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Volumn 3, Issue 11, 2002, Pages 833-849

The transitional ER defines a boundary for quality control in the secretion of tsO45 VSV glycoprotein

Author keywords

ER exit sites; Golgi complex; Molecular chaperones; Protein folding; Secretory pathway

Indexed keywords

CALNEXIN; CHAPERONE; TRANSITION ELEMENT; VIRUS GLYCOPROTEIN; BREFELDIN A; GREEN FLUORESCENT PROTEIN; MEMBRANE PROTEIN; NUCLEOPORIN; PHOTOPROTEIN; PROTEIN SYNTHESIS INHIBITOR; RECOMBINANT PROTEIN; SACCHAROMYCES CEREVISIAE PROTEIN; SEC13 PROTEIN, S CEREVISIAE; VIRUS ENVELOPE PROTEIN;

EID: 0036843919     PISSN: 13989219     EISSN: None     Source Type: Journal    
DOI: 10.1034/j.1600-0854.2002.31108.x     Document Type: Article
Times cited : (71)

References (69)
  • 1
    • 0024461745 scopus 로고
    • Protein oligomerization in the endoplasmic reticulum
    • Hurtley SM, Helenius A. Protein oligomerization in the endoplasmic reticulum. Annu Rev Cell Biol 1989;5:277-307.
    • (1989) Annu. Rev. Cell Biol , vol.5 , pp. 277-307
    • Hurtley, S.M.1    Helenius, A.2
  • 2
    • 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 1999;286:1882-1888.
    • (1999) Science , vol.286 , pp. 1882-1888
    • Ellgaard, L.1    Molinari, M.2    Helenius, A.3
  • 3
    • 0025041029 scopus 로고
    • Protein degradation in the endoplasmic reticulum
    • Klausner RD, Sitia R. Protein degradation in the endoplasmic reticulum. Cell 1990;62:611-614.
    • (1990) Cell , vol.62 , pp. 611-614
    • Klausner, R.D.1    Sitia, R.2
  • 4
    • 0030949874 scopus 로고    scopus 로고
    • ER quality control: The cytoplasmic connection
    • Kopito RR. ER quality control: the cytoplasmic connection. Cell 1997;88:427-430.
    • (1997) Cell , vol.88 , pp. 427-430
    • Kopito, R.R.1
  • 5
    • 0016785996 scopus 로고
    • Intracellular aspects of the process of protein synthesis
    • Palade GE. Intracellular aspects of the process of protein synthesis. Science 1975;189:347-358.
    • (1975) Science , vol.189 , pp. 347-358
    • Palade, G.E.1
  • 6
    • 0027580922 scopus 로고
    • Protein trafficking along the exocytotic pathway
    • Hong W, Tang BL. Protein trafficking along the exocytotic pathway. Bioessays 1993;15:231-238.
    • (1993) Bioessays , vol.15 , pp. 231-238
    • Hong, W.1    Tang, B.L.2
  • 7
    • 0034493602 scopus 로고    scopus 로고
    • Dynamics of transitional endoplasmic reticulum sites in vertebrate cells
    • Hammond AT, Glick BS. Dynamics of transitional endoplasmic reticulum sites in vertebrate cells. Mol Biol Cell 2000;11:3013-3030.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3013-3030
    • Hammond, A.T.1    Glick, B.S.2
  • 8
    • 0021148465 scopus 로고
    • Pre- and post-Golgi vacuoles operate in the transport of Semliki forest virus glycoproteins to the cell surface
    • Saraste J, Kuismanen E. Pre- and post-Golgi vacuoles operate in the transport of Semliki forest virus glycoproteins to the cell surface. Cell 1984;38:535-549.
    • (1984) Cell , vol.38 , pp. 535-549
    • Saraste, J.1    Kuismanen, E.2
  • 9
    • 0025610518 scopus 로고
    • Identification of an intermediate compartment involved in protein transport from endoplasmic reticulum to Golgi apparatus
    • Schweizer A, Fransen JAM, Matter K, Kreis TE, Ginsel L, Hauri H-P. Identification of an intermediate compartment involved in protein transport from endoplasmic reticulum to Golgi apparatus. Eur J Cell Biol 1990;53:185-196.
    • (1990) Eur. J. Cell Biol , vol.53 , pp. 185-196
    • Schweizer, A.1    Fransen, J.A.M.2    Matter, K.3    Kreis, T.E.4    Ginsel, L.5    Hauri, H.-P.6
  • 10
    • 0030742746 scopus 로고    scopus 로고
    • Membrane dynamics at the endoplasmic reticulum-Golgi interface
    • Bannykh SI, Balch WE. Membrane dynamics at the endoplasmic reticulum-Golgi interface. J Cell Biol 1997;138:1-4.
    • (1997) J. Cell Biol , vol.138 , pp. 1-4
    • Bannykh, S.I.1    Balch, W.E.2
  • 11
    • 0033938963 scopus 로고    scopus 로고
    • Transport between ER and Golgi
    • Klumperman J. Transport between ER and Golgi. Curr Opin Cell Biol 2000;12:445-449.
    • (2000) Curr. Opin. Cell Biol , vol.12 , pp. 445-449
    • Klumperman, J.1
  • 12
    • 0016287992 scopus 로고
    • Envelope proteins of vesicular stomatitis virus: Effect of temperature-sensitive mutations in complementation groups III and V
    • Lafay F. Envelope proteins of vesicular stomatitis virus: effect of temperature-sensitive mutations in complementation groups III and V. J Virol 1974;14:1220-1228.
    • (1974) J. Virol , vol.14 , pp. 1220-1228
    • Lafay, F.1
  • 13
    • 0020698846 scopus 로고
    • Nucleotide sequence of a cDNA clone encoding the entire glycoprotein from the New Jersey serotype of vesicular stomatitis virus
    • Gallione CJ, Rose JK. Nucleotide sequence of a cDNA clone encoding the entire glycoprotein from the New Jersey serotype of vesicular stomatitis virus. J Virol 1983;46:162-169.
    • (1983) J. Virol , vol.46 , pp. 162-169
    • Gallione, C.J.1    Rose, J.K.2
  • 14
    • 0024822838 scopus 로고
    • Using temperature-sensitive mutants of VSV to study membrane protein biogenesis
    • Bergmann JE. Using temperature-sensitive mutants of VSV to study membrane protein biogenesis. Meth Cell Biol 1989;32:85-110.
    • (1989) Meth. Cell Biol , vol.32 , pp. 85-110
    • Bergmann, J.E.1
  • 15
    • 0025210448 scopus 로고
    • Heavy chain binding protein recognizes incompletely disulfide-bonded forms of vesicular stomatitis virus G protein
    • Machamer CE, Doms RW, Bole DG, Helenius A, Rose JK. Heavy chain binding protein recognizes incompletely disulfide-bonded forms of vesicular stomatitis virus G protein. J Biol Chem 1990;265:6879-6883.
    • (1990) J. Biol. Chem , vol.265 , pp. 6879-6883
    • Machamer, C.E.1    Doms, R.W.2    Bole, D.G.3    Helenius, A.4    Rose, J.K.5
  • 16
    • 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. Posttranslational folding of vesicular stomatitis virus G protein in the ER: involvement of noncovalent and covalent complexes. J Cell Biol 1993;120:647-655.
    • (1993) J. Cell Biol , vol.120 , pp. 647-655
    • de Silva, A.1    Braakman, I.2    Helenius, A.3
  • 17
    • 0028076031 scopus 로고
    • Folding of VSVG protein sequential interaction with BiP and calnexin
    • Hammond C, Helenius A. Folding of VSVG protein sequential interaction with BiP and calnexin. Science 1994;266:456-458.
    • (1994) Science , vol.266 , pp. 456-458
    • Hammond, C.1    Helenius, A.2
  • 18
    • 0022834188 scopus 로고
    • ATP-coupled transport of vesicular stomatitis virus G protein. Functional boundaries of secretory compartments
    • Balch WE, Keller DS. ATP-coupled transport of vesicular stomatitis virus G protein. Functional boundaries of secretory compartments. J Biol Chem 1986;261:14690-14696.
    • (1986) J. Biol. Chem , vol.261 , pp. 14690-14696
    • Balch, W.E.1    Keller, D.S.2
  • 19
    • 0023550869 scopus 로고
    • Role for adenosine triphosphate in regulating the assembly and transport of vesicular stomatitis virus G protein trimers
    • Doms RW, Keller DS, Helenius A, Balch WE. Role for adenosine triphosphate in regulating the assembly and transport of vesicular stomatitis virus G protein trimers. J Cell Biol 1987;105:1957-1969.
    • (1987) J. Cell Biol , vol.105 , pp. 1957-1969
    • Doms, R.W.1    Keller, D.S.2    Helenius, A.3    Balch, W.E.4
  • 20
    • 23444432144 scopus 로고
    • Vesicular stomatitis virus glycoprotein is sorted and concentrated during export from the endoplasmic reticulum
    • Balch WE, McCaffery JM, Plutner H, Farquhar MG. Vesicular stomatitis virus glycoprotein is sorted and concentrated during export from the endoplasmic reticulum. Cell 1994;76:841-852.
    • (1994) Cell , vol.76 , pp. 841-852
    • Balch, W.E.1    McCaffery, J.M.2    Plutner, H.3    Farquhar, M.G.4
  • 22
    • 0021795178 scopus 로고
    • A single amino acid substitution in a hydrophobic domain causes temperature-sensitive cell-surface transport of a mutant viral glycoprotein
    • Gallione CJ, Rose JK. A single amino acid substitution in a hydrophobic domain causes temperature-sensitive cell-surface transport of a mutant viral glycoprotein. J Virol 1985;54:374-382.
    • (1985) J. Virol , vol.54 , pp. 374-382
    • Gallione, C.J.1    Rose, J.K.2
  • 24
    • 0030813162 scopus 로고    scopus 로고
    • Insights into secretory and endocytic membrane traffic using green fluorescent protein chimeras
    • Lippincott-Schwartz J, Smith CL. Insights into secretory and endocytic membrane traffic using green fluorescent protein chimeras. Curr Opin Neurobiol 1997;7:631-639.
    • (1997) Curr. Opin. Neurobiol , vol.7 , pp. 631-639
    • Lippincott-Schwartz, J.1    Smith, C.L.2
  • 25
    • 15844379984 scopus 로고    scopus 로고
    • Glycan-dependent and -independent association of vesicular stomatitis virus G protein with calnexin
    • Cannon KS, Hebert DN, Helenius A. Glycan-dependent and -independent association of vesicular stomatitis virus G protein with calnexin. J Biol Chem 1996;271:14280-14284.
    • (1996) J. Biol. Chem , vol.271 , pp. 14280-14284
    • Cannon, K.S.1    Hebert, D.N.2    Helenius, A.3
  • 26
    • 0024598083 scopus 로고
    • Selective retention of monoglucosylated high mannose oligosaccharides by a class of mutant vesicular stomatitis virus G proteins
    • Suh K, Bergmann JE, Gabel CA. Selective retention of monoglucosylated high mannose oligosaccharides by a class of mutant vesicular stomatitis virus G proteins. J Cell Biol 1989;108:811-819.
    • (1989) J. Cell Biol , vol.108 , pp. 811-819
    • Suh, K.1    Bergmann, J.E.2    Gabel, C.A.3
  • 27
    • 0033782777 scopus 로고    scopus 로고
    • Protein glucosylation and its role in protein folding
    • Parodi A. Protein glucosylation and its role in protein folding. Annu Rev Biochem 2000;69:69-93.
    • (2000) Annu. Rev. Biochem , vol.69 , pp. 69-93
    • Parodi, A.1
  • 28
    • 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 AM, Balch WE, 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 1990;111:857-866.
    • (1990) J. Cell Biol , vol.111 , pp. 857-866
    • de Silva, A.M.1    Balch, W.E.2    Helenius, A.3
  • 29
    • 0028339518 scopus 로고
    • Quality control in the secretory pathway retention of a misfolded viral membrane glycoprotein involves cycling between the ER, intermediate compartment and Golgi apparatus
    • Hammond C, Helenius A. Quality control in the secretory pathway retention of a misfolded viral membrane glycoprotein involves cycling between the ER, intermediate compartment and Golgi apparatus. J Cell Biol 1994;126:41-52.
    • (1994) J. Cell Biol , vol.126 , pp. 41-52
    • Hammond, C.1    Helenius, A.2
  • 30
    • 0033548479 scopus 로고    scopus 로고
    • Trimming and readdition of glucose to N-linked oligosaccharides determines calnexin association of a substrate glycoprotein in living cells
    • Cannon KSI, Helenius A. Trimming and readdition of glucose to N-linked oligosaccharides determines calnexin association of a substrate glycoprotein in living cells. J Biol Chem 1999;274:7537-7544.
    • (1999) J. Biol. Chem , vol.274 , pp. 7537-7544
    • Cannon, K.S.I.1    Helenius, A.2
  • 31
    • 0020804564 scopus 로고
    • Reduced temperature prevents transfer of a membrane glycoprotein to the cell surface but does not prevent terminal glycosylation
    • Matlin KS, Simons K. Reduced temperature prevents transfer of a membrane glycoprotein to the cell surface but does not prevent terminal glycosylation. Cell 1983;34:233-243.
    • (1983) Cell , vol.34 , pp. 233-243
    • Matlin, K.S.1    Simons, K.2
  • 32
    • 0022745592 scopus 로고
    • Temperature and energy dependence of secretory protein transport in the exocrine pancreas
    • Tartakoff AM. Temperature and energy dependence of secretory protein transport in the exocrine pancreas. EMBO J 1986;5:1477-1482.
    • (1986) EMBO J , vol.5 , pp. 1477-1482
    • Tartakoff, A.M.1
  • 33
    • 0030587433 scopus 로고    scopus 로고
    • Morphological analysis of the transfer of VSV ts-045 G glycoprotein from the endoplasmic reticulum to the intermediate compartment in vero cells
    • Lotti LV, Torrisi MR, Erra MC, Bonatti S. Morphological analysis of the transfer of VSV ts-045 G glycoprotein from the endoplasmic reticulum to the intermediate compartment in vero cells. Exp Cell Res 1996;227:323-331.
    • (1996) Exp. Cell Res , vol.227 , pp. 323-331
    • Lotti, L.V.1    Torrisi, M.R.2    Erra, M.C.3    Bonatti, S.4
  • 34
    • 0030928782 scopus 로고    scopus 로고
    • Visualization of ER-to-Golgi transport in living cells reveals a sequential mode of action for COPII and COPI
    • Scales SJ, Pepperkok R, Kreis TE. Visualization of ER-to-Golgi transport in living cells reveals a sequential mode of action for COPII and COPI. Cell 1997;90:1137-1148.
    • (1997) Cell , vol.90 , pp. 1137-1148
    • Scales, S.J.1    Pepperkok, R.2    Kreis, T.E.3
  • 35
    • 0020002482 scopus 로고
    • The interaction of antibody with the major surface glycoprotein of vesicular stomatitis virus. I. Analysis of neutralizing epitopes with monoclonal antibodies
    • Lefrancois L, Lyles DS. The interaction of antibody with the major surface glycoprotein of vesicular stomatitis virus. I. Analysis of neutralizing epitopes with monoclonal antibodies. Virology 1982;121:157-166.
    • (1982) Virology , vol.121 , pp. 157-166
    • Lefrancois, L.1    Lyles, D.S.2
  • 36
    • 0022721628 scopus 로고
    • Microinjected antibodies against the cytoplasmic domain of vesicular stomatitis virus glycoprotein block its transport to the cell surface
    • Kreis TE. Microinjected antibodies against the cytoplasmic domain of vesicular stomatitis virus glycoprotein block its transport to the cell surface. EMBO J 1986;5:931-941.
    • (1986) EMBO J , vol.5 , pp. 931-941
    • Kreis, T.E.1
  • 37
    • 0027455464 scopus 로고
    • Posttranslational folding of vesticular stomatitis Virus G protein in the ER: Involvement of noncovalent and covalent complexes
    • De Silva A, Braakman I, Helenius A. Posttranslational folding of vesticular stomatitis Virus G protein in the ER: Involvement of noncovalent and covalent complexes. J Cell Biol 1993;120:647-655.
    • (1993) J. Cell Biol , vol.120 , pp. 647-655
    • De Silva, A.1    Braakman, I.2    Helenius, A.3
  • 38
    • 0022550932 scopus 로고
    • Oligomerization is essential for transport of vesicular stomatitis viral glycoproteins to the cell surface
    • Kreis TE, Lodish HF. Oligomerization is essential for transport of vesicular stomatitis viral glycoproteins to the cell surface. Cell 1986;46:929-937.
    • (1986) Cell , vol.46 , pp. 929-937
    • Kreis, T.E.1    Lodish, H.F.2
  • 39
    • 0032516855 scopus 로고    scopus 로고
    • COPII and selective export from the endoplasmic reticulum
    • 1404
    • Barlowe C. COPII and selective export from the endoplasmic reticulum. Biochim Biophys Acta 1998;1404:67-76.
    • (1998) Biochim. Biophys. Acta , pp. 67-76
    • Barlowe, C.1
  • 40
    • 0033917563 scopus 로고    scopus 로고
    • COPI-coated ER-to-Golgi transport complexes segregate from COPII in close proximity to ER exit sites
    • Stephens DJ, Lin-Marq N, Pagano A, Pepperkok R, Paccaud JP. COPI-coated ER-to-Golgi transport complexes segregate from COPII in close proximity to ER exit sites. J Cell Sci 2000;113:2177-2185.
    • (2000) J. Cell Sci , vol.113 , pp. 2177-2185
    • Stephens, D.J.1    Lin-Marq, N.2    Pagano, A.3    Pepperkok, R.4    Paccaud, J.P.5
  • 42
    • 0000505092 scopus 로고    scopus 로고
    • The mammalian homolog of yeast Sec13p is enriched in the intermediate compartment and is essential for protein transport from the endoplasmic reticulum to the Golgi apparatus
    • Tang BL, Peter F, Krijnse-Locker J, Low SH, Griffiths G, Hong W. The mammalian homolog of yeast Sec13p is enriched in the intermediate compartment and is essential for protein transport from the endoplasmic reticulum to the Golgi apparatus. Mol Cell Biol 1997;17:256-266.
    • (1997) Mol. Cell Biol , vol.17 , pp. 256-266
    • Tang, B.L.1    Peter, F.2    Krijnse-Locker, J.3    Low, S.H.4    Griffiths, G.5    Hong, W.6
  • 43
    • 0033538549 scopus 로고    scopus 로고
    • Vesicular tubular clusters between the ER and Golgi mediate concentration of soluble secretory proteins by exclusion from COPI-coated vesicles
    • Martinez-Menarguez JA, Geuze HJ, Slot JW, Klumperman J. Vesicular tubular clusters between the ER and Golgi mediate concentration of soluble secretory proteins by exclusion from COPI-coated vesicles. Cell 1999;98:81-90.
    • (1999) Cell , vol.98 , pp. 81-90
    • Martinez-Menarguez, J.A.1    Geuze, H.J.2    Slot, J.W.3    Klumperman, J.4
  • 44
    • 0033574449 scopus 로고    scopus 로고
    • Brefeldin A: The advantage of being uncompetitive
    • Chardin P, McCormick F. Brefeldin A: the advantage of being uncompetitive. Cell 1999;97:153-155.
    • (1999) Cell , vol.97 , pp. 153-155
    • Chardin, P.1    McCormick, F.2
  • 45
    • 0028103695 scopus 로고
    • Role of N-linked oligosaccharides, glucose trimming and calnexin during glycoprotein folding in the endoplasmic reticulum
    • Hammond C, Braakman I, Helenius A. Role of N-linked oligosaccharides, glucose trimming and calnexin during glycoprotein folding in the endoplasmic reticulum. Proc Natl Acad Sci USA 1994;91:913-917.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 913-917
    • Hammond, C.1    Braakman, I.2    Helenius, A.3
  • 46
    • 0026934508 scopus 로고
    • Pathways of protein sorting and membrane traffic between the rough endoplasmic reticulum and the Golgi complex
    • [Review]
    • Saraste J, Kuismanen E. Pathways of protein sorting and membrane traffic between the rough endoplasmic reticulum and the Golgi complex. [Review] Semin Cell Biol 1992;3:343-355.
    • (1992) Semin. Cell Biol , vol.3 , pp. 343-355
    • Saraste, J.1    Kuismanen, E.2
  • 47
  • 49
    • 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 1993;12:2151-2157.
    • (1993) EMBO J , vol.12 , pp. 2151-2157
    • Tatu, U.1    Braakman, I.2    Helenius, A.3
  • 50
    • 0027373802 scopus 로고
    • In vitro unfolding of Retionol-binding protein by Dithiothreitol
    • Kaji EH, Lodish HF. In vitro unfolding of Retionol-binding protein by Dithiothreitol. J Biol Chem 1993;268:22195-22202.
    • (1993) J. Biol. Chem , vol.268 , pp. 22195-22202
    • Kaji, E.H.1    Lodish, H.F.2
  • 51
    • 0035845484 scopus 로고    scopus 로고
    • Immunolocalization of UDP-glucose: Glycoprotein glucosyltransferase indicates involvement of pre-Golgi intermediates in protein quality control
    • Zuber C, Fan JY, Guhl B, Parodi A, Fessler JH, Parker C, Roth J. Immunolocalization of UDP-glucose: glycoprotein glucosyltransferase indicates involvement of pre-Golgi intermediates in protein quality control. Proc Natl Acad Sci USA 2001;98:10710-10715.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 10710-10715
    • Zuber, C.1    Fan, J.Y.2    Guhl, B.3    Parodi, A.4    Fessler, J.H.5    Parker, C.6    Roth, J.7
  • 53
    • 0031786358 scopus 로고    scopus 로고
    • Protein transport from the endoplasmic reticulum to the Golgi apparatus
    • Hong W. Protein transport from the endoplasmic reticulum to the Golgi apparatus. J Cell Sci 1998;111:2831-2839.
    • (1998) J. Cell Sci , vol.111 , pp. 2831-2839
    • Hong, W.1
  • 55
    • 0026777411 scopus 로고
    • Immunocytochemical analysis of the transfer of vesicular stomatitis virus G protein from the intermediate compartment to the Golgi complex
    • Lotti IV, Torrisi M-R, Pascale MC, Bonatti S. Immunocytochemical analysis of the transfer of vesicular stomatitis virus G protein from the intermediate compartment to the Golgi complex. J Cell Biol 1992;118:43-50.
    • (1992) J. Cell Biol , vol.118 , pp. 43-50
    • Lotti, I.V.1    Torrisi, M.-R.2    Pascale, M.C.3    Bonatti, S.4
  • 56
    • 0009355284 scopus 로고
    • Transport of vesicular stomatitis virus glycoprotein in a cell-free extract
    • Fries E, Rothman JE. Transport of vesicular stomatitis virus glycoprotein in a cell-free extract. Proc Natl Acad Sci USA 1980;77:3870-3874.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 3870-3874
    • Fries, E.1    Rothman, J.E.2
  • 58
    • 0029587314 scopus 로고
    • Uncoupled packaging of targeting and cargo molecules during transport vesicle budding from the endoplasmic reticulum
    • Yeung T, Barlowe C, Schekman R. Uncoupled packaging of targeting and cargo molecules during transport vesicle budding from the endoplasmic reticulum. J Biol Chem 1995;270:30567-30570.
    • (1995) J. Biol. Chem , vol.270 , pp. 30567-30570
    • Yeung, T.1    Barlowe, C.2    Schekman, R.3
  • 59
    • 0029163053 scopus 로고
    • Sorting and retrieval between the endoplasmic reticulum and Golgi apparatus
    • Pelham HR. Sorting and retrieval between the endoplasmic reticulum and Golgi apparatus. Curr Opin Cell Biol 1995;7:530-535.
    • (1995) Curr. Opin. Cell Biol , vol.7 , pp. 530-535
    • Pelham, H.R.1
  • 60
    • 0031045007 scopus 로고    scopus 로고
    • Interactions between newly synthesized glycoproteins, calnexin and a network of resident chaperones in the endoplasmic reticulum
    • Tatu U, Helenius A. Interactions between newly synthesized glycoproteins, calnexin and a network of resident chaperones in the endoplasmic reticulum. J Cell Biol 1997;136:555-565.
    • (1997) J. Cell Biol , vol.136 , pp. 555-565
    • Tatu, U.1    Helenius, A.2
  • 61
    • 0030812940 scopus 로고    scopus 로고
    • A di-acidic signal required for selective export from the endoplasmic reticulum
    • Nishimura N, Balch WE. A di-acidic signal required for selective export from the endoplasmic reticulum. Science 1997;277:556-558.
    • (1997) Science , vol.277 , pp. 556-558
    • Nishimura, N.1    Balch, W.E.2
  • 62
    • 0033959784 scopus 로고    scopus 로고
    • Efficient export of the vesicular stomatitis virus G protein from the endoplasmic reticulum requires a signal in the cytoplasmic tail that includes both tyrosine-based and di-acidic motifs
    • Sevier CS, Weisz OA, Davis M, Machamer CE. Efficient export of the vesicular stomatitis virus G protein from the endoplasmic reticulum requires a signal in the cytoplasmic tail that includes both tyrosine-based and di-acidic motifs. Mol Biol Cell 2000;11:13-22.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 13-22
    • Sevier, C.S.1    Weisz, O.A.2    Davis, M.3    Machamer, C.E.4
  • 63
    • 0035875665 scopus 로고    scopus 로고
    • The KDEL receptor mediates a retrieval mechanism that contributes to quality control at the endoplasmic reticulum
    • Yamamoto K, Fujii R, Toyofuku Y, Saito T, Koseki H, Hsu VW, Aoe T. The KDEL receptor mediates a retrieval mechanism that contributes to quality control at the endoplasmic reticulum. EMBO J 2001;20:3082-3091.
    • (2001) EMBO J , vol.20 , pp. 3082-3091
    • Yamamoto, K.1    Fujii, R.2    Toyofuku, Y.3    Saito, T.4    Koseki, H.5    Hsu, V.W.6    Aoe, T.7
  • 64
    • 0035968205 scopus 로고    scopus 로고
    • Degradation of endoplasmic reticulum (ER) quality control substrates requires transport between the ER and Golgi
    • Caldwell SR, Hill KJ, Cooper AA. Degradation of endoplasmic reticulum (ER) quality control substrates requires transport between the ER and Golgi. J Biol Chem 2001;276:23296-23303.
    • (2001) J. Biol. Chem , vol.276 , pp. 23296-23303
    • Caldwell, S.R.1    Hill, K.J.2    Cooper, A.A.3
  • 65
    • 0035851911 scopus 로고    scopus 로고
    • Distinct retrieval and retention mechanisms are required for the quality control of endoplasmic reticulum protein folding
    • Vashist S, Kim W, Belden WJ, Spear ED, Barlowe C, Ng DT. Distinct retrieval and retention mechanisms are required for the quality control of endoplasmic reticulum protein folding. J Cell Biol 2001,155:355-368.
    • (2001) J. Cell. Biol , vol.155 , pp. 355-368
    • Vashist, S.1    Kim, W.2    Belden, W.J.3    Spear, E.D.4    Barlowe, C.5    Ng, D.T.6
  • 66
    • 0034768390 scopus 로고    scopus 로고
    • Release of polymannose oligosaccharides from vesicular stomatitis virus G protein during endoplasmic reticulum-associated degradation
    • Spiro MJ, Spiro RG. Release of polymannose oligosaccharides from vesicular stomatitis virus G protein during endoplasmic reticulum-associated degradation. Glycobiology 2001;11:803-811.
    • (2001) Glycobiology , vol.11 , pp. 803-811
    • Spiro, M.J.1    Spiro, R.G.2
  • 67
    • 0033523910 scopus 로고    scopus 로고
    • Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells
    • [see comments]
    • Molinari M, Helenius A. Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells [see comments]. Nature 1999;402:90-93.
    • (1999) Nature , vol.402 , pp. 90-93
    • Molinari, M.1    Helenius, A.2
  • 68
    • 0016335085 scopus 로고
    • Periodate-lysine-paraformaldehyde fixative. A new fixation for immunoelectron microscopy
    • McLean IW, Nakane PK. Periodate-lysine-paraformaldehyde fixative. A new fixation for immunoelectron microscopy. J Histochem Cytochem 1974;22:1077-1083.
    • (1974) J. Histochem. Cytochem , vol.22 , pp. 1077-1083
    • McLean, I.W.1    Nakane, P.K.2
  • 69
    • 0023424875 scopus 로고
    • Effects of transport inhibitors on the generation and transport of a soluble viral glycoprotein 160
    • Chen SS, Doherty R, O'Rourke EJ, Ariel N, Huang AS. Effects of transport inhibitors on the generation and transport of a soluble viral glycoprotein. Virology 1987;160:482-484.
    • (1987) Virology , pp. 482-484
    • Chen, S.S.1    Doherty, R.2    O'Rourke, E.J.3    Ariel, N.4    Huang, A.S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.