.D.1    Van Der Wal, F.J.2    Bulleid, N.J.3    High, S.4
  • 39
    • 0021668676 scopus 로고
    • [Determination of enzymatic catalysis for the cis-trans-isomerization of peptide binding in prolinecontaining peptides]
    • Fischer, G., Bang, H. & Mech, C. (1984). [Determination of enzymatic catalysis for the cis-trans-isomerization of peptide binding in prolinecontaining peptides]. Biomed Biochim Acta 43, 1101-1111.
    • (1984) Biomed Biochim Acta , vol.43 , pp. 1101-1111
    • Fischer, G.1    Bang, H.2    Mech, C.3
  • 41
    • 0023236959 scopus 로고
    • Catalysis of protein folding by prolyl isomerase
    • Lang, K., Schmid, F. X. & Fischer, G. (1987). Catalysis of protein folding by prolyl isomerase. Nature 329, 268-270.
    • (1987) Nature , vol.329 , pp. 268-270
    • Lang, K.1    Schmid, F.X.2    Fischer, G.3
  • 42
    • 0025968746 scopus 로고
    • Cyclosporin A slows collagen triple-helix formation in vivo: indirect evidence for a physiologic role of peptidyl-prolyl cistrans-isomerase
    • Steinmann, B., Bruckner, P. & Superti-Furga, A. (1991). Cyclosporin A slows collagen triple-helix formation in vivo: indirect evidence for a physiologic role of peptidyl-prolyl cistrans-isomerase. J Biol Chem 266, 1299-1303.
    • (1991) J Biol Chem , vol.266 , pp. 1299-1303
    • Steinmann, B.1    Bruckner, P.2    Superti-Furga, A.3
  • 43
    • 0025916166 scopus 로고
    • Cyclosporin A inhibits an initial step in folding of transferrin within the endoplasmic reticulum
    • Lodish, H. F. & Kong, N. (1991). Cyclosporin A inhibits an initial step in folding of transferrin within the endoplasmic reticulum. J Biol Chem 266, 14835-14838.
    • (1991) J Biol Chem , vol.266 , pp. 14835-14838
    • Lodish, H.F.1    Kong, N.2
  • 44
    • 0028127183 scopus 로고
    • Prolonged association of temperaturesensitive mutants of human Pglycoprotein with calnexin during biogenesis
    • Loo, T. W. & Clarke, D. M. (1994). Prolonged association of temperaturesensitive mutants of human Pglycoprotein with calnexin during biogenesis. J Biol Chem 269, 28683-28689.
    • (1994) J Biol Chem , vol.269 , pp. 28683-28689
    • Loo, T.W.1    Clarke, D.M.2
  • 45
    • 0028232167 scopus 로고
    • Participation of the endoplasmic reticulum chaperone calnexin (p88, IP90) in the biogenesis of the cystic fibrosis transmembrane conductance regulator
    • Pind, S., Riordan, J. R. & Williams, D. B. (1994). Participation of the endoplasmic reticulum chaperone calnexin (p88, IP90) in the biogenesis of the cystic fibrosis transmembrane conductance regulator. J Biol Chem 269, 12784-12788.
    • (1994) J Biol Chem , vol.269 , pp. 12784-12788
    • Pind, S.1    Riordan, J.R.2    Williams, D.B.3
  • 46
    • 0029099301 scopus 로고
    • P-glycoprotein. Associations between domains and between domains and molecular chaperones
    • Loo, T. W. & Clarke, D. M. (1995). P-glycoprotein. Associations between domains and between domains and molecular chaperones. J Biol Chem 270, 21839-21844.
    • (1995) J Biol Chem , vol.270 , pp. 21839-21844
    • Loo, T.W.1    Clarke, D.M.2
  • 47
    • 0027488993 scopus 로고
    • The common variant of cystic fibrosis transmembrane conductance regulator is recognized by hsp70 and degraded in a pre-Golgi nonlysosomal compartment
    • Yang, Y., Janich, S., Cohn, J. A. & Wilson, J. M. (1993). The common variant of cystic fibrosis transmembrane conductance regulator is recognized by hsp70 and degraded in a pre-Golgi nonlysosomal compartment. Proc Natl Acad Sci USA 90, 9480-9484.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 9480-9484
    • Yang, Y.1    Janich, S.2    Cohn, J.A.3    Wilson, J.M.4
  • 48
    • 0035142877 scopus 로고    scopus 로고
    • The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation
    • Meacham, G. C., Patterson, C., Zhang, W., Younger, J. M. & Cyr, D. M. (2001). The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation. Nat Cell Biol 3, 100-105.
    • (2001) Nat Cell Biol , vol.3 , pp. 100-105
    • Meacham, G.C.1    Patterson, C.2    Zhang, W.3    Younger, J.M.4    Cyr, D.M.5
  • 49
    • 0032401771 scopus 로고    scopus 로고
    • Perturbation of Hsp90 interaction with nascent CFTR prevents its maturation and accelerates its degradation by the proteasome
    • Loo, M. A., Jensen, T. J., Cui, L., Hou, Y., Chang, X. B. & Riordan, J. R. (1998). Perturbation of Hsp90 interaction with nascent CFTR prevents its maturation and accelerates its degradation by the proteasome. EMBO J 17, 6879-6887.
    • (1998) EMBO J , vol.17 , pp. 6879-6887
    • Loo, M.A.1    Jensen, T.J.2    Cui, L.3    Hou, Y.4    Chang, X.B.5    Riordan, J.R.6
  • 50
    • 0037447049 scopus 로고    scopus 로고
    • Mechanisms of protein import into mitochondria
    • Truscott, K. N., Brandner, K. & Pfanner, N. (2003). Mechanisms of protein import into mitochondria. Curr Biol 13, R326-337.
    • (2003) Curr Biol , vol.13
    • Truscott, K.N.1    Brandner, K.2    Pfanner, N.3
  • 51
    • 0036883476 scopus 로고    scopus 로고
    • Protein import into chloroplasts
    • Soll, J. (2002). Protein import into chloroplasts. Curr Opin Plant Biol 5, 529-535.
    • (2002) Curr Opin Plant Biol , vol.5 , pp. 529-535
    • Soll, J.1
  • 52
    • 0009499348 scopus 로고
    • Purification of a membrane-associated protein complex required for protein translocation across the endoplasmic reticulum
    • Walter, P. & Blobel, G. (1980). Purification of a membrane-associated protein complex required for protein translocation across the endoplasmic reticulum. Proc Natl Acad Sci USA 77, 7112-7116.
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 7112-7116
    • Walter, P.1    Blobel, G.2
  • 53
    • 0028022110 scopus 로고
    • Control of expression, glycosylation, and secretion of HIV-1 gp120 by homologous and heterologous signal sequences
    • Li, Y., Luo, L., Thomas, D. Y. & Kang, C. Y. (1994). Control of expression, glycosylation, and secretion of HIV-1 gp120 by homologous and heterologous signal sequences. Virology 204, 266-278.
    • (1994) Virology , vol.204 , pp. 266-278
    • Li, Y.1    Luo, L.2    Thomas, D.Y.3    Kang, C.Y.4
  • 54
    • 0035794608 scopus 로고    scopus 로고
    • Signal peptide cleavage of a type I membrane protein, HCMV US11, is dependent on its membrane anchor
    • Rehm, A., Stern, P., Ploegh, H. L. & Tortorella, D. (2001). Signal peptide cleavage of a type I membrane protein, HCMV US11, is dependent on its membrane anchor. EMBO J 20, 1573-1582.
    • (2001) EMBO J , vol.20 , pp. 1573-1582
    • Rehm, A.1    Stern, P.2    Ploegh, H.L.3    Tortorella, D.4
  • 55
    • 0020985425 scopus 로고
    • Analysis of cotranslational proteolytic processing of nascent chains using two-dimensional gel electrophoresis
    • Josefsson, L. G. & Randall, L. L. (1983). Analysis of cotranslational proteolytic processing of nascent chains using two-dimensional gel electrophoresis. Methods Enzymol 97, 77-85.
    • (1983) Methods Enzymol , vol.97 , pp. 77-85
    • Josefsson, L.G.1    Randall, L.L.2
  • 56
    • 0038725418 scopus 로고    scopus 로고
    • Folding of HIV-1 envelope glycoprotein involves extensive isomerization of disulfide bonds and conformation-dependent leader peptide cleavage
    • Land, A., Zonneveld, D. & Braakman, I. (2003). Folding of HIV-1 envelope glycoprotein involves extensive isomerization of disulfide bonds and conformation-dependent leader peptide cleavage. FASEB J 17, 1058-1067.
    • (2003) FASEB J , vol.17 , pp. 1058-1067
    • Land, A.1    Zonneveld, D.2    Braakman, I.3
  • 57
    • 0029792920 scopus 로고    scopus 로고
    • Effects of inefficient cleavage of the signal sequence of HIV-1 gp 120 on its association with calnexin, folding, and intracellular transport
    • Li, Y., Bergeron, J. J., Luo, L., Ou, W. J., Thomas, D. Y. & Kang, C. Y. (1996). Effects of inefficient cleavage of the signal sequence of HIV-1 gp 120 on its association with calnexin, folding, and intracellular transport. Proc Natl Acad Sci USA 93, 9606-9611.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 9606-9611
    • Li, Y.1    Bergeron, J.J.2    Luo, L.3    Ou, W.J.4    Thomas, D.Y.5    Kang, C.Y.6
  • 58
    • 0025367812 scopus 로고
    • Sequence differences between glycosylated and non-glycosylated Asn-X-Thr/Ser acceptor sites: implications for protein engineering
    • Gavel, Y. & von Heijne, G. (1990). Sequence differences between glycosylated and non-glycosylated Asn-X-Thr/Ser acceptor sites: implications for protein engineering. Protein Eng 3, 433-442.
    • (1990) Protein Eng , vol.3 , pp. 433-442
    • Gavel, Y.1    Von Heijne, G.2
  • 59
    • 0026500202 scopus 로고
    • Recognition of the oligosaccharide and protein moieties of glycoproteins by the UDPGlc: glycoprotein glucosyltransferase
    • Sousa, M. C., Ferrero-Garcia, M. A. & Parodi, A. J. (1992). Recognition of the oligosaccharide and protein moieties of glycoproteins by the UDPGlc: glycoprotein glucosyltransferase. Biochemistry 31, 97-105.
    • (1992) Biochemistry , vol.31 , pp. 97-105
    • Sousa, M.C.1    Ferrero-Garcia, M.A.2    Parodi, A.J.3
  • 60
    • 0026799435 scopus 로고
    • Purification to apparent homogeneity and partial characterization of rat liver UDPglucose: glycoprotein glucosyltransferase
    • Trombetta, S. E. & Parodi, A. J. (1992). Purification to apparent homogeneity and partial characterization of rat liver UDPglucose: glycoprotein glucosyltransferase. J Biol Chem 267, 9236-9240.
    • (1992) J Biol Chem , vol.267 , pp. 9236-9240
    • Trombetta, S.E.1    Parodi, A.J.2
  • 61
    • 0034031279 scopus 로고    scopus 로고
    • Recognition of local glycoprotein misfolding by the ER folding sensor UDP-glucose:glycoprotein glucosyltransferase
    • Ritter, C. & Helenius, A. (2000). Recognition of local glycoprotein misfolding by the ER folding sensor UDP-glucose:glycoprotein glucosyltransferase. Nat Struct Biol 7, 278-280.
    • (2000) Nat Struct Biol , vol.7 , pp. 278-280
    • Ritter, C.1    Helenius, A.2
  • 62
    • 0026698060 scopus 로고
    • Oxidized redox state of glutathione in the endoplasmic reticulum
    • Hwang, C., Sinskey, A. J. & Lodish, H. F. (1992). Oxidized redox state of glutathione in the endoplasmic reticulum. Science 257, 1496-1502.
    • (1992) Science , vol.257 , pp. 1496-1502
    • Hwang, C.1    Sinskey, A.J.2    Lodish, H.F.3
  • 63
    • 0034711439 scopus 로고    scopus 로고
    • Biochemical basis of oxidative protein folding in the endoplasmic reticulum
    • Tu, B. P., Ho-Schleyer, S. C., Travers, K. J. & Weissman, J. S. (2000). Biochemical basis of oxidative protein folding in the endoplasmic reticulum. Science 290, 1571-4.
    • (2000) Science , vol.290 , pp. 1571-1574
    • Tu, B.P.1    Ho-Schleyer, S.C.2    Travers, K.J.3    Weissman, J.S.4
  • 64
    • 0031609760 scopus 로고    scopus 로고
    • The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum
    • Frand, A. R. & Kaiser, C. A. (1998). The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum. Mol Cell 1, 161-170.
    • (1998) Mol Cell , vol.1 , pp. 161-170
    • Frand, A.R.1    Kaiser, C.A.2
  • 65
    • 0031610364 scopus 로고    scopus 로고
    • Ero1p: a novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulum
    • Pollard, M. G., Travers, K. J. & Weissman, J. S. (1998). Ero1p: a novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulum. Mol Cell 1, 171-182.
    • (1998) Mol Cell , vol.1 , pp. 171-182
    • Pollard, M.G.1    Travers, K.J.2    Weissman, J.S.3
  • 66
    • 0034681340 scopus 로고    scopus 로고
    • ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum
    • Cabibbo, A., Pagani, M., Fabbri, M., Rocchi, M., Farmery, M. R., Bulleid, N. J. & Sitia, R. (2000). ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum. J Biol Chem 275, 4827-4833.
    • (2000) J Biol Chem , vol.275 , pp. 4827-4833
    • Cabibbo, A.1    Pagani, M.2    Fabbri, M.3    Rocchi, M.4    Farmery, M.R.5    Bulleid, N.J.6    Sitia, R.7
  • 67
    • 0034604675 scopus 로고    scopus 로고
    • Endoplasmic reticulum oxidoreductin 1-lbeta (ERO1-Lbeta), a human gene induced in the course of the unfolded protein response
    • Pagani, M., Fabbri, M., Benedetti, C., Fassio, A., Pilati, S., Bulleid, N. J., Cabibbo, A. & Sitia, R. (2000). Endoplasmic reticulum oxidoreductin 1-lbeta (ERO1-Lbeta), a human gene induced in the course of the unfolded protein response. J Biol Chem 275, 23685-23692.
    • (2000) J Biol Chem , vol.275 , pp. 23685-23692
    • Pagani, M.1    Fabbri, M.2    Benedetti, C.3    Fassio, A.4    Pilati, S.5    Bulleid, N.J.6    Cabibbo, A.7    Sitia, R.8
  • 68
    • 0033213605 scopus 로고    scopus 로고
    • Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulum
    • Frand, A. R. & Kaiser, C. A. (1999). Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulum. Mol Cell 4, 469-477.
    • (1999) Mol Cell , vol.4 , pp. 469-477
    • Frand, A.R.1    Kaiser, C.A.2
  • 69
    • 0034790475 scopus 로고    scopus 로고
    • A flavoprotein oxidase defines a new endoplasmic reticulum pathway for biosynthetic disulphide bond formation
    • Sevier, C. S., Cuozzo, J. W., Vala, A., Aslund, F. & Kaiser, C. A. (2001). A flavoprotein oxidase defines a new endoplasmic reticulum pathway for biosynthetic disulphide bond formation. Nat Cell Biol 3, 874-882.
    • (2001) Nat Cell Biol , vol.3 , pp. 874-882
    • Sevier, C.S.1    Cuozzo, J.W.2    Vala, A.3    Aslund, F.4    Kaiser, C.A.5
  • 70
    • 0842266604 scopus 로고    scopus 로고
    • Oxidative protein folding in eukaryotes: mechanisms and consequences
    • Tu, B. P. & Weissman, J. S. (2004). Oxidative protein folding in eukaryotes: mechanisms and consequences. J Cell Biol 164, 341-346.
    • (2004) J Cell Biol , vol.164 , pp. 341-346
    • Tu, B.P.1    Weissman, J.S.2
  • 71
    • 0017815610 scopus 로고
    • Experimental studies of protein folding and unfolding
    • Creighton, T. E. (1978). Experimental studies of protein folding and unfolding. Prog Biophys Mol Biol 33, 231-297.
    • (1978) Prog Biophys Mol Biol , vol.33 , pp. 231-297
    • Creighton, T.E.1
  • 72
    • 0001922433 scopus 로고
    • Disulphide bonds between cysteine residues. In Protein structure
    • Creighton, T. E., ed., IRL Press, Oxford
    • Creighton, T. E. (1990). Disulphide bonds between cysteine residues. In Protein structure. A practical approach. (Creighton, T. E., ed.), pp. 155-168. IRL Press, Oxford.
    • (1990) A practical approach , pp. 155-168
    • Creighton, T.E.1
  • 73
    • 0030700576 scopus 로고    scopus 로고
    • Endoplasmic reticulum degradation: reverse protein flow of no return
    • Sommer, T. & Wolf, D. H. (1997). Endoplasmic reticulum degradation: reverse protein flow of no return. FASEB J 11, 1227-1233.
    • (1997) FASEB J , vol.11 , pp. 1227-1233
    • Sommer, T.1    Wolf, D.H.2
  • 76
    • 0037470515 scopus 로고    scopus 로고
    • EDEM as an acceptor of terminally misfolded glycoproteins released from calnexin
    • Oda, Y., Hosokawa, N., Wada, I. & Nagata, K. (2003). EDEM as an acceptor of terminally misfolded glycoproteins released from calnexin. Science 299, 1394-1397.
    • (2003) Science , vol.299 , pp. 1394-1397
    • Oda, Y.1    Hosokawa, N.2    Wada, I.3    Nagata, K.4
  • 77
    • 0037470410 scopus 로고    scopus 로고
    • Role of EDEM in the release of misfolded glycoproteins from the calnexin cycle
    • Molinari, M., Calanca, V., Galli, C., Lucca, P. & Paganetti, P. (2003). Role of EDEM in the release of misfolded glycoproteins from the calnexin cycle. Science 299, 1397-1400.
    • (2003) Science , vol.299 , pp. 1397-1400
    • Molinari, M.1    Calanca, V.2    Galli, C.3    Lucca, P.4    Paganetti, P.5
  • 79
    • 0025292252 scopus 로고
    • Assignment of intrachain disulfide bonds and characterization of potential glycosylation sites of the type 1 recombinant human immunodeficiency virus envelope glycoprotein (gp120) expressed in Chinese hamster ovary cells
    • Leonard, C. K., Spellman, M. W., Riddle, L., Harris, R. J., Thomas, J. N. & Gregory, T. J. (1990). Assignment of intrachain disulfide bonds and characterization of potential glycosylation sites of the type 1 recombinant human immunodeficiency virus envelope glycoprotein (gp120) expressed in Chinese hamster ovary cells. J Biol Chem 265, 10373-10382.
    • (1990) J Biol Chem , vol.265 , pp. 10373-10382
    • Leonard, C.K.1    Spellman, M.W.2    Riddle, L.3    Harris, R.J.4    Thomas, J.N.5    Gregory, T.J.6
  • 80
    • 0033769704 scopus 로고    scopus 로고
    • The effect of Golgi depletion on exocytic transport
    • Pelletier, L., Jokitalo, E. and Warren, G. (2000). The effect of Golgi depletion on exocytic transport. Nature Cell Biology 2, 840-846.
    • (2000) Nature Cell Biology , vol.2 , pp. 840-846
    • Pelletier, L.1    Jokitalo, E.2    Warren, G.3
  • 81
    • 0020181690 scopus 로고
    • Early stages in the yeast secretory pathway are required for transport of carboxypeptidase Y to the vacuole
    • Stevens, T., Esmon, B. & Schekman, R. (1982). Early stages in the yeast secretory pathway are required for transport of carboxypeptidase Y to the vacuole. Cell 30, 439-448.
    • (1982) Cell , vol.30 , pp. 439-448
    • Stevens, T.1    Esmon, B.2    Schekman, R.3
  • 82
    • 0021111582 scopus 로고
    • Purification and characterization of calsequestrin from canine cardiac sarcoplasmic reticulum and identification of the 53,000 dalton glycoprotein
    • Campbell, K. P., MacLennan, D. H., Jorgensen, A. O. & Mintzer, M. C. (1983). Purification and characterization of calsequestrin from canine cardiac sarcoplasmic reticulum and identification of the 53,000 dalton glycoprotein. J Biol Chem 258, 1197-1204.
    • (1983) J Biol Chem , vol.258 , pp. 1197-1204
    • Campbell, K.P.1    MacLennan, D.H.2    Jorgensen, A.O.3    Mintzer, M.C.4
  • 83
    • 0025313861 scopus 로고
    • Perturbation of cellular calcium blocks exit of secretory proteins from the rough endoplasmic reticulum
    • Lodish, H. F. & Kong, N. (1990). Perturbation of cellular calcium blocks exit of secretory proteins from the rough endoplasmic reticulum. J Biol Chem 265, 10893-10899.
    • (1990) J Biol Chem , vol.265 , pp. 10893-10899
    • Lodish, H.F.1    Kong, N.2
  • 84
    • 0021668435 scopus 로고
    • Inhibition of proteolytic cleavage of the hemagglutinin of influenza virus by the calcium-specific ionophore A23187
    • Klenk, H. D., Garten, W. & Rott, R. (1984). Inhibition of proteolytic cleavage of the hemagglutinin of influenza virus by the calcium-specific ionophore A23187. EMBO J 3, 2911-2915.
    • (1984) EMBO J , vol.3 , pp. 2911-2915
    • Klenk, H.D.1    Garten, W.2    Rott, R.3
  • 85
    • 0025332577 scopus 로고
    • Thapsigargin, a tumor promoter, discharges intracellular Ca2+ stores by specific inhibition of the endoplasmic reticulum Ca2(+)-ATPase
    • Thastrup, O., Cullen, P. J., Drobak, B. K., Hanley, M. R. & Dawson, A. P. (1990). Thapsigargin, a tumor promoter, discharges intracellular Ca2+ stores by specific inhibition of the endoplasmic reticulum Ca2(+)-ATPase. Proc Natl Acad Sci USA 87, 2466-2470.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 2466-2470
    • Thastrup, O.1    Cullen, P.J.2    Drobak, B.K.3    Hanley, M.R.4    Dawson, A.P.5
  • 86
    • 0026050850 scopus 로고
    • Thapsigargin inhibits the sarcoplasmic or endoplasmic reticulum Ca-ATPase family of calcium pumps
    • Lytton, J., Westlin, M. & Hanley, M. R. (1991). Thapsigargin inhibits the sarcoplasmic or endoplasmic reticulum Ca-ATPase family of calcium pumps. J Biol Chem 266, 17067-17071.
    • (1991) J Biol Chem , vol.266 , pp. 17067-17071
    • Lytton, J.1    Westlin, M.2    Hanley, M.R.3
  • 87
    • 0026508087 scopus 로고
    • Role of ATP and disulphide bonds during protein folding in the endoplasmic reticulum
    • Braakman, I., Helenius, J. & Helenius, A. (1992). Role of ATP and disulphide bonds during protein folding in the endoplasmic reticulum. Nature 356, 260-262.
    • (1992) Nature , vol.356 , pp. 260-262
    • Braakman, I.1    Helenius, J.2    Helenius, A.3
  • 88
    • 0018653540 scopus 로고
    • Interference with glycosylation of glycoproteins. Inhibition of formation of lipid-linked oligosaccharides in vivo
    • Datema, R. & Schwarz, R. T. (1979). Interference with glycosylation of glycoproteins. Inhibition of formation of lipid-linked oligosaccharides in vivo. Biochem J 184, 113-123.
    • (1979) Biochem J , vol.184 , pp. 113-123
    • Datema, R.1    Schwarz, R.T.2
  • 89
    • 0025119643 scopus 로고
    • Protein dissociation from GRP78 and secretion are blocked by depletion of cellular ATP levels
    • Dorner, A. J., Wasley, L. C. & Kaufman, R. J. (1990). Protein dissociation from GRP78 and secretion are blocked by depletion of cellular ATP levels. Proc Natl Acad Sci USA 87, 7429-7432.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 7429-7432
    • Dorner, A.J.1    Wasley, L.C.2    Kaufman, R.J.3
  • 90
    • 0016862381 scopus 로고
    • Analytical information obtainable by evaluation of the time course of firefly bioluminescence in the assay of ATP
    • Lundin, A. & Thore, A. (1975). Analytical information obtainable by evaluation of the time course of firefly bioluminescence in the assay of ATP. Anal Biochem 66, 47-63.
    • (1975) Anal Biochem , vol.66 , pp. 47-63
    • Lundin, A.1    Thore, A.2
  • 91
    • 0025121097 scopus 로고
    • ATP synthase complex from bovine heart mitochondria. Subunit arrangement as revealed by nearest neighbor analysis and susceptibility to trypsin
    • Joshi, S. & Burrows, R. (1990). ATP synthase complex from bovine heart mitochondria. Subunit arrangement as revealed by nearest neighbor analysis and susceptibility to trypsin. J Biol Chem 265, 14518-14525.
    • (1990) J Biol Chem , vol.265 , pp. 14518-14525
    • Joshi, S.1    Burrows, R.2
  • 92
    • 0025955452 scopus 로고
    • Production of multimeric forms of CD4 through a sugar-based cross-linking strategy
    • Chen, L. L., Rosa, J. J., Turner, S. & Pepinsky, R. B. (1991). Production of multimeric forms of CD4 through a sugar-based cross-linking strategy. J Biol Chem 266, 18237-18243.
    • (1991) J Biol Chem , vol.266 , pp. 18237-18243
    • Chen, L.L.1    Rosa, J.J.2    Turner, S.3    Pepinsky, R.B.4
  • 93
    • 0032807338 scopus 로고    scopus 로고
    • ERp57 functions as a subunit of specific complexes formed with the ER lectins calreticulin and calnexin
    • Oliver, J. D., Roderick, H. L., Llewellyn, D. H. & High, S. (1999). ERp57 functions as a subunit of specific complexes formed with the ER lectins calreticulin and calnexin. Mol Biol Cell 10, 2573-2582.
    • (1999) Mol Biol Cell , vol.10 , pp. 2573-2582
    • Oliver, J.D.1    Roderick, H.L.2    Llewellyn, D.H.3    High, S.4
  • 94
    • 0015041650 scopus 로고
    • Tunicamycin, a new antibiotic. I. Isolation and characterization of tunicamycin
    • Tokyo
    • Takatsuki, A., Arima, K. & Tamura, G. (1971). Tunicamycin, a new antibiotic. I. Isolation and characterization of tunicamycin. J Antibiot (Tokyo) 24, 215-223.
    • (1971) J Antibiot , vol.24 , pp. 215-223
    • Takatsuki, A.1    Arima, K.2    Tamura, G.3
  • 95
    • 0035370949 scopus 로고    scopus 로고
    • Intracellular signaling from the endoplasmic reticulum to the nucleus: the unfolded protein response in yeast and mammals
    • Patil, C. & Walter, P. (2001). Intracellular signaling from the endoplasmic reticulum to the nucleus: the unfolded protein response in yeast and mammals. Curr Opin Cell Biol 13, 349-355.
    • (2001) Curr Opin Cell Biol , vol.13 , pp. 349-355
    • Patil, C.1    Walter, P.2
  • 96
    • 0028241858 scopus 로고
    • Mapping of cystic fibrosis transmembrane conductance regulator membrane topology by glycosylation site insertion
    • Chang, X. B., Hou, Y. X., Jensen, T. J. & Riordan, J. R. (1994). Mapping of cystic fibrosis transmembrane conductance regulator membrane topology by glycosylation site insertion. J Biol Chem 269, 18572-18575.
    • (1994) J Biol Chem , vol.269 , pp. 18572-18575
    • Chang, X.B.1    Hou, Y.X.2    Jensen, T.J.3    Riordan, J.R.4
  • 97
    • 0025630758 scopus 로고
    • The stress response in Chinese hamster ovary cells. Regulation of ERp72 and protein disulfide isomerase expression and secretion
    • Dorner, A. J., Wasley, L. C., Raney, P., Haugejorden, S., Green, M. & Kaufman, R. J. (1990). The stress response in Chinese hamster ovary cells. Regulation of ERp72 and protein disulfide isomerase expression and secretion. J Biol Chem 265, 22029-22034.
    • (1990) J Biol Chem , vol.265 , pp. 22029-22034
    • Dorner, A.J.1    Wasley, L.C.2    Raney, P.3    Haugejorden, S.4    Green, M.5    Kaufman, R.J.6
  • 98
    • 0030804446 scopus 로고    scopus 로고
    • Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL
    • Rye, H. S., Burston, S. G., Fenton, W. A., Beechem, J. M., Xu, Z., Sigler, P. B. & Horwich, A. L. (1997). Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL. Nature 388, 792-798.
    • (1997) Nature , vol.388 , pp. 792-798
    • Rye, H.S.1    Burston, S.G.2    Fenton, W.A.3    Beechem, J.M.4    Xu, Z.5    Sigler, P.B.6    Horwich, A.L.7
  • 99
    • 0029890917 scopus 로고    scopus 로고
    • Inhibition of immunoglobulin folding and secretion by dominant negative BiP ATPase mutants
    • Hendershot, L., Wei, J., Gaut, J., Melnick, J., Aviel, S. & Argon, Y. (1996). Inhibition of immunoglobulin folding and secretion by dominant negative BiP ATPase mutants. Proc Natl Acad Sci USA 93, 5269-5274.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 5269-5274
    • Hendershot, L.1    Wei, J.2    Gaut, J.3    Melnick, J.4    Aviel, S.5    Argon, Y.6
  • 100
    • 0025286478 scopus 로고
    • Lectin-resistant CHO cells: selection of seven new mutants resistant to ricin
    • Stanley, P., Sallustio, S., Krag, S. S. & Dunn, B. (1990). Lectin-resistant CHO cells: selection of seven new mutants resistant to ricin. Somat Cell Mol Genet 16, 211-223.
    • (1990) Somat Cell Mol Genet , vol.16 , pp. 211-223
    • Stanley, P.1    Sallustio, S.2    Krag, S.S.3    Dunn, B.4
  • 101
    • 0026317971 scopus 로고
    • A novel glycosylation phenotype expressed by Lec23, a Chinese hamster ovary mutant deficient in alpha-glucosidase I
    • Ray, M. K., Yang, J., Sundaram, S. & Stanley, P. (1991). A novel glycosylation phenotype expressed by Lec23, a Chinese hamster ovary mutant deficient in alpha-glucosidase I. J Biol Chem 266, 22818-22825.
    • (1991) J Biol Chem , vol.266 , pp. 22818-22825
    • Ray, M.K.1    Yang, J.2    Sundaram, S.3    Stanley, P.4
  • 102
    • 0020385681 scopus 로고
    • A lectin-resistant mouse lymphoma cell line is deficient in glucosidase II, a glycoproteinprocessing enzyme
    • Reitman, M. L., Trowbridge, I. S. & Kornfeld, S. (1982). A lectin-resistant mouse lymphoma cell line is deficient in glucosidase II, a glycoproteinprocessing enzyme. J Biol Chem 257, 10357-10363.
    • (1982) J Biol Chem , vol.257 , pp. 10357-10363
    • Reitman, M.L.1    Trowbridge, I.S.2    Kornfeld, S.3
  • 103
    • 0021975925 scopus 로고
    • Natural killing target antigens as inducers of interferon: studies with an immunoselected, natural killingresistant human T lymphoblastoid cell line
    • Howell, D. N., Andreotti, P. E., Dawson, J. R. & Cresswell, P. (1985). Natural killing target antigens as inducers of interferon: studies with an immunoselected, natural killingresistant human T lymphoblastoid cell line. J Immunol 134, 971-976.
    • (1985) J Immunol , vol.134 , pp. 971-976
    • Howell, D.N.1    Andreotti, P.E.2    Dawson, J.R.3    Cresswell, P.4
  • 104
    • 0032545933 scopus 로고    scopus 로고
    • Potent and specific genetic interference by doublestranded RNA in Caenorhabditis elegans
    • Fire, A., Xu, S., Montgomery, M. K., Kostas, S. A., Driver, S. E. & Mello, C. C. (1998). Potent and specific genetic interference by doublestranded RNA in Caenorhabditis elegans. Nature 391, 806-811.
    • (1998) Nature , vol.391 , pp. 806-811
    • Fire, A.1    Xu, S.2    Montgomery, M.K.3    Kostas, S.A.4    Driver, S.E.5    Mello, C.C.6
  • 105
    • 0027295871 scopus 로고
    • Association of folding intermediates of glycoproteins with calnexin during protein maturation
    • Ou, W. J., Cameron, P. H., Thomas, D. Y. & Bergeron, J. J. (1993). Association of folding intermediates of glycoproteins with calnexin during protein maturation. Nature 364, 771-776.
    • (1993) Nature , vol.364 , pp. 771-776
    • Ou, W.J.1    Cameron, P.H.2    Thomas, D.Y.3    Bergeron, J.J.4
  • 106
    • 0026409298 scopus 로고
    • Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form
    • Schagger, H. & von Jagow, G. (1991). Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form. Anal Biochem 199, 223-231.
    • (1991) Anal Biochem , vol.199 , pp. 223-231
    • Schagger, H.1    Von Jagow, G.2


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