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Volumn 13, Issue 1, 2004, Pages 125-135

Contrasting Functions of Calreticulin and Calnexin in Glycoprotein Folding and ER Quality Control

Author keywords

[No Author keywords available]

Indexed keywords

CALNEXIN; CALRETICULIN; GLYCOPROTEIN; VIRUS HEMAGGLUTININ; VIRUS PROTEIN;

EID: 1342334746     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1097-2765(03)00494-5     Document Type: Article
Times cited : (191)

References (60)
  • 1
  • 2
    • 0026604334 scopus 로고
    • Manipulating disulfide bond formation and protein folding in the endoplasmic reticulum
    • a
    • Braakman I., Helenius J., Helenius A. Manipulating disulfide bond formation and protein folding in the endoplasmic reticulum. EMBO J. 11:1992;1717-1722. a.
    • (1992) EMBO J. , vol.11 , pp. 1717-1722
    • Braakman, I.1    Helenius, J.2    Helenius, A.3
  • 3
    • 0026508087 scopus 로고
    • Role of ATP and disulphide bonds during protein folding in the endoplasmic reticulum
    • b
    • Braakman I., Helenius J., Helenius A. Role of ATP and disulphide bonds during protein folding in the endoplasmic reticulum. Nature. 356:1992;260-262. b.
    • (1992) Nature , vol.356 , pp. 260-262
    • Braakman, I.1    Helenius, J.2    Helenius, A.3
  • 5
    • 0029558245 scopus 로고
    • A soluble domain of the membrane-anchoring chain of influenza virus hemagglutinin (HA2) folds in Escherichia coli into the low-pH-induced conformation
    • Chen J., Wharton S.A., Weissenhorn W., Calder L.J., Hughson F.M., Skehel J.J., Wiley D.C. A soluble domain of the membrane-anchoring chain of influenza virus hemagglutinin (HA2) folds in Escherichia coli into the low-pH-induced conformation. Proc. Natl. Acad. Sci. USA. 92:1995;12205-12209.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 12205-12209
    • Chen, J.1    Wharton, S.A.2    Weissenhorn, W.3    Calder, L.J.4    Hughson, F.M.5    Skehel, J.J.6    Wiley, D.C.7
  • 6
    • 0024294338 scopus 로고
    • Folding, trimerization, and transport are sequential events in the biogenesis of influenza virus hemagglutinin
    • Copeland C.S., Zimmer K.P., Wagner K.R., Healey G.A., Mellman I., Helenius A. Folding, trimerization, and transport are sequential events in the biogenesis of influenza virus hemagglutinin. Cell. 53:1988;197-209.
    • (1988) Cell , vol.53 , pp. 197-209
    • Copeland, C.S.1    Zimmer, K.P.2    Wagner, K.R.3    Healey, G.A.4    Mellman, I.5    Helenius, A.6
  • 7
    • 0037245727 scopus 로고    scopus 로고
    • N-linked glycans direct the cotranslational folding pathway of influenza hemagglutinin
    • Daniels R., Kurowski B., Johnson A.E., Hebert D.N. N-linked glycans direct the cotranslational folding pathway of influenza hemagglutinin. Mol. Cell. 11:2003;79-90.
    • (2003) Mol. Cell , vol.11 , pp. 79-90
    • Daniels, R.1    Kurowski, B.2    Johnson, A.E.3    Hebert, D.N.4
  • 8
    • 0034724690 scopus 로고    scopus 로고
    • Functional relationship between calreticulin, calnexin, and the endoplasmic reticulum luminal domain of calnexin
    • Danilczyk U.G., Cohen-Doyle M.F., Williams D.B. Functional relationship between calreticulin, calnexin, and the endoplasmic reticulum luminal domain of calnexin. J. Biol. Chem. 275:2000;13089-13097.
    • (2000) J. Biol. Chem. , vol.275 , pp. 13089-13097
    • Danilczyk, U.G.1    Cohen-Doyle, M.F.2    Williams, D.B.3
  • 9
    • 0025005759 scopus 로고
    • Quality control in the endoplasmic reticulum: Folding and misfolding of vesicular stomatitis virus G protein in cells and in vitro
    • de Silva A.M., Balch W.E., Helenius A. Quality control in the endoplasmic reticulum. folding and misfolding of vesicular stomatitis virus G protein in cells and in vitro J. Cell Biol. 111:1990;857-866.
    • (1990) J. Cell Biol. , vol.111 , pp. 857-866
    • De Silva, A.M.1    Balch, W.E.2    Helenius, A.3
  • 10
    • 0023788652 scopus 로고
    • Differential effects of mutations in three domains on folding, quaternary structure, and intracellular transport of vesicular stomatitis virus G protein
    • Doms R.W., Ruusala A., Machamer C., Helenius J., Helenius A., Rose J.K. Differential effects of mutations in three domains on folding, quaternary structure, and intracellular transport of vesicular stomatitis virus G protein. J. Cell Biol. 107:1988;89-99.
    • (1988) J. Cell Biol. , vol.107 , pp. 89-99
    • Doms, R.W.1    Ruusala, A.2    MacHamer, C.3    Helenius, J.4    Helenius, A.5    Rose, J.K.6
  • 11
    • 0023159808 scopus 로고
    • Inhibitors of the biosynthesis and processing of N-linked oligosaccharide chains
    • Elbein A.D. Inhibitors of the biosynthesis and processing of N-linked oligosaccharide chains. Annu. Rev. Biochem. 56:1987;497-534.
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 497-534
    • Elbein, A.D.1
  • 12
    • 0033521072 scopus 로고    scopus 로고
    • Setting the standards: Quality control in the secretory pathway
    • Ellgaard L., Molinari M., Helenius A. Setting the standards. quality control in the secretory pathway Science. 286:1999;1882-1888.
    • (1999) Science , vol.286 , pp. 1882-1888
    • Ellgaard, L.1    Molinari, M.2    Helenius, A.3
  • 13
    • 0029819131 scopus 로고    scopus 로고
    • N-butyldeoxynojirimycin-mediated inhibition of human immunodeficiency virus entry correlates with changes in antibody recognition of the V1/V2 region of gp120
    • Fischer P.B., Karlsson G.B., Butters T.D., Dwek R.A., Platt F.M. N-butyldeoxynojirimycin-mediated inhibition of human immunodeficiency virus entry correlates with changes in antibody recognition of the V1/V2 region of gp120. J. Virol. 70:1996;7143-7152.
    • (1996) J. Virol. , vol.70 , pp. 7143-7152
    • Fischer, P.B.1    Karlsson, G.B.2    Butters, T.D.3    Dwek, R.A.4    Platt, F.M.5
  • 14
    • 0036169941 scopus 로고    scopus 로고
    • Assembly and antigen-presenting function of MHC class I molecules in cells lacking the ER chaperone calreticulin
    • Gao B., Adhikari R., Howarth M., Nakamura K., Gold M.C., Hill A.B., Knee R., Michalak M., Elliott T. Assembly and antigen-presenting function of MHC class I molecules in cells lacking the ER chaperone calreticulin. Immunity. 16:2002;99-109.
    • (2002) Immunity , vol.16 , pp. 99-109
    • Gao, B.1    Adhikari, R.2    Howarth, M.3    Nakamura, K.4    Gold, M.C.5    Hill, A.B.6    Knee, R.7    Michalak, M.8    Elliott, T.9
  • 16
    • 0022552149 scopus 로고
    • Expression of wild-type and mutant forms of influenza hemagglutinin: The role of folding in intracellular transport
    • Gething M.-J., McCammon K., Sambrook J. Expression of wild-type and mutant forms of influenza hemagglutinin. the role of folding in intracellular transport Cell. 46:1986;939-950.
    • (1986) Cell , vol.46 , pp. 939-950
    • Gething, M.-J.1    McCammon, K.2    Sambrook, J.3
  • 17
  • 18
    • 0030912157 scopus 로고    scopus 로고
    • Aberrant retention of tyrosinase in the endoplasmic reticulum mediates accelerated degradation of the enzyme and contributes to the dedifferentiated phenotype of amelanotic melanoma cells
    • Halaban R., Cheng E., Zhang Y., Moellmann G., Hanlon D., Michalak M., Setaluri V., Hebert D.N. Aberrant retention of tyrosinase in the endoplasmic reticulum mediates accelerated degradation of the enzyme and contributes to the dedifferentiated phenotype of amelanotic melanoma cells. Proc. Natl. Acad. Sci. USA. 94:1997;6210-6215.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 6210-6215
    • Halaban, R.1    Cheng, E.2    Zhang, Y.3    Moellmann, G.4    Hanlon, D.5    Michalak, M.6    Setaluri, V.7    Hebert, D.N.8
  • 19
    • 0027141852 scopus 로고
    • A chaperone with a sweet tooth
    • Hammond C., Helenius A. A chaperone with a sweet tooth. Curr. Biol. 3:1993;884-886.
    • (1993) Curr. Biol. , vol.3 , pp. 884-886
    • Hammond, C.1    Helenius, A.2
  • 20
    • 0028076031 scopus 로고
    • Folding of VSV G protein: Sequential interaction with BiP and calnexin
    • Hammond C., Helenius A. Folding of VSV G protein. sequential interaction with BiP and calnexin Science. 266:1994;456-458.
    • (1994) Science , vol.266 , pp. 456-458
    • Hammond, C.1    Helenius, A.2
  • 21
    • 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. Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control. Proc. Natl. Acad. Sci. USA. 91:1994;913-917.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 913-917
    • Hammond, C.1    Braakman, I.2    Helenius, A.3
  • 22
    • 0029934119 scopus 로고    scopus 로고
    • Calnexin and calreticulin promote folding, delay oligomerization and suppress degradation of influenza hemagglutinin in microsomes
    • Hebert D.N., Foellmer B., Helenius A. Calnexin and calreticulin promote folding, delay oligomerization and suppress degradation of influenza hemagglutinin in microsomes. EMBO J. 15:1996;2961-2968.
    • (1996) EMBO J. , vol.15 , pp. 2961-2968
    • Hebert, D.N.1    Foellmer, B.2    Helenius, A.3
  • 23
    • 0030667061 scopus 로고    scopus 로고
    • The number and location of glycans on influenza hemagglutinin determine folding and association with calnexin and calreticulin
    • Hebert D.N., Zhang J.X., Chen W., Foellmer B., Helenius A. The number and location of glycans on influenza hemagglutinin determine folding and association with calnexin and calreticulin. J. Cell Biol. 139:1997;613-623.
    • (1997) J. Cell Biol. , vol.139 , pp. 613-623
    • Hebert, D.N.1    Zhang, J.X.2    Chen, W.3    Foellmer, B.4    Helenius, A.5
  • 24
    • 0028198111 scopus 로고
    • How N-linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum
    • Helenius A. How N-linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum. Mol. Biol. Cell. 5:1994;253-265.
    • (1994) Mol. Biol. Cell , vol.5 , pp. 253-265
    • Helenius, A.1
  • 25
    • 0027315845 scopus 로고
    • Characterization of endomannosidase inhibitors and evaluation of their effect on N-linked oligosaccharide processing during glycoprotein biosynthesis
    • Hiraizumi S., Spohr U., Spiro R.G. Characterization of endomannosidase inhibitors and evaluation of their effect on N-linked oligosaccharide processing during glycoprotein biosynthesis. J. Biol. Chem. 268:1993;9927-9935.
    • (1993) J. Biol. Chem. , vol.268 , pp. 9927-9935
    • Hiraizumi, S.1    Spohr, U.2    Spiro, R.G.3
  • 26
    • 0021975925 scopus 로고
    • Natural killing target antigens as inducers of interferon: Studies with an immunoselected, natural killing-resistant human T lymphoblastoid cell line
    • Howell D.N., Andreotti P.E., Dawson J.R., Cresswell P. Natural killing target antigens as inducers of interferon. studies with an immunoselected, natural killing-resistant human T lymphoblastoid cell line J. Immunol. 134:1985;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
  • 27
    • 0032479290 scopus 로고    scopus 로고
    • Inhibition of glucose trimming with castanospermine reduces calnexin association and promotes proteasome degradation of the alpha-subunit of the nicotinic acetylcholine receptor
    • Keller S.H., Lindstrom J., Taylor P. Inhibition of glucose trimming with castanospermine reduces calnexin association and promotes proteasome degradation of the alpha-subunit of the nicotinic acetylcholine receptor. J. Biol. Chem. 273:1998;17064-17072.
    • (1998) J. Biol. Chem. , vol.273 , pp. 17064-17072
    • Keller, S.H.1    Lindstrom, J.2    Taylor, P.3
  • 28
    • 0033569993 scopus 로고    scopus 로고
    • BiP-binding sequences in HIV gp160. Implications for the binding specificity of BiP
    • Knarr G., Modrow S., Todd A., Gething M.J., Buchner J. BiP-binding sequences in HIV gp160. Implications for the binding specificity of BiP. J. Biol. Chem. 274:1999;29850-29857.
    • (1999) J. Biol. Chem. , vol.274 , pp. 29850-29857
    • Knarr, G.1    Modrow, S.2    Todd, A.3    Gething, M.J.4    Buchner, J.5
  • 30
    • 0026654505 scopus 로고
    • Calcium is required for folding of newly-made subunits of the asilaoglycoprotein receptor within the endoplasmic reticulum
    • Lodish H.F., Kong N., Wikström L. Calcium is required for folding of newly-made subunits of the asilaoglycoprotein receptor within the endoplasmic reticulum. J. Biol. Chem. 267:1992;12753-12760.
    • (1992) J. Biol. Chem. , vol.267 , pp. 12753-12760
    • Lodish, H.F.1    Kong, N.2    Wikström, L.3
  • 31
    • 0030456367 scopus 로고    scopus 로고
    • Intermediates in the assembly and degradation of class I major histocompatibility complex (MHC) molecules probed with free heavy chain-specific monoclonal antibodies
    • Machold R.P., Ploegh H.L. Intermediates in the assembly and degradation of class I major histocompatibility complex (MHC) molecules probed with free heavy chain-specific monoclonal antibodies. J. Exp. Med. 184:1996;2251-2259.
    • (1996) J. Exp. Med. , vol.184 , pp. 2251-2259
    • MacHold, R.P.1    Ploegh, H.L.2
  • 32
    • 0031925211 scopus 로고    scopus 로고
    • The role of calnexin in NK-target cell interaction
    • Malyguine A.M., Scott J.E., Dawson J.R. The role of calnexin in NK-target cell interaction. Immunol. Lett. 61:1998;67-71.
    • (1998) Immunol. Lett. , vol.61 , pp. 67-71
    • Malyguine, A.M.1    Scott, J.E.2    Dawson, J.R.3
  • 33
    • 0020804564 scopus 로고
    • Reduced temperature prevents transfer of a membrane glycoprotein to the cell surface but does not prevent terminal glycosylation
    • Matlin K.S., Simons K. Reduced temperature prevents transfer of a membrane glycoprotein to the cell surface but does not prevent terminal glycosylation. Cell. 34:1983;233-243.
    • (1983) Cell , vol.34 , pp. 233-243
    • Matlin, K.S.1    Simons, K.2
  • 35
    • 0033523910 scopus 로고    scopus 로고
    • Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells
    • Molinari M., Helenius A. Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells. Nature. 402:1999;90-93.
    • (1999) Nature , vol.402 , pp. 90-93
    • Molinari, M.1    Helenius, A.2
  • 36
    • 0034646876 scopus 로고    scopus 로고
    • Chaperone selection during glycoprotein translocation into the endoplasmic reticulum
    • Molinari M., Helenius A. Chaperone selection during glycoprotein translocation into the endoplasmic reticulum. Science. 288:2000;331-333.
    • (2000) Science , vol.288 , pp. 331-333
    • Molinari, M.1    Helenius, A.2
  • 37
    • 0037157856 scopus 로고    scopus 로고
    • Sequential assistance of molecular chaperones and transient formation of covalent complexes during protein degradation from the ER
    • Molinari M., Galli C., Piccaluga V., Pieren M., Paganetti P. Sequential assistance of molecular chaperones and transient formation of covalent complexes during protein degradation from the ER. J. Cell Biol. 158:2002;247-257.
    • (2002) J. Cell Biol. , vol.158 , pp. 247-257
    • Molinari, M.1    Galli, C.2    Piccaluga, V.3    Pieren, M.4    Paganetti, P.5
  • 38
    • 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. Role of EDEM in the release of misfolded glycoproteins from the calnexin cycle. Science. 299:2003;1397-1400.
    • (2003) Science , vol.299 , pp. 1397-1400
    • Molinari, M.1    Calanca, V.2    Galli, C.3    Lucca, P.4    Paganetti, P.5
  • 40
    • 0037470515 scopus 로고    scopus 로고
    • EDEM as an acceptor of terminally misfolded glycoproteins released from calnexin
    • Oda Y., Hosokawa N., Wada I., Nagata K. EDEM as an acceptor of terminally misfolded glycoproteins released from calnexin. Science. 299:2003;1394-1397.
    • (2003) Science , vol.299 , pp. 1394-1397
    • Oda, Y.1    Hosokawa, N.2    Wada, I.3    Nagata, K.4
  • 41
    • 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. ERp57 functions as a subunit of specific complexes formed with the ER lectins calreticulin and calnexin. Mol. Biol. Cell. 10:1999;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
  • 42
    • 0030053103 scopus 로고    scopus 로고
    • Calreticulin interacts with newly synthesized human immunodeficiency virus type I envelope glycoprotein, suggesting a chaperone function similar to that of calnexin
    • Otteken A., Moss B. Calreticulin interacts with newly synthesized human immunodeficiency virus type I envelope glycoprotein, suggesting a chaperone function similar to that of calnexin. J. Biol. Chem. 271:1996;97-103.
    • (1996) J. Biol. Chem. , vol.271 , pp. 97-103
    • Otteken, A.1    Moss, B.2
  • 43
    • 0031895637 scopus 로고    scopus 로고
    • Mechanisms of MHC class I-restricted antigen processing
    • Pamer E., Cresswell P. Mechanisms of MHC class I-restricted antigen processing. Annu. Rev. Immunol. 16:1998;323-358.
    • (1998) Annu. Rev. Immunol. , vol.16 , pp. 323-358
    • Pamer, E.1    Cresswell, P.2
  • 44
    • 0033782777 scopus 로고    scopus 로고
    • Protein glucosylation and its role in protein folding
    • Parodi A.J. Protein glucosylation and its role in protein folding. Annu. Rev. Biochem. 69:2000;69-93.
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 69-93
    • Parodi, A.J.1
  • 45
    • 0029160540 scopus 로고
    • Transient, lectin-like association of calreticulin with folding intermediates of cellular and viral glycoproteins
    • Peterson J.R., Ora A., Van P.N., Helenius A. Transient, lectin-like association of calreticulin with folding intermediates of cellular and viral glycoproteins. Mol. Biol. Cell. 6:1995;1173-1184.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1173-1184
    • Peterson, J.R.1    Ora, A.2    Van, P.N.3    Helenius, A.4
  • 46
    • 0032478644 scopus 로고    scopus 로고
    • Differential interaction of coagulation factor VIII and factor V with protein chaperones calnexin and calreticulin
    • Pipe S.W., Morris J.A., Shah J., Kaufman R.J. Differential interaction of coagulation factor VIII and factor V with protein chaperones calnexin and calreticulin. J. Biol. Chem. 273:1998;8537-8544.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8537-8544
    • Pipe, S.W.1    Morris, J.A.2    Shah, J.3    Kaufman, R.J.4
  • 48
    • 0030217926 scopus 로고    scopus 로고
    • Roles for calreticulin and a novel glycoprotein, tapasin, in the interaction of MHC class I molecules with TAP
    • Sadasivan B., Lehner P.J., Ortmann B., Spies T., Cresswell P. Roles for calreticulin and a novel glycoprotein, tapasin, in the interaction of MHC class I molecules with TAP. Immunity. 5:1996;103-114.
    • (1996) Immunity , vol.5 , pp. 103-114
    • Sadasivan, B.1    Lehner, P.J.2    Ortmann, B.3    Spies, T.4    Cresswell, P.5
  • 49
    • 0025917331 scopus 로고
    • Stage-specific assays for coated pit formation and coated vesicle budding in vitro
    • Schmid S.L., Smythe E. Stage-specific assays for coated pit formation and coated vesicle budding in vitro. J. Cell Biol. 114:1991;869-880.
    • (1991) J. Cell Biol. , vol.114 , pp. 869-880
    • Schmid, S.L.1    Smythe, E.2
  • 51
    • 0029009565 scopus 로고
    • MHC class I expression and transport in a calnexin-deficient cell line
    • Scott J.E., Dawson J.R. MHC class I expression and transport in a calnexin-deficient cell line. J. Immunol. 155:1995;143-148.
    • (1995) J. Immunol. , vol.155 , pp. 143-148
    • Scott, J.E.1    Dawson, J.R.2
  • 52
    • 15844386822 scopus 로고    scopus 로고
    • Definition of the lectin-like properties of the molecular chaperone, calreticulin, and demonstration of its copurification with endomannosidase from rat liver Golgi
    • Spiro R.G., Zhu Q., Bhoyroo V., Soling H.D. Definition of the lectin-like properties of the molecular chaperone, calreticulin, and demonstration of its copurification with endomannosidase from rat liver Golgi. J. Biol. Chem. 271:1996;11588-11594.
    • (1996) J. Biol. Chem. , vol.271 , pp. 11588-11594
    • Spiro, R.G.1    Zhu, Q.2    Bhoyroo, V.3    Soling, H.D.4
  • 53
    • 0027174340 scopus 로고
    • Membrane glycoprotein folding, oligomerization and intracellular transport: Effects of dithiothreitol in living cells
    • Tatu U., Braakman I., Helenius A. Membrane glycoprotein folding, oligomerization and intracellular transport. effects of dithiothreitol in living cells EMBO J. 12:1993;2151-2157.
    • (1993) EMBO J. , vol.12 , pp. 2151-2157
    • Tatu, U.1    Braakman, I.2    Helenius, A.3
  • 54
    • 0028906029 scopus 로고
    • Folding and oligomerization of influenza hemagglutinin in the ER and the intermediate compartment
    • Tatu U., Hammond C., Helenius A. Folding and oligomerization of influenza hemagglutinin in the ER and the intermediate compartment. EMBO J. 14:1995;1340-1348.
    • (1995) EMBO J. , vol.14 , pp. 1340-1348
    • Tatu, U.1    Hammond, C.2    Helenius, A.3
  • 55
    • 0030467255 scopus 로고    scopus 로고
    • Deglucosylation of N-linked glycans is an important step in the dissociation of calreticulin-class I-TAP complexes
    • van Leeuwen J.E., Kearse K.P. Deglucosylation of N-linked glycans is an important step in the dissociation of calreticulin-class I-TAP complexes. Proc. Natl. Acad. Sci. USA. 93:1996;13997-14001.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 13997-14001
    • Van Leeuwen, J.E.1    Kearse, K.P.2
  • 56
    • 0029794718 scopus 로고    scopus 로고
    • The related molecular chaperones calnexin and calreticulin differentially associate with nascent T cell antigen receptor proteins within the endoplasmic reticulum
    • Van Leeuwen J.E.M., Kearse K.P. The related molecular chaperones calnexin and calreticulin differentially associate with nascent T cell antigen receptor proteins within the endoplasmic reticulum. J. Biol. Chem. 271:1996;25345-25349.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25345-25349
    • Van Leeuwen, J.E.M.1    Kearse, K.P.2
  • 57
    • 0028932360 scopus 로고
    • The molecular chaperone calnexin binds Glc1Man9GlcNAc2 oligosaccharide as an initial step in recognizing unfolded glycoproteins
    • Ware F.E., Vassilakos A., Peterson P.A., Jackson M.R., Lehrman M.A., Williams D.B. The molecular chaperone calnexin binds Glc1Man9GlcNAc2 oligosaccharide as an initial step in recognizing unfolded glycoproteins. J. Biol. Chem. 270:1995;4697-4704.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4697-4704
    • Ware, F.E.1    Vassilakos, A.2    Peterson, P.A.3    Jackson, M.R.4    Lehrman, M.A.5    Williams, D.B.6
  • 58
    • 0032513212 scopus 로고    scopus 로고
    • Enhanced catalysis of ribonuclease B folding by the interaction of calnexin or calreticulin with ERp57
    • Zapun A., Darby N.J., Tessier D.C., Michalak M., Bergeron J.J., Thomas D.Y. Enhanced catalysis of ribonuclease B folding by the interaction of calnexin or calreticulin with ERp57. J. Biol. Chem. 273:1998;6009-6012.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6009-6012
    • Zapun, A.1    Darby, N.J.2    Tessier, D.C.3    Michalak, M.4    Bergeron, J.J.5    Thomas, D.Y.6
  • 59
    • 0030881717 scopus 로고    scopus 로고
    • Quality control in the secretory pathway: The role of calreticulin, calnexin and BiP in the retention of glycoproteins with C-terminal truncations
    • Zhang J.X., Braakman I., Matlack K.E., Helenius A. Quality control in the secretory pathway. the role of calreticulin, calnexin and BiP in the retention of glycoproteins with C-terminal truncations Mol. Biol. Cell. 8:1997;1943-1954.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1943-1954
    • Zhang, J.X.1    Braakman, I.2    Matlack, K.E.3    Helenius, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.